Positive and negative control of helicase recruitment at a bacterial chromosome origin

The mechanisms responsible for helicase loading during the initiation of chromosome replication in bacteria are unclear. Here we report both a positive and a negative mechanism for directing helicase recruitment in the model organism Bacillus subtilis. Systematic mutagenesis of the essential replica...

Celý popis

Uložené v:
Podrobná bibliografia
Vydané v:bioRxiv
Hlavní autori: Winterhalter, Charles, Stevens, Daniel, Fenyk, Stepan, Pelliciari, Simone, Marchand, Elie, Cronin, Nora B, Soultanas, Panos, Costa, Tiago, Ilangovan, Aravindan, Heath, Murray
Médium: Paper
Jazyk:English
Vydavateľské údaje: Cold Spring Harbor Cold Spring Harbor Laboratory Press 16.08.2021
Cold Spring Harbor Laboratory
Vydanie:1.1
Predmet:
ISSN:2692-8205, 2692-8205
On-line prístup:Získať plný text
Tagy: Pridať tag
Žiadne tagy, Buďte prvý, kto otaguje tento záznam!
Abstract The mechanisms responsible for helicase loading during the initiation of chromosome replication in bacteria are unclear. Here we report both a positive and a negative mechanism for directing helicase recruitment in the model organism Bacillus subtilis. Systematic mutagenesis of the essential replication initiation gene dnaD and characterization of DnaD variants revealed protein interfaces required for interacting with the master initiator DnaA and with a specific single-stranded DNA (ssDNA) sequence located in the chromosome origin (DnaD Recognition Element, DRE). We propose that the location of the DRE within the replication origin orchestrates recruitment of helicase to achieve bidirectional DNA replication. We also report that the developmentally expressed repressor of DNA replication initiation, SirA, acts by blocking the interaction of DnaD with DnaA, thereby inhibiting helicase recruitment to the origin. These findings significantly advance our mechanistic understanding of helicase recruitment and regulation during bacterial DNA replication initiation. Because DnaD is essential for the viability of clinically relevant Gram-positive pathogens, DnaD is an attractive target for drug development. Competing Interest Statement The authors have declared no competing interest.
AbstractList The mechanisms responsible for helicase loading during the initiation of chromosome replication in bacteria are unclear. Here we report both a positive and a negative mechanism for directing helicase recruitment in the model organism Bacillus subtilis. Systematic mutagenesis of the essential replication initiation gene dnaD and characterization of DnaD variants revealed protein interfaces required for interacting with the master initiator DnaA and with a specific single-stranded DNA (ssDNA) sequence located in the chromosome origin (DnaD Recognition Element, DRE). We propose that the location of the DRE within the replication origin orchestrates recruitment of helicase to achieve bidirectional DNA replication. We also report that the developmentally expressed repressor of DNA replication initiation, SirA, acts by blocking the interaction of DnaD with DnaA, thereby inhibiting helicase recruitment to the origin. These findings significantly advance our mechanistic understanding of helicase recruitment and regulation during bacterial DNA replication initiation. Because DnaD is essential for the viability of clinically relevant Gram-positive pathogens, DnaD is an attractive target for drug development. Competing Interest Statement The authors have declared no competing interest.
The mechanisms responsible for helicase loading during the initiation of chromosome replication in bacteria are unclear. Here we report both a positive and a negative mechanism for directing helicase recruitment in the model organism Bacillus subtilis. Systematic mutagenesis of the essential replication initiation gene dnaD and characterization of DnaD variants revealed protein interfaces required for interacting with the master initiator DnaA and with a specific single-stranded DNA (ssDNA) sequence located in the chromosome origin (DnaD Recognition Element, “DRE”). We propose that the location of the DRE within the replication origin orchestrates recruitment of helicase to achieve bidirectional DNA replication. We also report that the developmentally expressed repressor of DNA replication initiation, SirA, acts by blocking the interaction of DnaD with DnaA, thereby inhibiting helicase recruitment to the origin. These findings significantly advance our mechanistic understanding of helicase recruitment and regulation during bacterial DNA replication initiation. Because DnaD is essential for the viability of clinically relevant Gram-positive pathogens, DnaD is an attractive target for drug development.
Author Fenyk, Stepan
Soultanas, Panos
Cronin, Nora B
Costa, Tiago
Stevens, Daniel
Winterhalter, Charles
Pelliciari, Simone
Ilangovan, Aravindan
Marchand, Elie
Heath, Murray
Author_xml – sequence: 1
  givenname: Charles
  surname: Winterhalter
  fullname: Winterhalter, Charles
– sequence: 2
  givenname: Daniel
  surname: Stevens
  fullname: Stevens, Daniel
– sequence: 3
  givenname: Stepan
  surname: Fenyk
  fullname: Fenyk, Stepan
– sequence: 4
  givenname: Simone
  surname: Pelliciari
  fullname: Pelliciari, Simone
– sequence: 5
  givenname: Elie
  surname: Marchand
  fullname: Marchand, Elie
– sequence: 6
  givenname: Nora
  surname: Cronin
  middlename: B
  fullname: Cronin, Nora B
– sequence: 7
  givenname: Panos
  surname: Soultanas
  fullname: Soultanas, Panos
– sequence: 8
  givenname: Tiago
  surname: Costa
  fullname: Costa, Tiago
– sequence: 9
  givenname: Aravindan
  surname: Ilangovan
  fullname: Ilangovan, Aravindan
– sequence: 10
  givenname: Murray
  surname: Heath
  fullname: Heath, Murray
BookMark eNpNkE1LAzEQhoNUsNb-AG8BL152nWSz2fQoxS8o6EG9hnxtm7Kb1GRb9N-7Wg_CwDsvPAzDc44mIQaH0CWBkhAgNxQoKUGUhJes5oyLEzSlfEELQaGe_NvP0DznLQDQBSdVw6bo_SVmP_iDwypYHNxa_RYTw5Bih2OLN67zRmWHkzNp74fehQGrcbBWZnDJqw6bTYp9zLF3OCa_9uECnbaqy27-lzP0dn_3unwsVs8PT8vbVaEJMFE4VhltGGuVbq0G2gpnLQgDoqFWU1FrK7Q2TmswtCZgDWGEN4q0fIR1W83Q9fGu9jF9-oPcJd-r9CV_lEgQknB5VDKiV0d0l-LH3uVBbuM-hfE7SWtOuGgq3lTfJuFkNw
ContentType Paper
Copyright 2021. This article is published under http://creativecommons.org/licenses/by/4.0/ (“the License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
2021, Posted by Cold Spring Harbor Laboratory
Copyright_xml – notice: 2021. This article is published under http://creativecommons.org/licenses/by/4.0/ (“the License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
– notice: 2021, Posted by Cold Spring Harbor Laboratory
DBID 8FE
8FH
ABUWG
AFKRA
AZQEC
BBNVY
BENPR
BHPHI
CCPQU
DWQXO
GNUQQ
HCIFZ
LK8
M7P
PHGZM
PHGZT
PIMPY
PKEHL
PQEST
PQGLB
PQQKQ
PQUKI
PRINS
FX.
