Nse5/6 is a negative regulator of the ATPase activity of the Smc5/6 complex

Abstract The multi-component Smc5/6 complex plays a critical role in the resolution of recombination intermediates formed during mitosis and meiosis, and in the cellular response to replication stress. Using recombinant proteins, we have reconstituted a series of defined Saccharomyces cerevisiae Smc...

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Published in:Nucleic acids research Vol. 49; no. 8; pp. 4534 - 4549
Main Authors: Hallett, Stephen T, Schellenberger, Pascale, Zhou, Lihong, Beuron, Fabienne, Morris, Ed, Murray, Johanne M, Oliver, Antony W
Format: Journal Article
Language:English
Published: England Oxford University Press 07.05.2021
Subjects:
Adenosine Triphosphatases - chemistry
Adenosine Triphosphatases - genetics
Adenosine Triphosphatases - metabolism
Cell Cycle Proteins - chemistry
Cell Cycle Proteins - genetics
Cell Cycle Proteins - metabolism
Cell Cycle Proteins - ultrastructure
Chromosomal Proteins, Non-Histone - chemistry
Chromosomal Proteins, Non-Histone - genetics
Chromosomal Proteins, Non-Histone - metabolism
Chromosomal Proteins, Non-Histone - ultrastructure
DNA - metabolism
Escherichia coli - metabolism
Genome Integrity, Repair and
Microscopy, Electron, Transmission
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Saccharomyces cerevisiae Proteins - ultrastructure
ISSN:0305-1048, 1362-4962, 1362-4962
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Abstract Abstract The multi-component Smc5/6 complex plays a critical role in the resolution of recombination intermediates formed during mitosis and meiosis, and in the cellular response to replication stress. Using recombinant proteins, we have reconstituted a series of defined Saccharomyces cerevisiae Smc5/6 complexes, visualised them by negative stain electron microscopy, and tested their ability to function as an ATPase. We find that only the six protein ‘holo-complex’ is capable of turning over ATP and that its activity is significantly increased by the addition of double-stranded DNA to reaction mixes. Furthermore, stimulation is wholly dependent on functional ATP-binding pockets in both Smc5 and Smc6. Importantly, we demonstrate that budding yeast Nse5/6 acts as a negative regulator of Smc5/6 ATPase activity, binding to the head-end of the complex to suppress turnover, irrespective of the DNA-bound status of the complex.
AbstractList The multi-component Smc5/6 complex plays a critical role in the resolution of recombination intermediates formed during mitosis and meiosis, and in the cellular response to replication stress. Using recombinant proteins, we have reconstituted a series of defined Saccharomyces cerevisiae Smc5/6 complexes, visualised them by negative stain electron microscopy, and tested their ability to function as an ATPase. We find that only the six protein ‘holo-complex’ is capable of turning over ATP and that its activity is significantly increased by the addition of double-stranded DNA to reaction mixes. Furthermore, stimulation is wholly dependent on functional ATP-binding pockets in both Smc5 and Smc6. Importantly, we demonstrate that budding yeast Nse5/6 acts as a negative regulator of Smc5/6 ATPase activity, binding to the head-end of the complex to suppress turnover, irrespective of the DNA-bound status of the complex.
Abstract The multi-component Smc5/6 complex plays a critical role in the resolution of recombination intermediates formed during mitosis and meiosis, and in the cellular response to replication stress. Using recombinant proteins, we have reconstituted a series of defined Saccharomyces cerevisiae Smc5/6 complexes, visualised them by negative stain electron microscopy, and tested their ability to function as an ATPase. We find that only the six protein ‘holo-complex’ is capable of turning over ATP and that its activity is significantly increased by the addition of double-stranded DNA to reaction mixes. Furthermore, stimulation is wholly dependent on functional ATP-binding pockets in both Smc5 and Smc6. Importantly, we demonstrate that budding yeast Nse5/6 acts as a negative regulator of Smc5/6 ATPase activity, binding to the head-end of the complex to suppress turnover, irrespective of the DNA-bound status of the complex.
