Structures of transcription pre-initiation complex with TFIIH and Mediator

For the initiation of transcription, RNA polymerase II (Pol II) assembles with general transcription factors on promoter DNA to form the pre-initiation complex (PIC). Here we report cryo-electron microscopy structures of the Saccharomyces cerevisiae PIC and PIC–core Mediator complex at nominal resol...

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Veröffentlicht in:Nature (London) Jg. 551; H. 7679; S. 204 - 209
Hauptverfasser: Schilbach, S., Hantsche, M., Tegunov, D., Dienemann, C., Wigge, C., Urlaub, H., Cramer, P.
Format: Journal Article
Sprache:Englisch
Veröffentlicht: London Nature Publishing Group UK 09.11.2017
Nature Publishing Group
Schlagworte:
13/109
14/28
631/1647/296
631/337/572
631/45/147
631/535/1258/1259
631/92/607/1167
82/58
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Analysis
Brewer's yeast
Coordination compounds
Cryoelectron Microscopy
Deoxyribonucleic acid
DNA
DNA - chemistry
DNA - genetics
DNA - metabolism
DNA binding proteins
DNA repair
DNA-directed RNA polymerase
Electron microscopy
Genetic aspects
Genetic transcription
Homology
Humanities and Social Sciences
Identification and classification
Initiation complex
Kinases
Mediator Complex - chemistry
Mediator Complex - metabolism
Mediator Complex - ultrastructure
Microscopy
Models, Molecular
multidisciplinary
Observations
Open spaces
Phosphorylation
Promoter Regions, Genetic
Protein Binding
Protein Subunits - chemistry
Protein Subunits - metabolism
Proteins
Ribonucleic acid
RNA
RNA polymerase II
RNA Polymerase II - metabolism
Saccharomyces cerevisiae
Saccharomyces cerevisiae - chemistry
Saccharomyces cerevisiae - enzymology
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - ultrastructure
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - metabolism
Saccharomyces cerevisiae Proteins - ultrastructure
Science
Structure
Transcription (Genetics)
Transcription factors
Transcription Factors, TFII - chemistry
Transcription Factors, TFII - metabolism
Transcription Factors, TFII - ultrastructure
Transcription Initiation, Genetic
Yeast
Germany
ISSN:0028-0836, 1476-4687, 1476-4687
Online-Zugang:Volltext
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Abstract For the initiation of transcription, RNA polymerase II (Pol II) assembles with general transcription factors on promoter DNA to form the pre-initiation complex (PIC). Here we report cryo-electron microscopy structures of the Saccharomyces cerevisiae PIC and PIC–core Mediator complex at nominal resolutions of 4.7 Å and 5.8 Å, respectively. The structures reveal transcription factor IIH (TFIIH), and suggest how the core and kinase TFIIH modules function in the opening of promoter DNA and the phosphorylation of Pol II, respectively. The TFIIH core subunit Ssl2 (a homologue of human XPB) is positioned on downstream DNA by the ‘E-bridge’ helix in TFIIE, consistent with TFIIE-stimulated DNA opening. The TFIIH kinase module subunit Tfb3 (MAT1 in human) anchors the kinase Kin28 (CDK7), which is mobile in the PIC but preferentially located between the Mediator hook and shoulder in the PIC–core Mediator complex. Open spaces between the Mediator head and middle modules may allow access of the kinase to its substrate, the C-terminal domain of Pol II. Cryo-electron microscopy structures of the yeast pre-initiation complex (PIC) and its complex with core Mediator provide insights into the opening of promoter DNA and the initiation of transcription. TFIIH in the transcription pre-initiation complex To initiate gene transcription, RNA polymerase (Pol) II assembles with general transcription factors on promoter DNA to form the pre-initiation complex (PIC). Here, Patrick Cramer and colleagues describe cryo-electron microscopy structures of the yeast PIC and the PIC bound to the core Mediator (cMed) complex. The latter structure with the general coactivator Mediator has 46 factors, including all those that are essential for transcription initiation in yeast. The structures reveal the architecture of transcription factor IIH (TFIIH) and suggest how its 'core' and 'kinase' modules might function in promoter opening and Pol II phosphorylation, respectively.