DOI 10.1101/2021.08.16.456468
DatabaseName ProQuest SciTech Collection
ProQuest Natural Science Collection
ProQuest Central (Alumni)
ProQuest Central UK/Ireland
ProQuest Central Essentials
Biological Science Collection
ProQuest Central
ProQuest Natural Science Collection
ProQuest One Community College
ProQuest Central
ProQuest Central Student
SciTech Premium Collection
Biological Sciences
Biological Science Database
ProQuest Central Premium
ProQuest One Academic (New)
Publicly Available Content Database
ProQuest One Academic Middle East (New)
ProQuest One Academic Eastern Edition (DO NOT USE)
ProQuest One Applied & Life Sciences
ProQuest One Academic (retired)
ProQuest One Academic UKI Edition
ProQuest Central China
bioRxiv
DatabaseTitle Publicly Available Content Database
ProQuest Central Student
ProQuest One Academic Middle East (New)
ProQuest Biological Science Collection
ProQuest Central Essentials
ProQuest One Academic Eastern Edition
ProQuest Central (Alumni Edition)
SciTech Premium Collection
ProQuest One Community College
ProQuest Natural Science Collection
Biological Science Database
ProQuest SciTech Collection
ProQuest Central China
ProQuest Central
ProQuest One Applied & Life Sciences
ProQuest One Academic UKI Edition
Natural Science Collection
ProQuest Central Korea
Biological Science Collection
ProQuest Central (New)
ProQuest One Academic
ProQuest One Academic (New)
DatabaseTitleList Publicly Available Content Database

Database_xml – sequence: 1
  dbid: PIMPY
  name: Publicly Available Content Database
  url: http://search.proquest.com/publiccontent
  sourceTypes: Aggregation Database
DeliveryMethod fulltext_linktorsrc
Discipline Biology
EISSN 2692-8205
Edition 1.1
ExternalDocumentID 2021.08.16.456468v1
Genre Working Paper/Pre-Print
GroupedDBID 8FE
8FH
ABUWG
AFKRA
ALMA_UNASSIGNED_HOLDINGS
AZQEC
BBNVY
BENPR
BHPHI
CCPQU
DWQXO
GNUQQ
HCIFZ
LK8
M7P
NQS
PHGZM
PHGZT
PIMPY
PKEHL
PQEST
PQGLB
PQQKQ
PQUKI
PRINS
PROAC
RHI
FX.
ID FETCH-LOGICAL-b1048-e43cbc44fabfdb02f8edd08c0872db285bd8bbcebb0c2510dc14167a1f602fbf3
IEDL.DBID M7P
ISSN 2692-8205
IngestDate Tue Jan 07 18:58:44 EST 2025
Fri Jul 25 09:18:20 EDT 2025
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed false
IsScholarly false
Keywords replication
SirA
initiation
DNA
origin
DnaA
helicase
DnaD
Language English
License This pre-print is available under a Creative Commons License (Attribution 4.0 International), CC BY 4.0, as described at http://creativecommons.org/licenses/by/4.0
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-b1048-e43cbc44fabfdb02f8edd08c0872db285bd8bbcebb0c2510dc14167a1f602fbf3
Notes SourceType-Working Papers-1
ObjectType-Working Paper/Pre-Print-1
content type line 50
Competing Interest Statement: The authors have declared no competing interest.