The multi-component Smc5/6 complex plays a critical role in the resolution of recombination intermediates formed during mitosis and meiosis, and in the cellular response to replication stress. Using recombinant proteins, we have reconstituted a series of defined Saccharomyces cerevisiae Smc5/6 complexes, visualised them by negative stain electron microscopy, and tested their ability to function as an ATPase. We find that only the six protein 'holo-complex' is capable of turning over ATP and that its activity is significantly increased by the addition of double-stranded DNA to reaction mixes. Furthermore, stimulation is wholly dependent on functional ATP-binding pockets in both Smc5 and Smc6. Importantly, we demonstrate that budding yeast Nse5/6 acts as a negative regulator of Smc5/6 ATPase activity, binding to the head-end of the complex to suppress turnover, irrespective of the DNA-bound status of the complex.The multi-component Smc5/6 complex plays a critical role in the resolution of recombination intermediates formed during mitosis and meiosis, and in the cellular response to replication stress. Using recombinant proteins, we have reconstituted a series of defined Saccharomyces cerevisiae Smc5/6 complexes, visualised them by negative stain electron microscopy, and tested their ability to function as an ATPase. We find that only the six protein 'holo-complex' is capable of turning over ATP and that its activity is significantly increased by the addition of double-stranded DNA to reaction mixes. Furthermore, stimulation is wholly dependent on functional ATP-binding pockets in both Smc5 and Smc6. Importantly, we demonstrate that budding yeast Nse5/6 acts as a negative regulator of Smc5/6 ATPase activity, binding to the head-end of the complex to suppress turnover, irrespective of the DNA-bound status of the complex.
Author Hallett, Stephen T
Schellenberger, Pascale
Zhou, Lihong
Morris, Ed
Oliver, Antony W
Beuron, Fabienne
Murray, Johanne M
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  surname: Oliver
  fullname: Oliver, Antony W
  email: antony.oliver@sussex.ac.uk
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Cites_doi 10.1038/ncomms14011
10.1038/emboj.2008.220
10.1016/j.molcel.2020.11.012
10.1128/MCB.00767-07
10.1016/j.molcel.2020.11.011
10.1038/emboj.2009.413
10.7554/eLife.42166
10.1016/j.molcel.2019.03.037
10.1016/S1097-2765(02)00515-4
10.1016/j.jmb.2020.04.024
10.1093/nar/gkq038
10.1016/S1097-2765(03)00476-3
10.1016/j.celrep.2016.08.026
10.1128/MCB.26.5.1617-1630.2006
10.1016/j.molcel.2006.05.014
10.1126/science.1253671
10.1016/S0092-8674(00)80524-3
10.1074/jbc.M111.336263
10.1016/j.molcel.2019.09.020
10.1016/j.jsb.2012.09.006
10.1016/j.molcel.2019.05.035
10.1016/j.molcel.2020.07.013
10.1096/fj.201800899R
10.26508/lsa.201800143
10.1128/MCB.00271-18
10.1016/j.molcel.2020.04.026
10.1073/pnas.1604935113
10.1074/jbc.M809139200
10.1016/j.celrep.2015.07.048
10.1038/emboj.2010.315
10.1042/BST20200389
10.1093/emboj/19.7.1691
10.1083/jcb.200111002
10.1128/JVI.00356-18
10.7554/eLife.59560
10.1016/j.molcel.2018.05.022
10.3390/genes10010007
10.1002/jcc.20084
10.1016/j.molcel.2009.06.032
10.1038/s41594-019-0196-z
10.1007/s00294-018-0922-9
10.3390/genes9010036
10.1038/nrm.2016.30
10.1074/jbc.M608004200
10.1016/j.molcel.2017.01.026
10.1172/JCI73264
