Structure of the RNA polymerase domain of E. coli primase

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

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish (US)
Pages (from-to)2482-2486
Number of pages5
JournalScience
Volume287
Issue number5462
DOIs
StatePublished - Mar 31 2000
Externally publishedYes

ASJC Scopus subject areas

  • General

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