OpenAccessLink https://www.proquest.com/docview/2561687367?pq-origsite=%requestingapplication%
PQID 2561687367
PQPubID 2050091
PageCount 54
ParticipantIDs biorxiv_primary_2021_08_16_456468
proquest_journals_2561687367
PublicationCentury 2000
PublicationDate 20210816
PublicationDateYYYYMMDD 2021-08-16
PublicationDate_xml – month: 08
  year: 2021
  text: 20210816
  day: 16
PublicationDecade 2020
PublicationPlace Cold Spring Harbor
PublicationPlace_xml – name: Cold Spring Harbor
PublicationTitle bioRxiv
PublicationYear 2021
Publisher Cold Spring Harbor Laboratory Press
Cold Spring Harbor Laboratory
Publisher_xml – name: Cold Spring Harbor Laboratory Press
– name: Cold Spring Harbor Laboratory
References Bleichert, Botchan, Berger (2021.08.16.456468v1.4) 2017; 355
Ticau, Friedman, Ivica, Gelles, Bell (2021.08.16.456468v1.77) 2015; 161
Erzberger, Mott, Berger (2021.08.16.456468v1.18) 2006; 13
Wang, Montero Llopis, Rudner (2021.08.16.456468v1.81) 2014
Kobayashi, Ehrlich, Albertini, Amati, Andersen, Arnaud, Asai, Ashikaga, Aymerich, Bessieres (2021.08.16.456468v1.39) 2003; 100
Krause, Messer (2021.08.16.456468v1.43) 1999; 228
van Eijk, Wittekoek, Kuijper, Smits (2021.08.16.456468v1.79) 2017; 72
Bruand, Velten, McGovern, Marsin, Serena, Ehrlich, Polard (2021.08.16.456468v1.8) 2005; 55
Duderstadt, Chuang, Berger (2021.08.16.456468v1.15) 2011; 478
Ishikawa, Ogura, Yoshimura, Okumura, Cho, Kawai, Kurokawa, Oshima, Ogasawara (2021.08.16.456468v1.30) 2007; 14
Boonstra, de Jong, Scholefield, Murray, Kuipers, Veening (2021.08.16.456468v1.5) 2013; 87
Keyamura, Fujikawa, Ishida, Ozaki, Su’etsugu, Fujimitsu, Kagawa, Yokoyama, Kurumizaka, Katayama (2021.08.16.456468v1.36) 2007; 21
Liebschner, Afonine, Baker, Bunkoczi, Chen, Croll, Hintze, Hung, Jain, McCoy (2021.08.16.456468v1.45) 2019; 75
Rahn-Lee, Gorbatyuk, Skovgaard, Losick (2021.08.16.456468v1.61) 2009; 191
Richardson, Stevens, Pelliciari, Harran, Sperlea, Murray (2021.08.16.456468v1.64) 2019; 38
Weigel, Schmidt, Seitz, Tungler, Welzeck, Messer (2021.08.16.456468v1.83) 1999; 34
Huang, Lien, Huang, Huang (2021.08.16.456468v1.28) 2016; 11
Kohler, Marahiel (2021.08.16.456468v1.41) 1997; 179
Smits, Merrikh, Bonilla, Grossman (2021.08.16.456468v1.75) 2011; 193
Carneiro, Zhang, Ioannou, Scott, Allen, Roberts, Soultanas (2021.08.16.456468v1.9) 2006; 60
Noguchi, Katayama (2021.08.16.456468v1.55) 2016; 7
Fuller, Funnell, Kornberg (2021.08.16.456468v1.24) 1984; 38
Rokop, Grossman (2021.08.16.456468v1.67) 2009; 4
Ozaki, Kawakami, Nakamura, Fujikawa, Kagawa, Park, Yokoyama, Kurumizaka, Katayama (2021.08.16.456468v1.57) 2008; 283
Pelliciari, Dong, Gao, Murray (2021.08.16.456468v1.58) 2021; 49
Abe, Jo, Matsuda, Matsunaga, Katayama, Ueda (2021.08.16.456468v1.1) 2007; 282
Sutton, Carr, Vicente, Kaguni (2021.08.16.456468v1.76) 1998; 273
Jaworski, Zyla-Uklejewicz, Nowaczyk-Cieszewska, Donczew, Mielke, Weigel, Zawilak-Pawlik (2021.08.16.456468v1.32) 2021; 22
Kogoma, von Meyenburg (2021.08.16.456468v1.40) 1983; 2
Kowalski, Eddy (2021.08.16.456468v1.42) 1989; 8
Smits, Goranov, Grossman (2021.08.16.456468v1.74) 2010; 75
Hood, Berger (2021.08.16.456468v1.27) 2016; 5
Schaper, Messer (2021.08.16.456468v1.69) 1997; 28
Tinevez, Perry, Schindelin, Hoopes, Reynolds, Laplantine, Bednarek, Shorte, Eliceiri (2021.08.16.456468v1.78) 2017; 115
Bell, Kaguni (2021.08.16.456468v1.3) 2013; 5
Schindelin, Arganda-Carreras, Frise, Kaynig, Longair, Pietzsch, Preibisch, Rueden, Saalfeld, Schmid (2021.08.16.456468v1.70) 2012; 9
Messer, Blaesing, Majka, Nardmann, Schaper, Schmidt, Seitz, Speck, Tungler, Wegrzyn (2021.08.16.456468v1.50) 1999; 81
Erzberger, Pirruccello, Berger (2021.08.16.456468v1.19) 2002; 21
Fang, Davey, O’Donnell (2021.08.16.456468v1.20) 1999; 4
Wagner, Marquis, Rudner (2021.08.16.456468v1.80) 2009; 73
Briggs, Smits, Soultanas (2021.08.16.456468v1.6) 2012; 194
Weigel, Seitz (2021.08.16.456468v1.84) 2002; 46
Krause, Ruckert, Lurz, Messer (2021.08.16.456468v1.44) 1997; 274
Natrajan, Noirot-Gros, Zawilak-Pawlik, Kapp, Terradot (2021.08.16.456468v1.54) 2009; 106
Schumacher, Tonthat, Kwong, Chinnam, Liu, Skurray, Firth (2021.08.16.456468v1.72) 2014; 111
Seitz, Weigel, Messer (2021.08.16.456468v1.73) 2000; 37
Hagel (2021.08.16.456468v1.25) 2001; 19
Klein, Lanka, Schuster (2021.08.16.456468v1.38) 1980; 105
Andrup, Atlung, Ogasawara, Yoshikawa, Hansen (2021.08.16.456468v1.2) 1988; 170
Fisher, Pastrana, Higman, Koh, Taylor, Butterer, Craggs, Sobott, Murray, Crump (2021.08.16.456468v1.22) 2017; 6
Marston, Grainger, Smits, Hopcroft, Green, Hounslow, Grossman, Craven, Soultanas (2021.08.16.456468v1.47) 2010; 38
Zhang, Allen, Roberts, Soultanas (2021.08.16.456468v1.86) 2006; 188
Rohou, Grigorieff (2021.08.16.456468v1.66) 2015; 192
Roth, Messer (2021.08.16.456468v1.68) 1995; 14
Chaudhuri, Allen, Owen, Shalom, Stone, Harrison, Burgis, Lockyer, Garcia-Lara, Foster (2021.08.16.456468v1.10) 2009; 10
Rahn-Lee, Merrikh, Grossman, Losick (2021.08.16.456468v1.62) 2011; 193
Kaguni (2021.08.16.456468v1.33) 2018; 7
Zhang, Machon, Orta, Phillips, Roberts, Allen, Soultanas (2021.08.16.456468v1.88) 2008; 377
Collier, Machon, Briggs, Smits, Soultanas (2021.08.16.456468v1.13) 2012; 40
Errington (2021.08.16.456468v1.17) 2003; 1
Keyamura, Abe, Higashi, Ueda, Katayama (2021.08.16.456468v1.35) 2009; 284