10.1107/S1744309109027900
10.1128/JVI.00825-18
10.1172/JCI82890
10.1126/science.abb0981
10.1038/nature17170
10.1074/jbc.M111.235200
10.1074/jbc.M111.311860
10.1074/jbc.M301004200
10.7554/eLife.68579.sa2
10.3390/antib3020182
10.1534/genetics.105.044966
10.1021/cb800025k
10.3390/pathogens9100786
10.1091/mbc.10.9.2905
10.1007/978-1-4939-2272-7_12
10.1038/nature12867
10.1016/j.molcel.2010.06.019
10.1016/j.cub.2018.08.034
10.3390/genes9120581
10.1146/annurev-genet-120417-031353
10.1038/s41594-020-0457-x
10.1093/nar/gkv1021
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References Hassler (2021070811582426900_B5) 2018; 28
Oravcova (2021070811582426900_B23) 2019; 39
Higashi (2021070811582426900_B57) 2020; 79
Gutierrez-Escribano (2021070811582426900_B52) 2020; 80
Oravcova (2021070811582426900_B22) 2019; 65
Telmer (2021070811582426900_B47) 2003; 278
Litwin (2021070811582426900_B24) 2018; 9
Los (2021070811582426900_B37) 2008; 3
Duan (2021070811582426900_B43) 2009; 35
Fousteri (2021070811582426900_B48) 2000; 19
Gibson (2021070811582426900_B16) 2020; 9
Adamus (2021070811582426900_B31) 2020; 432
Bentley (2021070811582426900_B15) 2018; 92
Murphy (2021070811582426900_B13) 2016; 16
Lee (2021070811582426900_B59) 2020; 27
Li (2021070811582426900_B67) 2012; 287
Bustard (2021070811582426900_B26) 2012; 287
Alt (2021070811582426900_B1) 2017; 8
Pebernard (2021070811582426900_B63) 2008; 27
Raschle (2021070811582426900_B21) 2015; 348
Burmann (2021070811582426900_B61) 2017; 65
Serrano (2021070811582426900_B53) 2020; 80
Palecek (2021070811582426900_B10) 2019; 10
Kanno (2021070811582426900_B49) 2015; 12
Payne (2021070811582426900_B17) 2014; 124
Williams (2021070811582426900_B68) 2010; 29
Wan (2021070811582426900_B30) 2019; 75
Uhlmann (2021070811582426900_B6) 2016; 17
Hassler (2021070811582426900_B46) 2019; 74
Schrödinger, LLC (2021070811582426900_B42)
Kimura (2021070811582426900_B50) 1997; 90
Kurze (2021070811582426900_B4) 2011; 30
Aragon (2021070811582426900_B8) 2018; 52
Decorsiere (2021070811582426900_B12) 2016; 531
Taylor (2021070811582426900_B7) 2008; 28
Sheedy (2021070811582426900_B29) 2005; 171
Hazbun (2021070811582426900_B19) 2003; 12
Zabrady (2021070811582426900_B69) 2016; 44
Shi (2021070811582426900_B60) 2020; 368
Minamino (2021070811582426900_B64) 2018; 1
Palecek (2021070811582426900_B33) 2006; 281
Zivanov (2021070811582426900_B40) 2018; 7
Pebernard (2021070811582426900_B20) 2006; 26
Sole-Soler (2021070811582426900_B11) 2020; 48
Xu (2021070811582426900_B14) 2018; 92
Duan (2021070811582426900_B32) 2009; 284
Scheres (2021070811582426900_B39) 2012; 180
Duan (2021070811582426900_B44) 2009; 65
Haering (2021070811582426900_B3) 2002; 9
Petela (2021070811582426900_B65) 2018; 70
Kong (2021070811582426900_B58) 2020; 79
Djender (2021070811582426900_B36) 2014; 3
Collier (2021070811582426900_B56) 2020; 9
Murayama (2021070811582426900_B51) 2014; 505
Griese (2021070811582426900_B2) 2010; 38
Verkade (2021070811582426900_B28) 1999; 10
Anderson (2021070811582426900_B54) 2002; 156
Weissmann (2021070811582426900_B34) 2016; 113
Burmann (2021070811582426900_B55) 2019; 26
van der Crabben (2021070811582426900_B18) 2016; 126
Elbatsh (2021070811582426900_B45) 2019; 76
Ohouo (2021070811582426900_B27) 2010; 39
Barnett (2021070811582426900_B38) 2019; 33
Diaz (2021070811582426900_B9) 2018; 9
