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Structural Basis of Transcription: RNA Polymerase II at 2.8 Ångstrom Resolution
Open accessAbstract
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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“A short acidic peptide in the active site of cellular RNA polymerase binds Mg 2+ and positions it for catalysis (Zhang et al. 1999;Cramer et al. 2001).”
From Protocells and RNA Self-Replication (2018) · cites this paper as Cramer et al. 2001
In the citing paper
“RNA polymerase enzymes solve these problems by binding and precisely positioning the metal ion for catalysis (Zhang et al. 1999;Cramer et al. 2001;Robertson and Scott 2007;Shechner et al. 2009).”
From Protocells and RNA Self-Replication (2018) · cites this paper as Cramer et al. 2001
In the citing paper
“Interestingly, the multi-subunit cellular RNA polymerases also use two Mg 2+ ions in the active site, of which the more tightly bound ion is coordinated to three asp residues in a highly conserved NADFDGD peptide sequence [60,61].”
From The eightfold path to non-enzymatic RNA replication (2012) · cites this paper as [61]
Citations
Cites
Thompson, J. D., Higgins, D. G., & Gibson, T. J. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.22.4673 · Cited by 64,617
[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
The CCP4 suite: programs for protein crystallography
Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,317
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,011
Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,616
Nicholls, A. O., Sharp, K. A., & Honig, B. H. (1991) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340110407 · Cited by 5,230
An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
Esnouf, R. M. (1997) · Journal of Molecular Graphics and Modelling · doi:10.1016/s1093-3263(97)00021-1 · Cited by 1,703
Dali: a network tool for protein structure comparison
Holm, L., & Sander, C. (1995) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)89105-7 · Cited by 1,462
Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution
Doublié, S., Tabor, S., Long, A. M., Richardson, C. C., & Ellenberger, T. (1998) · Nature · doi:10.1038/34593 · Cited by 1,184
Beese, L. S., & Steitz, T. A. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07917.x · Cited by 1,059
The role of general initiation factors in transcription by RNA polymerase II
ROEDER, R. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)10050-5 · Cited by 1,009
Structural Basis of Transcription: An RNA Polymerase II Elongation Complex at 3.3 Å Resolution
Gnatt, A., Cramer, P., Fu, J.-L., Bushnell, D., & Kornberg, R. (2001) · Science · doi:10.1126/science.1059495 · Cited by 921
Self-citationTRANSCRIPTION OF EUKARYOTIC PROTEIN-CODING GENES
Lee, T. I., & Young, R. A. (2000) · Annual Review of Genetics · doi:10.1146/annurev.genet.34.1.77 · Cited by 889
Crystal Structure of Thermus aquaticus Core RNA Polymerase at 3.3 Å Resolution
Zhang, G., Campbell, E. A., Minakhin, L., Richter, C., Severinov, K., & Darst, S. A. (1999) · Cell · doi:10.1016/s0092-8674(00)81515-9 · Cited by 813
Architecture of RNA Polymerase II and Implications for the Transcription Mechanism
Cramer, P., Bushnell, D. A., Fu, J., Gnatt, A. L., Maier-Davis, B., Thompson, N. E., Burgess, R. R., Edwards, A. M., David, P. R., & Kornberg, R. D. (2000) · Science · doi:10.1126/science.288.5466.640 · Cited by 627
Self-citationPROTEIN-NUCLEIC ACID INTERACTIONS IN TRANSCRIPTION: A Molecular Analysis
von Hippel, P. H., Bear, D. G., Morgan, W. D., & McSwiggen, J. A. (1984) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.53.070184.002133 · Cited by 621
A mechanism for all polymerases
Steitz, T. A. (1998) · Nature · doi:10.1038/34542 · Cited by 611
Sawaya, M. R., Prasad, R., Wilson, S. H., Kraut, J., & Pelletier, H. (1997) · Biochemistry · doi:10.1021/bi9703812 · Cited by 593
RNA polymerase II and the integration of nuclear eventsPreprint
Hirose, Y., & Manley, J. L. (2000) · Genes & Development · doi:10.1101/gad.14.12.1415 · Cited by 577
Molchanov, V. N., & Simonov, V. I. (1998) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767398011465 · Cited by 548
Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal
Kiefer, J. R., Mao, C., Braman, J. C., & Beese, L. S. (1998) · Nature · doi:10.1038/34693 · Cited by 518
Carson, M. (1997) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(97)77027-7 · Cited by 510
Mediator of transcriptional regulation.
Myers, L., & Kornberg, R. (2000) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.69.1.729 · Cited by 466
Self-citationViral and cellular mRNA capping: Past and prospects
Furuichi, Y., & Shatkin, A. J. (2000) · Advances in virus research · doi:10.1016/s0065-3527(00)55003-9 · Cited by 408
A Structural Model of Transcription Elongation
Korzheva, N., MUSTAEV, A. A., Kozlov, M. V., Malhotra, A., Nikiforov, V., Goldfarb, A., & Darst, S. A. (2000) · Science · doi:10.1126/science.289.5479.619 · Cited by 402
Structure of a Transcribing T7 RNA Polymerase Initiation Complex
Cheetham, G. M. T., & Steitz, A. T. A. (1999) · Science · doi:10.1126/science.286.5448.2305 · Cited by 369
Prokaryotic and eukaryotic RNA polymerases have homologous core subunits.