Fujikawa, Kurumizaka, Nureki, Terada, Shirouzu, Katayama, Yokoyama (2021.08.16.456468v1.23) 2003; 31
Matthews, Simmons (2021.08.16.456468v1.49) 2018; 111
Chodavarapu, Gomez, Vicente, Kaguni (2021.08.16.456468v1.12) 2008b; 67
Hassan, Moriya, Ogura, Tanaka, Kawamura, Ogasawara (2021.08.16.456468v1.26) 1997; 179
Fawcett, Eichenberger, Losick, Youngman (2021.08.16.456468v1.21) 2000; 97
Moerke (2021.08.16.456468v1.52) 2009; 1
Chodavarapu, Felczak, Yaniv, Kaguni (2021.08.16.456468v1.11) 2008a; 67
Mott, Erzberger, Coons, Berger (2021.08.16.456468v1.53) 2008; 135
Imai, Ogasawara, Ishigo-Oka, Kadoya, Daito, Moriya (2021.08.16.456468v1.29) 2000; 36
Zhang, Carneiro, Turner, Allen, Roberts, Soultanas (2021.08.16.456468v1.87) 2005; 351
Zheng, Palovcak, Armache, Verba, Cheng, Agard (2021.08.16.456468v1.89) 2017; 14
Webb, Teleman, Gordon, Straight, Belmont, Lin, Grossman, Wright, Losick (2021.08.16.456468v1.82) 1997; 88
Kimura, Amaya, Kobayashi, Ogasawara, Sato (2021.08.16.456468v1.37) 2010; 192
Pettersen, Goddard, Huang, Couch, Greenblatt, Meng, Ferrin (2021.08.16.456468v1.59) 2004; 25
Jameson, Rostami, Fogg, Turkenburg, Grahl, Murray, Wilkinson (2021.08.16.456468v1.31) 2014; 93
Schneider, Zhang, Soultanas, Paoli (2021.08.16.456468v1.71) 2008; 376
Odegrip, Schoen, Haggard-Ljungquist, Park, Chattoraj (2021.08.16.456468v1.56) 2000; 74
Emsley, Cowtan (2021.08.16.456468v1.16) 2004; 60
Karimova, Pidoux, Ullmann, Ladant (2021.08.16.456468v1.34) 1998; 95
Wyatt (2021.08.16.456468v1.85) 1993; 272
Coster, Diffley (2021.08.16.456468v1.14) 2017; 357
Liu, Gallay, Kjos, Domenech, Slager, van Kessel, Knoops, Sorg, Zhang, Veening (2021.08.16.456468v1.46) 2017; 13
Martin, Williams, Pitoulias, Stevens, Winterhalter, Craggs, Murray, Searle, Soultanas (2021.08.16.456468v1.48) 2019; 47
Punjani, Rubinstein, Fleet, Brubaker (2021.08.16.456468v1.60) 2017; 14
Richardson, Harran, Murray (2021.08.16.456468v1.63) 2016; 534
Robinson, Causer, Dixon (2021.08.16.456468v1.65) 2012; 13
Bruand, Ehrlich, Janniere (2021.08.16.456468v1.7) 1995; 14
Miller, Locke, Greiwe, Diffley, Costa (2021.08.16.456468v1.51) 2019; 575
References_xml – volume: 351
  start-page: 66
  year: 2005
  end-page: 75
  ident: 2021.08.16.456468v1.87
  article-title: The Bacillus subtilis DnaD and DnaB proteins exhibit different DNA remodelling activities
  publication-title: Journal of molecular biology
– volume: 283
  start-page: 8351
  year: 2008
  end-page: 8362
  ident: 2021.08.16.456468v1.57
  article-title: A common mechanism for the ATP-DnaA- dependent formation of open complexes at the replication origin
  publication-title: J. Biol. Chem
– volume: 1
  start-page: 117
  year: 2003
  end-page: 126
  ident: 2021.08.16.456468v1.17
  article-title: Regulation of endospore formation in Bacillus subtilis
  publication-title: Nature Reviews Microbiology
– volume: 111
  start-page: 9121
  year: 2014
  end-page: 9126
  ident: 2021.08.16.456468v1.72
  article-title: Mechanism of staphylococcal multiresistance plasmid replication origin assembly by the RepA protein
  publication-title: Proc Natl Acad Sci U S A
– volume: 87
  start-page: 925
  year: 2013
  end-page: 938
  ident: 2021.08.16.456468v1.5
  article-title: Spo0A regulates chromosome copy number during sporulation by directly binding to the origin of replication in Bacillus subtilis
  publication-title: Mol Microbiol
– volume: 272
  start-page: 1
  year: 1993
  end-page: 40
  ident: 2021.08.16.456468v1.85
  article-title: Light scattering and the absolute characterization of macromolecules
  publication-title: Analytica Chimica Acta
– volume: 111
  start-page: 118
  year: 2018
  end-page: 130
  ident: 2021.08.16.456468v1.49
  article-title: Cryptic protein interactions regulate DNA replication initiation
  publication-title: Mol. Microbiol
– volume: 8
  start-page: 4335
  year: 1989
  end-page: 4344
  ident: 2021.08.16.456468v1.42
  article-title: The DNA unwinding element: a novel, cis-acting component that facilitates opening of the Escherichia coli replication origin
  publication-title: EMBO J
– volume: 478
  start-page: 209
  year: 2011
  end-page: 213
  ident: 2021.08.16.456468v1.15
  article-title: DNA stretching by bacterial initiators promotes replication origin opening
  publication-title: Nature
– volume: 14
  start-page: 2106
  year: 1995
  end-page: 2111
  ident: 2021.08.16.456468v1.68
  article-title: The DNA binding domain of the initiator protein DnaA
  publication-title: EMBO J
– volume: 7
  start-page: 239
  year: 2016
  ident: 2021.08.16.456468v1.55
  article-title: The Escherichia coli Cryptic Prophage Protein YfdR Binds to DnaA and Initiation of Chromosomal Replication Is Inhibited by Overexpression of the Gene Cluster yfdQ-yfdR-yfdS-yfdT
  publication-title: Front Microbiol
– volume: 37
  start-page: 1270
  year: 2000
  end-page: 1279
  ident: 2021.08.16.456468v1.73
  article-title: The interaction domains of the DnaA and DnaB replication proteins of Escherichia coli
  publication-title: Mol Microbiol
– volume: 274
  start-page: 365
  year: 1997
  end-page: 380
  ident: 2021.08.16.456468v1.44
  article-title: Complexes at the replication origin of Bacillus subtilis with homologous and heterologous DnaA protein
  publication-title: J. Mol. Biol
– volume: 14
  start-page: 331
  year: 2017
  end-page: 332