Leung (2021070811582426900_B66) 2011; 286
Pettersen (2021070811582426900_B41) 2004; 25
Etheridge (2021070811582426900_B25) 2021
Fairhead (2021070811582426900_B35) 2015; 1266
Lindroos (2021070811582426900_B62) 2006; 22
References_xml – volume: 8
  start-page: 14011
  year: 2017
  ident: 2021070811582426900_B1
  article-title: Specialized interfaces of Smc5/6 control hinge stability and DNA association
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms14011
– volume: 27
  start-page: 3011
  year: 2008
  ident: 2021070811582426900_B63
  article-title: Localization of Smc5/6 to centromeres and telomeres requires heterochromatin and SUMO, respectively
  publication-title: EMBO J.
  doi: 10.1038/emboj.2008.220
– volume: 80
  start-page: 1039
  year: 2020
  ident: 2021070811582426900_B52
  article-title: Purified Smc5/6 complex exhibits DNA substrate recognition and compaction
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2020.11.012
– volume: 28
  start-page: 1197
  year: 2008
  ident: 2021070811582426900_B7
  article-title: Identification of the proteins, including MAGEG1, that make up the human SMC5-6 protein complex
  publication-title: Mol. Cell. Biol.
  doi: 10.1128/MCB.00767-07
– volume: 80
  start-page: 1025
  year: 2020
  ident: 2021070811582426900_B53
  article-title: The Smc5/6 core complex is a structure-specific DNA binding and compacting machine
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2020.11.011
– volume: 29
  start-page: 1136
  year: 2010
  ident: 2021070811582426900_B68
  article-title: gammaH2A binds Brc1 to maintain genome integrity during S-phase
  publication-title: EMBO J.
  doi: 10.1038/emboj.2009.413
– volume: 7
  start-page: e42166
  year: 2018
  ident: 2021070811582426900_B40
  article-title: New tools for automated high-resolution cryo-EM structure determination in RELION-3
  publication-title: Elife
  doi: 10.7554/eLife.42166
– volume: 74
  start-page: 1175
  year: 2019
  ident: 2021070811582426900_B46
  article-title: Structural basis of an asymmetric condensin ATPase cycle
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2019.03.037
– volume: 9
  start-page: 773
  year: 2002
  ident: 2021070811582426900_B3
  article-title: Molecular architecture of SMC proteins and the yeast cohesin complex
  publication-title: Mol. Cell
  doi: 10.1016/S1097-2765(02)00515-4
– volume: 432
  start-page: 3820
  year: 2020
  ident: 2021070811582426900_B31
  article-title: Molecular insights into the architecture of the human SMC5/6 complex
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2020.04.024
– volume: 38
  start-page: 3454
  year: 2010
  ident: 2021070811582426900_B2
  article-title: Structure and DNA binding activity of the mouse condensin hinge domain highlight common and diverse features of SMC proteins
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkq038
– volume: 12
  start-page: 1353
  year: 2003
  ident: 2021070811582426900_B19
  article-title: Assigning function to yeast proteins by integration of technologies
  publication-title: Mol. Cell
  doi: 10.1016/S1097-2765(03)00476-3
– volume: 16
  start-page: 2846
  year: 2016
  ident: 2021070811582426900_B13
  article-title: Hepatitis B virus X protein promotes degradation of SMC5/6 to enhance HBV replication
  publication-title: Cell Rep.