Sweetser, D. B., Nonet, M. L., & Young, R. A. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.5.1192 · Cited by 354
Structural basis for initiation of transcription from an RNA polymerase–promoter complex
Cheetham, G. M. T., Jeruzalmi, D., & Steitz, T. A. (1999) · Nature · doi:10.1038/19999 · Cited by 346
Structure, mechanism, and evolution of the mRNA capping apparatus
Shuman, S. (2000) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(00)66025-7 · Cited by 289
Станиславович, М. Л., Bhagat, S., Brunning, A., Campbell, E. A., Darst, S. A., Ebright, R. H., & Severinov, K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.3.892 · Cited by 226
DNA- and RNA-dependent DNA polymerases
Steitz, T. A. (1993) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(93)90198-t · Cited by 220
Crystal structure of a thermostable type B DNA polymerase from Thermococcus gorgonarius
Hopfner, K., Eichinger, A., Engh, R. A., Laue, F., Ankenbauer, W., Huber, R., & Angerer, B. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3600 · Cited by 209
Analysis of the gene encoding the largest subunit of RNA polymerase II in Drosophila
Jokerst, R. S., Weeks, J. R., Zehring, W. A., & Greenleaf, A. L. (1989) · Molecular and General Genetics MGG · doi:10.1007/bf00339727 · Cited by 197
Structure of T7 RNA polymerase complexed to the transcriptional inhibitor T7 lysozyme
Jeruzalmi, D., & Steitz, T. A. (1998) · The EMBO Journal · doi:10.1093/emboj/17.14.4101 · Cited by 179
Connecting transcription to messenger RNA processing
Proudfoot, N. J. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01591-7 · Cited by 179
2.3 Å crystal structure of the catalytic domain of DNA polymerase β
Davies, J. F., Almassy, R. J., Hostomska, Z., Ferre, R. A., & Hostomský, Z. (1994) · Cell · doi:10.1016/0092-8674(94)90388-3 · Cited by 168
Pre-mRNA Processing and the CTD of RNA Polymerase II: The Tail That Wags the Dog?
Steinmetz, E. J. (1997) · Cell · doi:10.1016/s0092-8674(00)80230-5 · Cited by 166
Eukaryotic transcriptional control
Kornberg, R. D. (1999) · Trends in Genetics · doi:10.1016/s0168-9525(99)01901-0 · Cited by 147
Self-citationGenetic Interaction between Transcription Elongation Factor TFIIS and RNA Polymerase II
Archambault, J., Lacroute, F., Ruet, A., & Friesen, J. D. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.9.4142-4152.1992 · Cited by 139
Rodriguez, A. C., Park, H.-W., Mao, C., & Beese, L. S. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3728 · Cited by 137
Eukaryotic transcriptional control
Kornberg, R. D. (1999) · Trends in Cell Biology · doi:10.1016/s0962-8924(99)01679-7 · Cited by 136
Self-citationFunctional domains of transcription factor TFIIB.
Buratowski, S., & Zhou, H. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.12.5633 · Cited by 133
Yeast RNA Polymerase II at 5 Å Resolution
Fu, J., Gnatt, A. L., Bushnell, D. A., Jensen, G. J., Thompson, N. E., Burgess, R. R., David, P. R., & Kornberg, R. D. (1999) · Cell · doi:10.1016/s0092-8674(00)81514-7 · Cited by 128
Self-citationLeuther, K. K., Bushnell, D. A., & Kornberg, R. D. (1996) · Cell · doi:10.1016/s0092-8674(00)81242-8 · Cited by 114
Self-citationFunctional topography of nascent RNA in elongation intermediates of RNA polymerase
Komissarova, N. V., & Kashlev, M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.25.14699 · Cited by 110
RNA polymerase II subunit RPB9 is required for accurate start site selection.Preprint
Hull, M. W., McKune, K., & Woychik, N. A. (1995) · Genes & Development · doi:10.1101/gad.9.4.481 · Cited by 109
Interactions between three common subunits of yeast RNA polymerases I and III.