  ident: 2021.08.16.456468v1.89
  article-title: MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
  publication-title: Nat Methods
– volume: 228
  start-page: 123
  year: 1999
  end-page: 132
  ident: 2021.08.16.456468v1.43
  article-title: DnaA proteins of Escherichia coli and Bacillus subtilis: coordinate actions with single-stranded DNA-binding protein and interspecies inhibition during open complex formation at the replication origins
  publication-title: Gene
– volume: 67
  start-page: 1331
  year: 2008b
  end-page: 1346
  ident: 2021.08.16.456468v1.12
  article-title: Escherichia coli Dps interacts with DnaA protein to impede initiation: a model of adaptive mutation
  publication-title: Mol Microbiol
– volume: 75
  start-page: 861
  year: 2019
  end-page: 877
  ident: 2021.08.16.456468v1.45
  article-title: Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix
  publication-title: Acta Crystallogr D Struct Biol
– volume: 97
  start-page: 8063
  year: 2000
  end-page: 8068
  ident: 2021.08.16.456468v1.21
  article-title: The transcriptional profile of early to middle sporulation in Bacillus subtilis
  publication-title: Proceedings of the National Academy of Sciences of the United States of America
– volume: 81
  start-page: 819
  year: 1999
  end-page: 825
  ident: 2021.08.16.456468v1.50
  article-title: Functional domains of DnaA proteins
  publication-title: Biochimie
– volume: 105
  start-page: 1
  year: 1980
  end-page: 6
  ident: 2021.08.16.456468v1.38
  article-title: Isolation of a complex between the P protein of phage lambda and the dnaB protein of Escherichia coli
  publication-title: Eur J Biochem
– volume: 75
  start-page: 452
  year: 2010
  end-page: 461
  ident: 2021.08.16.456468v1.74
  article-title: Ordered association of helicase loader proteins with the Bacillus subtilis origin of replication in vivo
  publication-title: Mol Microbiol
– volume: 72
  start-page: 1275
  year: 2017
  end-page: 1284
  ident: 2021.08.16.456468v1.79
  article-title: DNA replication proteins as potential targets for antimicrobials in drug-resistant bacterial pathogens
  publication-title: J Antimicrob Chemother
– volume: 40
  start-page: 739
  year: 2012
  end-page: 750
  ident: 2021.08.16.456468v1.13
  article-title: Untwisting of the DNA helix stimulates the endonuclease activity of Bacillus subtilis Nth at AP sites
  publication-title: Nucleic acids research
– volume: 1
  start-page: 1
  year: 2009
  end-page: 15
  ident: 2021.08.16.456468v1.52
  article-title: Fluorescence Polarization (FP) Assays for Monitoring Peptide-Protein or Nucleic Acid-Protein Binding
  publication-title: Curr Protoc Chem Biol
– volume: 135
  start-page: 623
  year: 2008
  end-page: 634
  ident: 2021.08.16.456468v1.53
  article-title: Structural synergy and molecular crosstalk between bacterial helicase loaders and replication initiators
  publication-title: Cell
– volume: 2
  start-page: 463
  year: 1983
  end-page: 468
  ident: 2021.08.16.456468v1.40
  article-title: The origin of replication, oriC, and the dnaA protein are dispensable in stable DNA replication (sdrA) mutants of Escherichia coli K-12
  publication-title: The EMBO journal
– volume: 192
  start-page: 216
  year: 2015
  end-page: 221
  ident: 2021.08.16.456468v1.66
  article-title: CTFFIND4: Fast and accurate defocus estimation from electron micrographs
  publication-title: Journal of structural biology
– volume: 38
  start-page: e101649
  year: 2019
  ident: 2021.08.16.456468v1.64
  article-title: Identification of a basal system for unwinding a bacterial chromosome origin
  publication-title: The EMBO journal
– volume: 5
  year: 2013
  ident: 2021.08.16.456468v1.3
  article-title: Helicase loading at chromosomal origins of replication
  publication-title: Cold Spring Harb Perspect Biol
– volume: 47
  start-page: 2101
  year: 2019
  end-page: 2112
  ident: 2021.08.16.456468v1.48
  article-title: DNA replication initiation in Bacillus subtilis: structural and functional characterization of the essential DnaA-DnaD interaction
  publication-title: Nucleic Acids Res
– year: 2014
  ident: 2021.08.16.456468v1.81
  article-title: Bacillus subtilis chromosome organization oscillates between two distinct patterns
  publication-title: Proc Natl Acad Sci U S A
– volume: 88
  start-page: 667
  year: 1997
  end-page: 674
  ident: 2021.08.16.456468v1.82
  article-title: Bipolar localization of the replication origin regions of chromosomes in vegetative and sporulating cells of B. subtilis
  publication-title: Cell
– volume: 67
  start-page: 781
  year: 2008a
  end-page: 792
  ident: 2021.08.16.456468v1.11
  article-title: Escherichia coli DnaA interacts with HU in initiation at the E. coli replication origin
  publication-title: Mol. Microbiol
– volume: 179
  start-page: 2494
  year: 1997
  end-page: 2502
  ident: 2021.08.16.456468v1.26
  article-title: Suppression of initiation defects of chromosome replication in Bacillus subtilis dnaA and oriC-deleted mutants by integration of a plasmid replicon into the chromosomes
  publication-title: Journal of bacteriology
– volume: 194
  start-page: 5162
  year: 2012
  end-page: 5170
  ident: 2021.08.16.456468v1.6
  article-title: Chromosomal replication initiation machinery of low-G+C-content Firmicutes
