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Cited by 161

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Structure of the RNA Polymerase Domain of E. coli Primase

Keck, James L., Roche, Daniel D., Lynch, A. Simon, Berger, James M.·2000·Science

Abstract

All cellular organisms use specialized RNA polymerases called “primases” to synthesize RNA primers for the initiation of DNA replication. The high-resolution crystal structure of a primase, comprising the catalytic core of the Escherichia coli DnaG protein, was determined. The core structure contains an active-site architecture that is unrelated to other DNA or RNA polymerase palm folds, but is instead related to the “toprim” fold. On the basis of the structure, it is likely that DnaG binds nucleic acid in a groove clustered with invariant residues and that DnaG is positioned within the replisome to accept single-stranded DNA directly from the replicative helicase.

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Metadata

Authors
Keck, J. L., Roche, D. D., Lynch, A. S., & Berger, J. M.
Venue
Science
Published
2000-03-31
Volume
287
Issue
5462
Pages
2482-2486
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2065857906
Cited by
161
References
2
FWCI
14.16
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Structure of the RNA Polymerase Domain of E. coli Primase. https://app.cochat.ai/papers/10.1126/science.287.5462.2482
The paper
Keck, J. L., Roche, D. D., Lynch, A. S., & Berger, J. M. (2000). Structure of the RNA Polymerase Domain of E. coli Primase. Science. https://doi.org/10.1126/science.287.5462.2482

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

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.