The DOI matches its Crossref record; 73 of the 73 references it cites were found in a registry or an index.
Structure of Eukaryotic RNA Polymerases
Abstract
The eukaryotic RNA polymerases Pol I, Pol II, and Pol III are the central multiprotein machines that synthesize ribosomal, messenger, and transfer RNA, respectively. Here we provide a catalog of available structural information for these three enzymes. Most structural data have been accumulated for Pol II and its functional complexes. These studies have provided insights into many aspects of the transcription mechanism, including initiation at promoter DNA, elongation of the mRNA chain, tunability of the polymerase active site, which supports RNA synthesis and cleavage, and the response of Pol II to DNA lesions. Detailed structural studies of Pol I and Pol III were reported recently and showed that the active center region and core enzymes are similar to Pol II and that strong structural differences on the surfaces account for gene class-specific functions.
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Cites
Structural Basis of Transcription: RNA Polymerase II at 2.8 Ångstrom Resolution
Cramer, P., Bushnell, D. A., & Kornberg, R. D. (2001) · Science · doi:10.1126/science.1059493 · Cited by 1,247
Self-citationStructural Basis of Transcription: An RNA Polymerase II Elongation Complex at 3.3 Å Resolution
Gnatt, A. L., Cramer, P., Fu, J., Bushnell, D. A., & Kornberg, R. D. (2001) · Science · doi:10.1126/science.1059495 · Cited by 903
Self-citationCrystal 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
Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 Å resolution
Vassylyev, D. G., Sekine, S.-I., Laptenko, O., Lee, J., Vassylyeva, M. N., Borukhov, S., & Yokoyama, S. (2002) · Nature · doi:10.1038/nature752 · Cited by 743
Structural basis for phosphoserine-proline recognition by group IV WW domains.
Verdecia, M. A., Bowman, M. E., Lu, K. P., Hunter, T. R., & Noel, J. P. (2000) · Nature Structural Biology · doi:10.1038/77929 · Cited by 704
Recruitment of RNA polymerase III to its target promoters
Schramm, L., & Hernandez, N. (2002) · Genes & Development · doi:10.1101/gad.1018902 · Cited by 628
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-citationA mechanism for all polymerases
Steitz, T. A. (1998) · Nature · doi:10.1038/34542 · Cited by 596
RNA polymerase II and the integration of nuclear events
Hirose, Y., & Manley, J. L. (2000) · Genes & Development · doi:10.1101/gad.14.12.1415 · Cited by 575
Structure and mechanism of the RNA polymerase II transcription machinery
Hahn, S. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb763 · Cited by 547
Cited by
Evolution of multisubunit RNA polymerases in the three domains of life
Werner, F., & Grohmann, D. (2011) · Nature Reviews Microbiology · doi:10.1038/nrmicro2507 · Cited by 431
Conservation between the RNA Polymerase I, II, and III Transcription Initiation Machineries
Vannini, A., & Cramer, P. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.01.023 · Cited by 425
Self-citationTranscription termination and the control of the transcriptome: why, where and how to stop
Porrua, O., & Libri, D. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3943 · Cited by 324
RNA polymerase II–TFIIB structure and mechanism of transcription initiation
Kostrewa, D., Zeller, M. E., Armache, K.-J., Seizl, M., Leike, K., Thomm, M., & Cramer, P. (2009) · Nature · doi:10.1038/nature08548 · Cited by 317
Self-citationBernard, G., Chouery, E., Putorti, M. L., Tétreault, M., Takanohashi, A., Carosso, G., Clément, I., Boespflug-Tanguy, O., Rodriguez, D., Delague, V., et al. (2011) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2011.07.014 · Cited by 261
Metadata
- Authors
- Cramer, P., Armache, K.-J., Baumli, S., Benkert, S., Brueckner, F., Buchen, C., Damsma, G. E., Dengl, S., Geiger, S. R., Jasiak, A. J., Jawhari, A., Jennebach, S., Kamenski, T., Kettenberger, H., Kuhn, C.-D., Lehmann, E., Leike, K., Sydow, J. F., & Vannini, A.
- Venue
- Annual Review of Biophysics
- Publisher
- Annual Reviews
- Published
- 2008-06-01
- Volume
- 37
- Issue
- 1
- Pages
- 337-352
- ISSN
- 1936-122X (ISSN-L)
- 1936-1238
- OpenAlex
- W2164251316
- Cited by
- 304
- References
- 73
- FWCI
- 1.17
- Type
- journal article
- Language
- en
- Open access
- closed
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- Cramer, P., Armache, K.-J., Baumli, S., Benkert, S., Brueckner, F., Buchen, C., Damsma, G. E., Dengl, S., Geiger, S. R., Jasiak, A. J., Jawhari, A., Jennebach, S., Kamenski, T., Kettenberger, H., Kuhn, C.-D., Lehmann, E., Leike, K., Sydow, J. F., & Vannini, A. (2008). Structure of Eukaryotic RNA Polymerases. Annual Review of Biophysics. https://doi.org/10.1146/annurev.biophys.37.032807.130008
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