  publication-title: Journal of bacteriology
– volume: 14
  start-page: 290
  year: 2017
  end-page: 296
  ident: 2021.08.16.456468v1.60
  article-title: cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
  publication-title: Nat Methods
– volume: 21
  start-page: 4763
  year: 2002
  end-page: 4773
  ident: 2021.08.16.456468v1.19
  article-title: The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation
  publication-title: EMBO J
– volume: 95
  start-page: 5752
  year: 1998
  end-page: 5756
  ident: 2021.08.16.456468v1.34
  article-title: A bacterial two-hybrid system based on a reconstituted signal transduction pathway
  publication-title: Proc Natl Acad Sci U S A
– volume: 179
  start-page: 2060
  year: 1997
  end-page: 2064
  ident: 2021.08.16.456468v1.41
  article-title: Association of the histone-like protein HBsu with the nucleoid of Bacillus subtilis
  publication-title: Journal of bacteriology
– volume: 106
  start-page: 21115
  year: 2009
  end-page: 21120
  ident: 2021.08.16.456468v1.54
  article-title: The structure of a DnaA/HobA complex from Helicobacter pylori provides insight into regulation of DNA replication in bacteria
  publication-title: Proc. Natl. Acad. Sci. USA
– volume: 28
  start-page: 1
  year: 1997
  end-page: 9
  ident: 2021.08.16.456468v1.69
  article-title: Prediction of the structure of the replication initiator protein DnaA
  publication-title: Proteins
– volume: 14
  start-page: 155
  year: 2007
  end-page: 168
  ident: 2021.08.16.456468v1.30
  article-title: Distribution of stable DnaA-binding sites on the Bacillus subtilis genome detected using a modified ChIP-chip method
  publication-title: DNA Res
– volume: 74
  start-page: 4057
  year: 2000
  end-page: 4063
  ident: 2021.08.16.456468v1.56
  article-title: The interaction of bacteriophage P2 B protein with Escherichia coli DnaB helicase
  publication-title: J Virol
– volume: 38
  start-page: 889
  year: 1984
  end-page: 900
  ident: 2021.08.16.456468v1.24
  article-title: The dnaA protein complex with the E. coli chromosomal replication origin (oriC) and other DNA sites
  publication-title: Cell
– volume: 46
  start-page: 1149
  year: 2002
  end-page: 1156
  ident: 2021.08.16.456468v1.84
  article-title: Strand-specific loading of DnaB helicase by DnaA to a substrate mimicking unwound oriC
  publication-title: Mol Microbiol
– volume: 22
  year: 2021
  ident: 2021.08.16.456468v1.32
  article-title: Putative Cooperative ATP-DnaA Binding to Double-Stranded DnaA Box and Single-Stranded DnaA-Trio Motif upon Helicobacter pylori Replication Initiation Complex Assembly
  publication-title: International journal of molecular sciences
– volume: 19
  year: 2001
  ident: 2021.08.16.456468v1.25
  article-title: Gel-filtration chromatography
  publication-title: Curr Protoc Mol Biol
– volume: 60
  start-page: 2126
  year: 2004
  end-page: 2132
  ident: 2021.08.16.456468v1.16
  article-title: Coot: model-building tools for molecular graphics
  publication-title: Acta Crystallogr D Biol Crystallogr
– volume: 34
  start-page: 53
  year: 1999
  end-page: 66
  ident: 2021.08.16.456468v1.83
  article-title: The N- terminus promotes oligomerization of the Escherichia coli initiator protein DnaA
  publication-title: Mol. Microbiol
– volume: 192
  start-page: 6209
  year: 2010
  end-page: 6216
  ident: 2021.08.16.456468v1.37
  article-title: Repression of sigK intervening (skin) element gene expression by the CI-like protein SknR and effect of SknR depletion on growth of Bacillus subtilis cells
  publication-title: Journal of bacteriology
– volume: 170
  start-page: 1333
  year: 1988
  end-page: 1338
  ident: 2021.08.16.456468v1.2
  article-title: Interaction of the Bacillus subtilis DnaA-like protein with the Escherichia coli DnaA protein
  publication-title: Journal of bacteriology
– volume: 9
  start-page: 676
  year: 2012
  end-page: 682
  ident: 2021.08.16.456468v1.70
  article-title: Fiji: an open-source platform for biological-image analysis
  publication-title: Nat. Methods
– volume: 282
  start-page: 17816
  year: 2007
  end-page: 17827
  ident: 2021.08.16.456468v1.1
  article-title: Structure and function of DnaA N-terminal domains: specific sites and mechanisms in inter-DnaA interaction and in DnaB helicase loading on oriC
  publication-title: The Journal of biological chemistry
– volume: 38
  start-page: 6930
  year: 2010
  end-page: 6942
  ident: 2021.08.16.456468v1.47
  article-title: When simple sequence comparison fails: the cryptic case of the shared domains of the bacterial replication initiation proteins DnaB and DnaD
  publication-title: Nucleic acids research
– volume: 273
  start-page: 34255
  year: 1998
  end-page: 34262
  ident: 2021.08.16.456468v1.76
  article-title: Escherichia coli DnaA protein
  publication-title: The N-terminal domain and loading of DnaB helicase at the E. coli chromosomal origin. J. Biol. Chem
– volume: 11
  start-page: e0157593
  year: 2016
  ident: 2021.08.16.456468v1.28
  article-title: Characterization of Staphylococcus aureus Primosomal DnaD Protein: Highly Conserved C-Terminal Region Is Crucial for ssDNA and PriA Helicase Binding but Not for DnaA Protein-Binding and Self- Tetramerization
  publication-title: PloS one
– volume: 13
  start-page: 676
  year: 2006
  end-page: 683