AbstractList For the initiation of transcription, RNA polymerase II (Pol II) assembles with general transcription factors on promoter DNA to form the pre-initiation complex (PIC). Here we report cryo-electron microscopy structures of the Saccharomyces cerevisiae PIC and PIC-core Mediator complex at nominal resolutions of 4.7 Å and 5.8 Å, respectively. The structures reveal transcription factor IIH (TFIIH), and suggest how the core and kinase TFIIH modules function in the opening of promoter DNA and the phosphorylation of Pol II, respectively. The TFIIH core subunit Ssl2 (a homologue of human XPB) is positioned on downstream DNA by the 'E-bridge' helix in TFIIE, consistent with TFIIE-stimulated DNA opening. The TFIIH kinase module subunit Tfb3 (MAT1 in human) anchors the kinase Kin28 (CDK7), which is mobile in the PIC but preferentially located between the Mediator hook and shoulder in the PIC-core Mediator complex. Open spaces between the Mediator head and middle modules may allow access of the kinase to its substrate, the C-terminal domain of Pol II.
For the initiation of transcription, RNA polymerase II (Pol II) assembles with general transcription factors on promoter DNA to form the pre-initiation complex (PIC). Here we report cryo-electron microscopy structures of the Saccharomyces cerevisiae PIC and PIC–core Mediator complex at nominal resolutions of 4.7 Å and 5.8 Å, respectively. The structures reveal transcription factor IIH (TFIIH), and suggest how the core and kinase TFIIH modules function in the opening of promoter DNA and the phosphorylation of Pol II, respectively. The TFIIH core subunit Ssl2 (a homologue of human XPB) is positioned on downstream DNA by the ‘E-bridge’ helix in TFIIE, consistent with TFIIE-stimulated DNA opening. The TFIIH kinase module subunit Tfb3 (MAT1 in human) anchors the kinase Kin28 (CDK7), which is mobile in the PIC but preferentially located between the Mediator hook and shoulder in the PIC–core Mediator complex. Open spaces between the Mediator head and middle modules may allow access of the kinase to its substrate, the C-terminal domain of Pol II. Cryo-electron microscopy structures of the yeast pre-initiation complex (PIC) and its complex with core Mediator provide insights into the opening of promoter DNA and the initiation of transcription. TFIIH in the transcription pre-initiation complex To initiate gene transcription, RNA polymerase (Pol) II assembles with general transcription factors on promoter DNA to form the pre-initiation complex (PIC). Here, Patrick Cramer and colleagues describe cryo-electron microscopy structures of the yeast PIC and the PIC bound to the core Mediator (cMed) complex. The latter structure with the general coactivator Mediator has 46 factors, including all those that are essential for transcription initiation in yeast. The structures reveal the architecture of transcription factor IIH (TFIIH) and suggest how its 'core' and 'kinase' modules might function in promoter opening and Pol II phosphorylation, respectively.
For transcription initiation, RNA polymerase (Pol) II assembles with general transcription factors on promoter DNA to form the pre-initiation complex (PIC). We report cryo-EM structures of the yeast PIC and PIC-core Mediator (cMed) complex at nominal resolutions of 4.7 Å and 5.8 Å, respectively. The structures reveal TFIIH and suggest how the TFIIH modules ‘core’ and ‘kinase’ function in promoter opening and Pol II phosphorylation, respectively. The TFIIH core subunit Ssl2 (human XPB) is positioned on downstream DNA by the ‘E-bridge’ helix in TFIIE, consistent with TFIIE-stimulated DNA opening. The TFIIH kinase module subunit Tfb3 (human MAT1) anchors the kinase Kin28 (human Cdk7) that is mobile in the PIC but preferentially located between the Mediator hook and shoulder in the PIC-cMed complex. Open spaces between the Mediator head and middle modules may allow access of the kinase to its substrate, the C-terminal domain (CTD) of Pol II.