  doi: 10.1016/j.celrep.2016.08.026
– volume: 26
  start-page: 1617
  year: 2006
  ident: 2021070811582426900_B20
  article-title: The Nse5-Nse6 dimer mediates DNA repair roles of the Smc5-Smc6 complex
  publication-title: Mol. Cell. Biol.
  doi: 10.1128/MCB.26.5.1617-1630.2006
– volume: 22
  start-page: 755
  year: 2006
  ident: 2021070811582426900_B62
  article-title: Chromosomal association of the Smc5/6 complex reveals that it functions in differently regulated pathways
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2006.05.014
– volume: 348
  start-page: 1253671
  year: 2015
  ident: 2021070811582426900_B21
  article-title: DNA repair. Proteomics reveals dynamic assembly of repair complexes during bypass of DNA cross-links
  publication-title: Science
  doi: 10.1126/science.1253671
– volume: 90
  start-page: 625
  year: 1997
  ident: 2021070811582426900_B50
  article-title: ATP-dependent positive supercoiling of DNA by 13S condensin: a biochemical implication for chromosome condensation
  publication-title: Cell
  doi: 10.1016/S0092-8674(00)80524-3
– volume: 287
  start-page: 11374
  year: 2012
  ident: 2021070811582426900_B26
  article-title: During replication stress, non-SMC element 5 (NSE5) is required for Smc5/6 protein complex functionality at stalled forks
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M111.336263
– volume: 76
  start-page: 724
  year: 2019
  ident: 2021070811582426900_B45
  article-title: Distinct roles for condensin's two ATPase sites in chromosome condensation
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2019.09.020
– volume: 180
  start-page: 519
  year: 2012
  ident: 2021070811582426900_B39
  article-title: RELION: implementation of a Bayesian approach to cryo-EM structure determination
  publication-title: J. Struct. Biol.
  doi: 10.1016/j.jsb.2012.09.006
– volume: 75
  start-page: 238
  year: 2019
  ident: 2021070811582426900_B30
  article-title: Molecular basis for control of diverse genome stability factors by the multi-BRCT scaffold Rtt107
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2019.05.035
– volume: 79
  start-page: 917
  year: 2020
  ident: 2021070811582426900_B57
  article-title: A structure-based mechanism for DNA entry into the cohesin ring
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2020.07.013
– volume: 33
  start-page: 763
  year: 2019
  ident: 2021070811582426900_B38
  article-title: Understanding the coupling between DNA damage detection and UvrA’s ATPase using bulk and single molecule kinetics
  publication-title: FASEB J.
  doi: 10.1096/fj.201800899R
– volume: 1
  start-page: e201800143
  year: 2018
  ident: 2021070811582426900_B64
  article-title: Topological in vitro loading of the budding yeast cohesin ring onto DNA
  publication-title: Life Sci. Alliance
  doi: 10.26508/lsa.201800143
– volume: 39
  start-page: e00271-18
  year: 2019
  ident: 2021070811582426900_B23
  article-title: Brc1 promotes the focal accumulation and SUMO ligase activity of Smc5-Smc6 during replication stress
  publication-title: Mol. Cell. Biol.
  doi: 10.1128/MCB.00271-18
– volume: 79
  start-page: 99
  year: 2020
  ident: 2021070811582426900_B58
  article-title: Human condensin I and II drive extensive ATP-dependent compaction of nucleosome-bound DNA
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2020.04.026
– volume: 113
  start-page: E2564
  year: 2016
  ident: 2021070811582426900_B34
  article-title: biGBac enables rapid gene assembly for the expression of large multisubunit protein complexes
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  doi: 10.1073/pnas.1604935113
– volume: 284
  start-page: 8507
  year: 2009
  ident: 2021070811582426900_B32
  article-title: Architecture of the Smc5/6 complex of Saccharomyces cerevisiae reveals a unique interaction between the Nse5-6 subcomplex and the hinge regions of Smc5 and Smc6
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M809139200
– volume: 12
  start-page: 1471
  year: 2015
  ident: 2021070811582426900_B49
  article-title: The Smc5/6 complex is an ATP-dependent intermolecular DNA linker
  publication-title: Cell Rep.
