4.8 Article

Structure of the RNA polymerase domain of E-coli primase

Journal

SCIENCE
Volume 287, Issue 5462, Pages 2482-2486

Publisher

AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.287.5462.2482

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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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