The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
Structural Basis of Transcription Initiation: An RNA Polymerase Holoenzyme-DNA Complex
Abstract
The crystal structure of Thermus aquaticus RNA polymerase holoenzyme (α 2 ββ′ωσ A ) complexed with a fork-junction promoter DNA fragment has been determined by fitting high-resolution x-ray structures of individual components into a 6.5-angstrom resolution map. The DNA lies across one face of the holoenzyme, completely outside the RNA polymerase active site channel. All sequence-specific contacts with core promoter elements are mediated by the σ subunit. A universally conserved tryptophan is ideally positioned to stack on the exposed face of the base pair at the upstream edge of the transcription bubble. Universally conserved basic residues of the σ subunit provide critical contacts with the DNA phosphate backbone and play a role in directing the melted DNA template strand into the RNA polymerase active site. The structure explains how holoenzyme recognizes promoters containing variably spaced –10 and –35 elements and provides the basis for models of the closed and open promoter complexes.
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Cites
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Structural Mechanism for Rifampicin Inhibition of Bacterial RNA Polymerase
Campbell, E. A., Korzheva, N., Mustaev, A., Murakami, K., Nair, S., Goldfarb, A., & Darst, S. A. (2001) · Cell · doi:10.1016/s0092-8674(01)00286-0 · Cited by 1,556
Self-citationLavery, R., & Sklenar, H. (1988) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.1988.10506483 · Cited by 894
The sigma 70 family: sequence conservation and evolutionary relationships
Lonetto, M., Gribskov, M., & Gross, C. A. (1992) · Journal of Bacteriology · doi:10.1128/jb.174.12.3843-3849.1992 · Cited by 888
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
Self-citationCarson, M. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891007240 · Cited by 808
Structural Basis of Transcription Initiation: RNA Polymerase Holoenzyme at 4 Å Resolution
Murakami, K. S., Masuda, S., & Darst, S. A. (2002) · Science · doi:10.1126/science.1069594 · Cited by 541
Self-citationStructure of the Bacterial RNA Polymerase Promoter Specificity σ Subunit
Campbell, E. A., Muzzin, O., Chlenov, M., Sun, J. L., Olson, C. A., Weinman, O., Trester-Zedlitz, M. L., & Darst, S. A. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00470-7 · Cited by 491
Self-citationThe Functional and Regulatory Roles of Sigma Factors in Transcription
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Cited by
The regulation of bacterial transcription initiation
Browning, D. F., & Busby, S. J. W. (2004) · Nature Reviews Microbiology · doi:10.1038/nrmicro787 · Cited by 1,019
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
rRNA Transcription in Escherichia coli
Paul, B. J., Ross, W., Gaal, T., & Gourse, R. L. (2004) · Annual Review of Genetics · doi:10.1146/annurev.genet.38.072902.091347 · Cited by 336
Advances in bacterial promoter recognition and its control by factors that do not bind DNA
Haugen, S. P., Ross, W., & Gourse, R. L. (2008) · Nature Reviews Microbiology · doi:10.1038/nrmicro1912 · Cited by 320
Kaplan, C. D., Larsson, K.-M., & Kornberg, R. D. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.04.023 · Cited by 246
Metadata
- Authors
- Murakami, K. S., Masuda, S., Campbell, E. A., Muzzin, O., & Darst, S. A.
- Venue
- Science
- Published
- 2002-05-17
- Volume
- 296
- Issue
- 5571
- Pages
- 1285-1290
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2143641256
- Cited by
- 641
- References
- 26
- FWCI
- 19.87
- Type
- journal article
- Language
- en
- Open access
- closed
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- Murakami, K. S., Masuda, S., Campbell, E. A., Muzzin, O., & Darst, S. A. (2002). Structural Basis of Transcription Initiation: An RNA Polymerase Holoenzyme-DNA Complex. Science. https://doi.org/10.1126/science.1069595
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