Lalo, D., Carles, C., Sentenac, A., & Thuriaux, P. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.12.5524 · Cited by 108
Factors regulating the transcriptional elongation activity of RNA polymerase II
Shilatifard, A. (1998) · The FASEB Journal · doi:10.1096/fasebj.12.14.1437 · Cited by 104
General Transcription Factors for RNA Polymerase II1
Conaway, R., & Conaway, J. W. (1997) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(08)61009-0 · Cited by 99
Transcription Elongation and Human Disease
Conaway, J. W., & Conaway, R. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.301 · Cited by 99
Bartolomei, M. S., & Corden, J. L. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.2.586 · Cited by 97
RNA Polymerase II Subunit Rpb9 Regulates Transcription Elongation in Vivo
Hemming, S. A., Jansma, D. B., Macgregor, P. F., Goryachev, A. B., Friesen, J. D., & Edwards, A. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004721200 · Cited by 94
Protein-RNA interactions in the active center of transcription elongation complex.
Markovtsov, V. V., MUSTAEV, A. A., & Goldfarb, A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.8.3221 · Cited by 91
Berroteran, R. W., Ware, D. E., & Hampsey, M. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.1.226 · Cited by 86
Werner, M., Denmat, S. H., Treich, I., Sentenac, A., & Thuriaux, P. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.3.1087 · Cited by 76
Spatial Organization of Transcription Elongation Complex in Escherichia coli
Nudler, E., Gusarov, I., Avetissova, E., Kozlov, M. V., & Goldfarb, A. (1998) · Science · doi:10.1126/science.281.5375.424 · Cited by 76
RNA Polymerase II Subunits 2, 3, and 11 Form a Core Subassembly with DNA Binding Activity
Kimura, M., Ishiguro, A., & Ishihama, A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.41.25851 · Cited by 74
Increased accommodation of nascent RNA in a product site on RNA polymerase II during arrest.
Gu, W., Wind, M., & Reines, D. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.14.6935 · Cited by 63
Wu, J., Awrey, D. E., Edwards, A. M., Archambault, J., & Friesen, J. D. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.21.11552 · Cited by 50
2 Yeast RNA Polymerase Subunits and GenesPreprint
Sentenac, A., Riva, M., Thuriaux, P., Buhler, J., Treich, I., Carles, C., Werner, M., Ruet, A., Huet, J., Mann, C., et al. (1992) · Cold Spring Harbor Monograph Archive · doi:10.1101/087969425.22a.27 · Cited by 50
Hekmatpanah, D. S., & Young, R. A. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.11.5781 · Cited by 48
Cagas, P., & Corden, J. L. (1995) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340210209 · Cited by 48
Selenomethionine Incorporation in Saccharomyces cerevisiae RNA Polymerase II
Bushnell, D. A., Cramer, P., & Kornberg, R. D. (2001) · Structure · doi:10.1016/s0969-2126(00)00554-2 · Cited by 42
Self-citationXiao, H., Friesen, J. D., & Lis, J. T. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.11.7507-7516.1994 · Cited by 36
Donaldson, I. M., & Friesen, J. D. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.18.13780 · Cited by 36
Rubbi, L., Mariotte, S., Chédin, S., & Thuriaux, P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.44.31485 · Cited by 36
Clustered α-amanitin resistance mutations in mouse
Bartolomei, M. S., & Corden, J. L. (1995) · Molecular and General Genetics MGG · doi:10.1007/bf00290727 · Cited by 31
Yeast RNA Polymerase II Subunit RPB9
Hemming, S. A., & Edwards, A. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.4.2288 · Cited by 31
Solution structure of the hRPABC14.4 subunit of human RNA polymerases.
Wagner, G., del Río‐Portilla, F., Gaskell, A., Gilbert, D. E., & Ladias, J. A. A. (1999) · Nature Structural Biology · doi:10.1038/14923 · Cited by 17
Geiduschek, E. P., & Bartlett, M. S. (2000) · Nature Structural Biology · doi:10.1038/75820 · Cited by 9
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Research works printed but not linked: 9
- 10.1016/0968-0004(96)10050-5 · DOI
- ; published online 19 April 2001 (10.1126/science.1059495). · DOI
- Werner M., Hermann-Le Denmat S., Treich I., Sentenac A., Thuriaux P., Mol. Cell. Biol. 12, 1087 (1992).
- Archambault J., Lacroute F., Ruet A., Friesen J. D., Mol. Cell. Biol. 12, 4142 (1992).
- ___, Mol. Cell. Biol. 7, 586 (1987).
- Berroteran R. W., Ware D. E., Hampsey M., Mol. Cell. Biol. 14, 226 (1994).
- Hekmatpanah D. S., Young R. A., Mol. Cell. Biol. 11, 5781 (1991).
- Xiao H., Friesen J. D., Lis J. T., Mol. Cell. Biol. 14, 7507 (1994).
- Cowtan K., Joint CCP4 ESF-EACBM Newslett. Protein Crystallogr. 31, 34 (1994).
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Self-citation
Metadata
- Authors
- Cramer, P., Bushnell, D. A., & Kornberg, R. D.
- Affiliations
- Stanford Medicine (US)
- Corresponding author
- Cramer, Patrick
- Kornberg, Roger D.
- Venue
- Science
- Published
- 2001-06-08
- Volume
- 292
- Issue
- 5523
- Pages
- 1863-1876
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- 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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