  doi: 10.1016/j.celrep.2015.07.048
– volume: 30
  start-page: 364
  year: 2011
  ident: 2021070811582426900_B4
  article-title: A positively charged channel within the Smc1/Smc3 hinge required for sister chromatid cohesion
  publication-title: EMBO J.
  doi: 10.1038/emboj.2010.315
– volume: 48
  start-page: 2159
  year: 2020
  ident: 2021070811582426900_B11
  article-title: Smc5/6, an atypical SMC complex with two RING-type subunits
  publication-title: Biochem Soc T
  doi: 10.1042/BST20200389
– volume: 19
  start-page: 1691
  year: 2000
  ident: 2021070811582426900_B48
  article-title: A novel SMC protein complex in Schizosaccharomyces pombe contains the Rad18 DNA repair protein
  publication-title: EMBO J.
  doi: 10.1093/emboj/19.7.1691
– volume: 156
  start-page: 419
  year: 2002
  ident: 2021070811582426900_B54
  article-title: Condensin and cohesin display different arm conformations with characteristic hinge angles
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.200111002
– volume: 92
  start-page: e00356-18
  year: 2018
  ident: 2021070811582426900_B15
  article-title: The SMC5/6 complex interacts with the Papillomavirus E2 protein and influences maintenance of viral episomal DNA
  publication-title: J. Virol.
  doi: 10.1128/JVI.00356-18
– volume: 9
  start-page: e59560
  year: 2020
  ident: 2021070811582426900_B56
  article-title: Transport of DNA within cohesin involves clamping on top of engaged heads by Scc2 and entrapment within the ring by Scc3
  publication-title: Elife
  doi: 10.7554/eLife.59560
– volume: 70
  start-page: 1134
  year: 2018
  ident: 2021070811582426900_B65
  article-title: Scc2 is a potent activator of cohesin's ATPase that promotes loading by binding Scc1 without Pds5
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2018.05.022
– volume: 10
  start-page: 7
  year: 2019
  ident: 2021070811582426900_B10
  article-title: SMC5/6: multifunctional player in replication
  publication-title: Genes-Basel
  doi: 10.3390/genes10010007
– volume: 25
  start-page: 1605
  year: 2004
  ident: 2021070811582426900_B41
  article-title: UCSF Chimera—a visualization system for exploratory research and analysis
  publication-title: J. Comput. Chem.
  doi: 10.1002/jcc.20084
– volume: 35
  start-page: 657
  year: 2009
  ident: 2021070811582426900_B43
  article-title: Structural and functional insights into the roles of the Mms21 subunit of the Smc5/6 complex
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2009.06.032
– volume: 26
  start-page: 227
  year: 2019
  ident: 2021070811582426900_B55
  article-title: A folded conformation of MukBEF and cohesin
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/s41594-019-0196-z
– volume: 65
  start-page: 669
  year: 2019
  ident: 2021070811582426900_B22
  article-title: Recruitment, loading, and activation of the Smc5-Smc6 SUMO ligase
  publication-title: Curr. Genet.
  doi: 10.1007/s00294-018-0922-9
– volume: 9
  start-page: 36
  year: 2018
  ident: 2021070811582426900_B9
  article-title: Scaffolding for repair: understanding molecular functions of the SMC5/6 complex
  publication-title: Genes
  doi: 10.3390/genes9010036
– volume: 17
  start-page: 399
  year: 2016
  ident: 2021070811582426900_B6
  article-title: SMC complexes: from DNA to chromosomes
  publication-title: Nat. Rev. Mol. Cell Biol.