For the initiation of transcription, RNA polymerase II (Pol II) assembles with general transcription factors on promoter DNA to form the pre-initiation complex (PIC). Here we report cryo-electron microscopy structures of the Saccharomyces cerevisiae PIC and PIC-core Mediator complex at nominal resolutions of 4.7 Å and 5.8 Å, respectively. The structures reveal transcription factor IIH (TFIIH), and suggest how the core and kinase TFIIH modules function in the opening of promoter DNA and the phosphorylation of Pol II, respectively. The TFIIH core subunit Ssl2 (a homologue of human XPB) is positioned on downstream DNA by the 'E-bridge' helix in TFIIE, consistent with TFIIE-stimulated DNA opening. The TFIIH kinase module subunit Tfb3 (MAT1 in human) anchors the kinase Kin28 (CDK7), which is mobile in the PIC but preferentially located between the Mediator hook and shoulder in the PIC-core Mediator complex. Open spaces between the Mediator head and middle modules may allow access of the kinase to its substrate, the C-terminal domain of Pol II. Cryo-electron microscopy structures of the yeast pre-initiation complex (PIC) and its complex with core Mediator provide insights into the opening of promoter DNA and the initiation of transcription. TFIIH in the transcription pre-initiation complex To initiate gene transcription, RNA polymerase (Pol) II assembles with general transcription factors on promoter DNA to form the pre-initiation complex (PIC). Here, Patrick Cramer and colleagues describe cryo-electron microscopy structures of the yeast PIC and the PIC bound to the core Mediator (cMed) complex. The latter structure with the general coactivator Mediator has 46 factors, including all those that are essential for transcription initiation in yeast. The structures reveal the architecture of transcription factor IIH (TFIIH) and suggest how its 'core' and 'kinase' modules might function in promoter opening and Pol II phosphorylation, respectively.
For the initiation of transcription, RNA polymerase II (Pol II) assembles with general transcription factors on promoter DNA to form the pre-initiation complex (PIC). Here we report cryo-electron microscopy structures of the Saccharomyces cerevisiae PIC and PIC-core Mediator complex at nominal resolutions of 4.7 Å and 5.8 Å, respectively. The structures reveal transcription factor IIH (TFIIH), and suggest how the core and kinase TFIIH modules function in the opening of promoter DNA and the phosphorylation of Pol II, respectively. The TFIIH core subunit Ssl2 (a homologue of human XPB) is positioned on downstream DNA by the 'E-bridge' helix in TFIIE, consistent with TFIIE-stimulated DNA opening. The TFIIH kinase module subunit Tfb3 (MAT1 in human) anchors the kinase Kin28 (CDK7), which is mobile in the PIC but preferentially located between the Mediator hook and shoulder in the PIC-core Mediator complex. Open spaces between the Mediator head and middle modules may allow access of the kinase to its substrate, the C-terminal domain of Pol II.For the initiation of transcription, RNA polymerase II (Pol II) assembles with general transcription factors on promoter DNA to form the pre-initiation complex (PIC). Here we report cryo-electron microscopy structures of the Saccharomyces cerevisiae PIC and PIC-core Mediator complex at nominal resolutions of 4.7 Å and 5.8 Å, respectively. The structures reveal transcription factor IIH (TFIIH), and suggest how the core and kinase TFIIH modules function in the opening of promoter DNA and the phosphorylation of Pol II, respectively. The TFIIH core subunit Ssl2 (a homologue of human XPB) is positioned on downstream DNA by the 'E-bridge' helix in TFIIE, consistent with TFIIE-stimulated DNA opening. The TFIIH kinase module subunit Tfb3 (MAT1 in human) anchors the kinase Kin28 (CDK7), which is mobile in the PIC but preferentially located between the Mediator hook and shoulder in the PIC-core Mediator complex. Open spaces between the Mediator head and middle modules may allow access of the kinase to its substrate, the C-terminal domain of Pol II.
Audience Academic
Author Tegunov, D.
Cramer, P.
Wigge, C.
Hantsche, M.
Schilbach, S.
Dienemann, C.
Urlaub, H.
