Cited by 1,247Genomics and Chromatin DynamicsEnzyme Structure and FunctionProtein Structure and Dynamics

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Structural Basis of Transcription: RNA Polymerase II at 2.8 Ångstrom Resolution

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Cramer, Patrick, Bushnell, David A., Kornberg, Roger D.·2001·Science

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Abstract

Structures of a 10-subunit yeast RNA polymerase II have been derived from two crystal forms at 2.8 and 3.1 angstrom resolution. Comparison of the structures reveals a division of the polymerase into four mobile modules, including a clamp, shown previously to swing over the active center. In the 2.8 angstrom structure, the clamp is in an open state, allowing entry of straight promoter DNA for the initiation of transcription. Three loops extending from the clamp may play roles in RNA unwinding and DNA rewinding during transcription. A 2.8 angstrom difference Fourier map reveals two metal ions at the active site, one persistently bound and the other possibly exchangeable during RNA synthesis. The results also provide evidence for RNA exit in the vicinity of the carboxyl-terminal repeat domain, coupling synthesis to RNA processing by enzymes bound to this domain.

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Authors: Cramer, P., Bushnell, D. A., & Kornberg, R. D.
Affiliations: Stanford Medicine (US)
Corresponding author: Cramer, Patrick
Kornberg, Roger D.
ORCID: Cramer, Patrick
Kornberg, Roger D.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2001-06-08
Volume: 292
Issue: 5523
Pages: 1863-1876
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.1059493
OpenAlex: W2074206760
Cited by: 1,247
References: 71
Citations by year: 2026: 18 · 2025: 16 · 2024: 40 · 2023: 29 · 2022: 29 · 2021: 38 · 2020: 38 · 2019: 48 · 2018: 34 · 2017: 51 · 2016: 33 · 2015: 37 · 2014: 50 · 2013: 55 · 2012: 63
FWCI: 27.00
Type: journal article
Language: en
Open access: green
hdl.handle.net
Licence: other-oa
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Max Planck Digital Library (submittedVersion, other-oa)
GRO (submittedVersion)
MPG.PuRe (Max Planck Society) (submittedVersion, other-oa)
Funders: National Institute of General Medical Sciences (GM49985, R01GM049985)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords: RNA polymerase II, transcription initiation, active site metal ions, RNA unwinding, promoter DNA, crystal structure
MeSH terms: Amino Acid Sequence, Binding Sites, DNA, Fungal, Fourier Analysis, Hydrogen Bonding, Magnesium, Metals, Models, Molecular, Molecular Sequence Data, Promoter Regions, Genetic, Protein Conformation, RNA Polymerase II, RNA Processing, Post-Transcriptional, RNA, Fungal, RNA, Messenger, Saccharomyces cerevisiae, Transcription Factors, Transcription, Genetic, Conserved Sequence, Protein Structure, Secondary, Protein Structure, Tertiary, Crystallography, X-Ray, Protein Structure, Quaternary, Protein Subunits

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Structural Basis of Transcription: RNA Polymerase II at 2.8 Ångstrom Resolution

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