  doi: 10.1038/nrm.2016.30
– volume: 281
  start-page: 36952
  year: 2006
  ident: 2021070811582426900_B33
  article-title: The Smc5-Smc6 DNA repair complex. bridging of the Smc5-Smc6 heads by the KLEISIN, Nse4, and non-Kleisin subunits
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M608004200
– volume: 65
  start-page: 861
  year: 2017
  ident: 2021070811582426900_B61
  article-title: Tuned SMC arms drive chromosomal loading of prokaryotic condensin
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2017.01.026
– volume: 124
  start-page: 4028
  year: 2014
  ident: 2021070811582426900_B17
  article-title: Hypomorphism in human NSMCE2 linked to primordial dwarfism and insulin resistance
  publication-title: J. Clin. Invest.
  doi: 10.1172/JCI73264
– volume: 65
  start-page: 849
  year: 2009
  ident: 2021070811582426900_B44
  article-title: Purification, crystallization and preliminary X-ray crystallographic studies of the complex between Smc5 and the SUMO E3 ligase Mms21
  publication-title: Acta Crystallogr. F Struct. Biol. Cryst. Commun.
  doi: 10.1107/S1744309109027900
– volume: 92
  start-page: e00825-18
  year: 2018
  ident: 2021070811582426900_B14
  article-title: PJA1 coordinates with the SMC5/6 complex to restrict DNA viruses and episomal genes in an interferon-independent manner
  publication-title: J. Virol.
  doi: 10.1128/JVI.00825-18
– volume: 126
  start-page: 2881
  year: 2016
  ident: 2021070811582426900_B18
  article-title: Destabilized SMC5/6 complex leads to chromosome breakage syndrome with severe lung disease
  publication-title: J. Clin. Invest.
  doi: 10.1172/JCI82890
– volume: 368
  start-page: 1454
  year: 2020
  ident: 2021070811582426900_B60
  article-title: Cryo-EM structure of the human cohesin-NIPBL-DNA complex
  publication-title: Science
  doi: 10.1126/science.abb0981
– volume: 531
  start-page: 386
  year: 2016
  ident: 2021070811582426900_B12
  article-title: Hepatitis B virus X protein identifies the Smc5/6 complex as a host restriction factor
  publication-title: Nature
  doi: 10.1038/nature17170
– volume: 286
  start-page: 26250
  year: 2011
  ident: 2021070811582426900_B66
  article-title: Rtt107 is required for recruitment of the SMC5/6 complex to DNA double strand breaks
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M111.235200
– ident: 2021070811582426900_B42
  article-title: The PyMOL Molecular Graphics System, Version 2.0
– volume: 287
  start-page: 9137
  year: 2012
  ident: 2021070811582426900_B67
  article-title: Structure of C-terminal tandem BRCT repeats of Rtt107 protein reveals critical role in interaction with phosphorylated histone H2A during DNA damage repair
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M111.311860
– volume: 278
  start-page: 34555
  year: 2003
  ident: 2021070811582426900_B47
  article-title: Insights into the conformational equilibria of maltose-binding protein by analysis of high affinity mutants
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M301004200
– year: 2021
  ident: 2021070811582426900_B25
  article-title: Live-cell single-molecule tracking highlights requirements for stable Smc5/6 chromatin association in vivo
  doi: 10.7554/eLife.68579.sa2
– volume: 3
  start-page: 182
  year: 2014
  ident: 2021070811582426900_B36
  article-title: The biotechnological applications of recombinant single-domain antibodies are optimized by the C-terminal fusion to the EPEA sequence (C Tag)
  publication-title: Antibodies
  doi: 10.3390/antib3020182
– volume: 171
  start-page: 457
  year: 2005
  ident: 2021070811582426900_B29
  article-title: Brc1-mediated DNA repair and damage tolerance
  publication-title: Genetics
  doi: 10.1534/genetics.105.044966
– volume: 3
  start-page: 373
  year: 2008
  ident: 2021070811582426900_B37
  article-title: HaloTag: a novel protein labeling technology for cell imaging and protein analysis
  publication-title: ACS Chem. Biol.