AuthorAffiliation 1 Max Planck Institute for Biophysical Chemistry, Department of Molecular Biology, Am Fassberg 11, 37077 Göttingen, Germany
AuthorAffiliation_xml – name: 1 Max Planck Institute for Biophysical Chemistry, Department of Molecular Biology, Am Fassberg 11, 37077 Göttingen, Germany
Author_xml – sequence: 1
  givenname: S.
  surname: Schilbach
  fullname: Schilbach, S.
  organization: Department of Molecular Biology, Max Planck Institute for Biophysical Chemistry
– sequence: 2
  givenname: M.
  surname: Hantsche
  fullname: Hantsche, M.
  organization: Department of Molecular Biology, Max Planck Institute for Biophysical Chemistry
– sequence: 3
  givenname: D.
  surname: Tegunov
  fullname: Tegunov, D.
  organization: Department of Molecular Biology, Max Planck Institute for Biophysical Chemistry
– sequence: 4
  givenname: C.
  surname: Dienemann
  fullname: Dienemann, C.
  organization: Department of Molecular Biology, Max Planck Institute for Biophysical Chemistry
– sequence: 5
  givenname: C.
  surname: Wigge
  fullname: Wigge, C.
  organization: Department of Molecular Biology, Max Planck Institute for Biophysical Chemistry
– sequence: 6
  givenname: H.
  surname: Urlaub
  fullname: Urlaub, H.
  organization: Department of Molecular Biology, Max Planck Institute for Biophysical Chemistry, University Medical Center Göttingen, Institute of Clinical Chemistry, Bioanalytics Group
– sequence: 7
  givenname: P.
  surname: Cramer
  fullname: Cramer, P.
  email: patrick.cramer@mpibpc.mpg.de
  organization: Department of Molecular Biology, Max Planck Institute for Biophysical Chemistry
BackLink https://www.ncbi.nlm.nih.gov/pubmed/29088706$$D View this record in MEDLINE/PubMed
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Copyright Macmillan Publishers Limited, part of Springer Nature. All rights reserved. 2017
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  start-page: 7
  year: 2015
  ident: BFnature24282_CR62
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.3213
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Snippet For the initiation of transcription, RNA polymerase II (Pol II) assembles with general transcription factors on promoter DNA to form the pre-initiation complex...
For transcription initiation, RNA polymerase (Pol) II assembles with general transcription factors on promoter DNA to form the pre-initiation complex (PIC). We...
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StartPage 204
SubjectTerms 13/109
14/28
631/1647/296
631/337/572
631/45/147
631/535/1258/1259
631/92/607/1167
82/58
82/80
82/83
Analysis
Brewer's yeast
Coordination compounds
Cryoelectron Microscopy
Deoxyribonucleic acid
DNA
DNA - chemistry
DNA - genetics
DNA - metabolism
DNA binding proteins
DNA repair
DNA-directed RNA polymerase
Electron microscopy
Genetic aspects
Genetic transcription
Homology
Humanities and Social Sciences
Identification and classification
Initiation complex
Kinases
Mediator Complex - chemistry
Mediator Complex - metabolism
Mediator Complex - ultrastructure
Microscopy
Models, Molecular
multidisciplinary
Observations
Open spaces
Phosphorylation
Promoter Regions, Genetic
Protein Binding
Protein Subunits - chemistry
Protein Subunits - metabolism
Proteins
Ribonucleic acid
RNA
RNA polymerase II
RNA Polymerase II - metabolism
Saccharomyces cerevisiae
Saccharomyces cerevisiae - chemistry
Saccharomyces cerevisiae - enzymology
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - ultrastructure
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - metabolism
Saccharomyces cerevisiae Proteins - ultrastructure
Science
Structure
Transcription (Genetics)
Transcription factors
Transcription Factors, TFII - chemistry
Transcription Factors, TFII - metabolism
Transcription Factors, TFII - ultrastructure
Transcription Initiation, Genetic
Yeast
Title Structures of transcription pre-initiation complex with TFIIH and Mediator
URI https://link.springer.com/article/10.1038/nature24282
https://www.ncbi.nlm.nih.gov/pubmed/29088706
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https://pubmed.ncbi.nlm.nih.gov/PMC6078178
Volume 551
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