Abstract
A backbone model of a 10-subunit yeast RNA polymerase II has been derived from x-ray diffraction data extending to 3 angstroms resolution. All 10 subunits exhibit a high degree of identity with the corresponding human proteins, and 9 of the 10 subunits are conserved among the three eukaryotic RNA polymerases I, II, and III. Notable features of the model include a pair of jaws, formed by subunits Rpb1, Rpb5, and Rpb9, that appear to grip DNA downstream of the active center. A clamp on the DNA nearer the active center, formed by Rpb1, Rpb2, and Rpb6, may be locked in the closed position by RNA, accounting for the great stability of transcribing complexes. A pore in the protein complex beneath the active center may allow entry of substrates for polymerization and exit of the transcript during proofreading and passage through pause sites in the DNA.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Motifs
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Binding Sites
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Catalytic Domain
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Crystallization
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Crystallography, X-Ray
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DNA, Fungal / chemistry
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DNA, Fungal / metabolism
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Enzyme Stability
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Escherichia coli / enzymology
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Humans
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Models, Molecular*
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Protein Binding
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Protein Structure, Quaternary
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Protein Structure, Secondary
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RNA Polymerase II / chemistry*
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RNA Polymerase II / genetics
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RNA Polymerase II / metabolism
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RNA, Fungal / chemistry
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RNA, Fungal / metabolism
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RNA, Messenger / chemistry
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RNA, Messenger / metabolism
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Thermus / enzymology
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Transcription Factors / chemistry
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Transcription Factors / metabolism
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Transcription Factors, General*
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Transcription, Genetic*
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Transcriptional Elongation Factors*
Substances
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DNA, Fungal
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RNA, Fungal
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RNA, Messenger
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Transcription Factors
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Transcription Factors, General
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Transcriptional Elongation Factors
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transcription factor S-II
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RNA Polymerase II