  ident: 2021.08.16.456468v1.18
  article-title: Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling
  publication-title: Nature structural & molecular biology
– volume: 355
  year: 2017
  ident: 2021.08.16.456468v1.4
  article-title: Mechanisms for initiating cellular DNA replication. Science (New York
  publication-title: N.Y
– volume: 14
  start-page: 2642
  year: 1995
  end-page: 2650
  ident: 2021.08.16.456468v1.7
  article-title: Primosome assembly site in Bacillus subtilis
  publication-title: The EMBO journal
– volume: 4
  start-page: 541
  year: 1999
  end-page: 553
  ident: 2021.08.16.456468v1.20
  article-title: Replisome assembly at oriC, the replication origin of E. coli, reveals an explanation for initiation sites outside an origin
  publication-title: Molecular cell
– volume: 376
  start-page: 1237
  year: 2008
  end-page: 1250
  ident: 2021.08.16.456468v1.71
  article-title: Structure of the N-terminal oligomerization domain of DnaD reveals a unique tetramerization motif and provides insights into scaffold formation
  publication-title: J. Mol. Biol
– volume: 284
  start-page: 25038
  year: 2009
  end-page: 25050
  ident: 2021.08.16.456468v1.35
  article-title: DiaA dynamics are coupled with changes in initial origin complexes leading to helicase loading
  publication-title: The Journal of biological chemistry
– volume: 49
  start-page: 7525
  year: 2021
  end-page: 7536
  ident: 2021.08.16.456468v1.58
  article-title: Evidence for a chromosome origin unwinding system broadly conserved in bacteria
  publication-title: Nucleic acids research
– volume: 60
  start-page: 917
  year: 2006
  end-page: 924
  ident: 2021.08.16.456468v1.9
  article-title: The DNA-remodelling activity of DnaD is the sum of oligomerization and DNA- binding activities on separate domains
  publication-title: Mol Microbiol
– volume: 6
  year: 2017
  ident: 2021.08.16.456468v1.22
  article-title: The structural basis for dynamic DNA binding and bridging interactions which condense the bacterial centromere
  publication-title: Elife
– volume: 357
  start-page: 314
  year: 2017
  end-page: 318
  ident: 2021.08.16.456468v1.14
  article-title: Bidirectional eukaryotic DNA replication is established by quasi-symmetrical helicase loading. Science (New York
  publication-title: N.Y
– volume: 4
  start-page: e6774
  year: 2009
  ident: 2021.08.16.456468v1.67
  article-title: Intragenic and extragenic suppressors of temperature sensitive mutations in the replication initiation genes dnaD and dnaB of Bacillus subtilis
  publication-title: PloS one
– volume: 188
  start-page: 5487
  year: 2006
  end-page: 5493
  ident: 2021.08.16.456468v1.86
  article-title: The Bacillus subtilis primosomal protein DnaD untwists supercoiled DNA
  publication-title: Journal of bacteriology
– volume: 193
  start-page: 640
  year: 2011
  end-page: 648
  ident: 2021.08.16.456468v1.75
  article-title: Primosomal proteins DnaD and DnaB are recruited to chromosomal regions bound by DnaA in Bacillus subtilis
  publication-title: Journal of bacteriology
– volume: 25
  start-page: 1605
  year: 2004
  end-page: 1612
  ident: 2021.08.16.456468v1.59
  article-title: UCSF Chimera--a visualization system for exploratory research and analysis
  publication-title: J Comput Chem
– volume: 161
  start-page: 513
  year: 2015
  end-page: 525
  ident: 2021.08.16.456468v1.77
  article-title: Single-molecule studies of origin licensing reveal mechanisms ensuring bidirectional helicase loading
  publication-title: Cell
– volume: 73
  start-page: 963
  year: 2009
  end-page: 974
  ident: 2021.08.16.456468v1.80
  article-title: SirA enforces diploidy by inhibiting the replication initiator DnaA during spore formation in Bacillus subtilis
  publication-title: Mol. Microbiol
– volume: 55
  start-page: 1138
  year: 2005
  end-page: 1150
  ident: 2021.08.16.456468v1.8
  article-title: Functional interplay between the Bacillus subtilis DnaD and DnaB proteins essential for initiation and re-initiation of DNA replication
  publication-title: Mol Microbiol
– volume: 534
  start-page: 412
  year: 2016
  end-page: 416
  ident: 2021.08.16.456468v1.63
  article-title: The bacterial DnaA-trio replication origin element specifies single-stranded DNA initiator binding
  publication-title: Nature
– volume: 13
  start-page: 352
  year: 2012
  end-page: 372
  ident: 2021.08.16.456468v1.65
  article-title: Architecture and conservation of the bacterial DNA replication machinery, an underexploited drug target
  publication-title: Curr Drug Targets
– volume: 13
  start-page: 931
  year: 2017
  ident: 2021.08.16.456468v1.46
  article-title: High-throughput CRISPRi phenotyping identifies new essential genes in Streptococcus pneumoniae
  publication-title: Mol Syst Biol
– volume: 36
  start-page: 1037
  year: 2000
  end-page: 1048
  ident: 2021.08.16.456468v1.29
  article-title: Subcellular localization of Dna-initiation proteins of Bacillus subtilis: evidence that chromosome replication begins at either edge of the nucleoids
  publication-title: Mol Microbiol
– volume: 193
  start-page: 1302
  year: 2011
  end-page: 1307
  ident: 2021.08.16.456468v1.62
  article-title: The sporulation protein SirA inhibits the binding of DnaA to the origin of replication by contacting a patch of clustered amino acids