  doi: 10.1021/cb800025k
– volume: 9
  start-page: 786
  year: 2020
  ident: 2021070811582426900_B16
  article-title: The SMC5/6 complex represses the replicative program of high-risk human Papillomavirus type 31
  publication-title: Pathogens
  doi: 10.3390/pathogens9100786
– volume: 10
  start-page: 2905
  year: 1999
  ident: 2021070811582426900_B28
  article-title: Rad18 is required for DNA repair and checkpoint responses in fission yeast
  publication-title: Mol. Biol. Cell
  doi: 10.1091/mbc.10.9.2905
– volume: 1266
  start-page: 171
  year: 2015
  ident: 2021070811582426900_B35
  article-title: Site-specific biotinylation of purified proteins using BirA
  publication-title: Methods Mol. Biol.
  doi: 10.1007/978-1-4939-2272-7_12
– volume: 505
  start-page: 367
  year: 2014
  ident: 2021070811582426900_B51
  article-title: Biochemical reconstitution of topological DNA binding by the cohesin ring
  publication-title: Nature
  doi: 10.1038/nature12867
– volume: 39
  start-page: 300
  year: 2010
  ident: 2021070811582426900_B27
  article-title: DNA damage signaling recruits the Rtt107-Slx4 scaffolds via Dpb11 to mediate replication stress response
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2010.06.019
– volume: 28
  start-page: R1266
  year: 2018
  ident: 2021070811582426900_B5
  article-title: Towards a unified model of SMC complex function
  publication-title: Curr. Biol.
  doi: 10.1016/j.cub.2018.08.034
– volume: 9
  start-page: 581
  year: 2018
  ident: 2021070811582426900_B24
  article-title: The emerging role of cohesin in the DNA damage response
  publication-title: Genes
  doi: 10.3390/genes9120581
– volume: 52
  start-page: 89
  year: 2018
  ident: 2021070811582426900_B8
  article-title: The Smc5/6 complex: new and old functions of the enigmatic long-distance relative
  publication-title: Annu. Rev. Genet.
  doi: 10.1146/annurev-genet-120417-031353
– volume: 27
  start-page: 743
  year: 2020
  ident: 2021070811582426900_B59
  article-title: Cryo-EM structures of holo condensin reveal a subunit flip-flop mechanism
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/s41594-020-0457-x
– volume: 44
  start-page: 1064
  year: 2016
  ident: 2021070811582426900_B69
  article-title: Chromatin association of the SMC5/6 complex is dependent on binding of its NSE3 subunit to DNA
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkv1021
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Snippet Abstract The multi-component Smc5/6 complex plays a critical role in the resolution of recombination intermediates formed during mitosis and meiosis, and in...
The multi-component Smc5/6 complex plays a critical role in the resolution of recombination intermediates formed during mitosis and meiosis, and in the...
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SubjectTerms Adenosine Triphosphatases - chemistry
Adenosine Triphosphatases - genetics
Adenosine Triphosphatases - metabolism
Cell Cycle Proteins - chemistry
Cell Cycle Proteins - genetics
Cell Cycle Proteins - metabolism
Cell Cycle Proteins - ultrastructure
Chromosomal Proteins, Non-Histone - chemistry
Chromosomal Proteins, Non-Histone - genetics
Chromosomal Proteins, Non-Histone - metabolism
Chromosomal Proteins, Non-Histone - ultrastructure
DNA - metabolism
Escherichia coli - metabolism
Genome Integrity, Repair and
Microscopy, Electron, Transmission
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Saccharomyces cerevisiae Proteins - ultrastructure
Title Nse5/6 is a negative regulator of the ATPase activity of the Smc5/6 complex
URI https://www.ncbi.nlm.nih.gov/pubmed/33849072
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https://pubmed.ncbi.nlm.nih.gov/PMC8096239
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