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Science 31 March 2000:
Vol. 287. no. 5462, pp. 2482 - 2486
DOI: 10.1126/science.287.5462.2482
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Reports

Structure of the RNA Polymerase Domain of E. coli Primase

James L. Keck, 1 Daniel D. Roche, 2 A. Simon Lynch, 2* James M. Berger 1*

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.

1 Department of Molecular and Cell Biology, University of California, Berkeley, 229 Stanley Hall, no. 3206, Berkeley, CA 94720, USA.
2 Tularik, 2 Corporate Drive, South San Francisco, CA 94080, USA.
*   To whom correspondence should be addressed.

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