  publication-title: Journal of bacteriology
– volume: 10
  start-page: 291
  year: 2009
  ident: 2021.08.16.456468v1.10
  article-title: Comprehensive identification of essential Staphylococcus aureus genes using Transposon-Mediated Differential Hybridisation (TMDH)
  publication-title: BMC Genomics
– volume: 21
  start-page: 2083
  year: 2007
  end-page: 2099
  ident: 2021.08.16.456468v1.36
  article-title: The interaction of DiaA and DnaA regulates the replication cycle in E. coli by directly promoting ATP DnaA-specific initiation complexes
  publication-title: Genes & development
– volume: 93
  start-page: 975
  year: 2014
  end-page: 991
  ident: 2021.08.16.456468v1.31
  article-title: Structure and interactions of the Bacillus subtilis sporulation inhibitor of DNA replication, SirA, with domain I of DnaA
  publication-title: Mol Microbiol
– volume: 5
  year: 2016
  ident: 2021.08.16.456468v1.27
  article-title: Viral hijacking of a replicative helicase loader and its implications for helicase loading control and phage replication
  publication-title: Elife
– volume: 377
  start-page: 706
  year: 2008
  end-page: 714
  ident: 2021.08.16.456468v1.88
  article-title: Single-molecule atomic force spectroscopy reveals that DnaD forms scaffolds and enhances duplex melting
  publication-title: Journal of molecular biology
– volume: 31
  start-page: 2077
  year: 2003
  end-page: 2086
  ident: 2021.08.16.456468v1.23
  article-title: Structural basis of replication origin recognition by the DnaA protein
  publication-title: Nucleic Acids Res
– volume: 575
  start-page: 704
  year: 2019
  end-page: 710
  ident: 2021.08.16.456468v1.51
  article-title: Mechanism of head-to-head MCM double-hexamer formation revealed by cryo-EM
  publication-title: Nature
– volume: 100
  start-page: 4678
  year: 2003
  end-page: 4683
  ident: 2021.08.16.456468v1.39
  article-title: Essential Bacillus subtilis genes
  publication-title: Proc Natl Acad Sci U S A
– volume: 191
  start-page: 3736
  year: 2009
  end-page: 3739
  ident: 2021.08.16.456468v1.61
  article-title: The conserved sporulation protein YneE inhibits DNA replication in Bacillus subtilis
  publication-title: Journal of bacteriology
– volume: 7
  year: 2018
  ident: 2021.08.16.456468v1.33
  article-title: The Macromolecular Machines that Duplicate the Escherichia coli Chromosome as Targets for Drug Discovery
  publication-title: Antibiotics (Basel
– volume: 115
  start-page: 80
  year: 2017
  end-page: 90
  ident: 2021.08.16.456468v1.78
  article-title: TrackMate: An open and extensible platform for single-particle tracking
  publication-title: Methods
SSID ssj0002961374
Score 1.6304642
SecondaryResourceType preprint
Snippet The mechanisms responsible for helicase loading during the initiation of chromosome replication in bacteria are unclear. Here we report both a positive and a...
SourceID biorxiv
proquest
SourceType Open Access Repository
Aggregation Database
SubjectTerms Chromosomes
DNA biosynthesis
DNA helicase
Drug development
Interfaces
Microbiology
Mutagenesis
Nucleotide sequence
Replication initiation
Replication origins
Single-stranded DNA
Title Positive and negative control of helicase recruitment at a bacterial chromosome origin
URI https://www.proquest.com/docview/2561687367
https://www.biorxiv.org/content/10.1101/2021.08.16.456468
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV3PS8MwFA66KXjyN07niOC12vRndhKUDQUdRVTmqeQlqStoO9tt6H9vkmZ6ELwIvYSWR3gk7728fP0-hE6BhBBBKBwiCHUCRpnTl6F04pD5qj7lgeubH4Vv49GIjsf9xDbcagurXMZEE6hFyXWP_FylZhLRWBm4mL47WjVK365aCY1V1NYsCb6B7iXfPRavr5KVIWL2or7a-J4b2otNtRD1sd_Qd5LoTHOqaLLVdcjL6iNf_ArMJtsMN_87zy3UTthUVttoRRY7aL3Rm_zcRU-JgWgtJGaFwIV8Mazf2MLVcZnhidRNvFpiFQireW4g6JipB0ND68xeMZ9oCF9dvkncyGrtocfh4OHq2rHCCg6o0xd1ZOBz4EGQMcgEuF5GpRAu5S6NPQEeDUFQAC4BXK7qH1dwouq2mJEsUh9D5u-jVlEW8gBhwkASqgwBU5UXMBrQjHNf8Fh4XhbLDjqxPk2nDX1Gqv2eujQlUdr4vYO6S1emdgfV6Y8fD_9-fYQ2tEXd5yVRF7Vm1VweozW-mOV11UPty8Eoue-ZhaFGyc1d8vwF3arCkg
linkProvider ProQuest
linkToHtml http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V3fT9RAEJ4gJ5En8QcRRFwTfax2t7_2HogJCIFwXi4GDW91Z3cql2h7tnDCP-Xf6GzbgwcT3ngg6VubSdpvOjM7O_t9AG9RJphi4gLppA5io00wpISCLDER16c2DqP2oPAoG4_16elwsgR_F2dh_FjlIia2gdpV1vfIP3BqlqnO2MDH2e_Aq0b53dWFhEbnFsd09YeXbM3O0SfG951SB_sne4dBryoQIC89dEBxZNHGcWGwcBiqQpNzobahzpRDpRN0GtESYmg5-YfOSi5aMiOLlB_GImK7D2AQR3HG_9Vgd388-XLd1VFDTo8t9bNKhxxqVJj0W6ns-r7R0BKGyvS9Z3Hx9K4rOK3qy-n8v1TQ5reDx_fty6zBYGJmVD-BJSqfwkqnqHn1DL5N2iG0OQlTOlHSj5bXXPQD-aIqxBn5NmVDgkN9fTFth-yF4UtgR1xtfgp75ocUm-oXiU447Dl8vZNXWYflsirpBQhpkKRmQ2i4tkSjY11YGzmbOaWKjDbgTY9hPusIQnKPcx7qXKZ5h_MGbC2gy_sY0eQ3uG3efvs1PDo8-TzKR0fj45ew6q37rrZMt2D5vL6gV_DQzs-nTb3du6OA73eN8z8ttCEW
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Positive+and+negative+control+of+helicase+recruitment+at+a+bacterial+chromosome+origin&rft.jtitle=bioRxiv&rft.au=Winterhalter%2C+Charles&rft.au=Stevens%2C+Daniel&rft.au=Fenyk%2C+Stepan&rft.au=Pelliciari%2C+Simone&rft.date=2021-08-16&rft.pub=Cold+Spring+Harbor+Laboratory+Press&rft.issn=2692-8205&rft.eissn=2692-8205&rft_id=info:doi/10.1101%2F2021.08.16.456468
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2692-8205&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2692-8205&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2692-8205&client=summon