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The primase DnaG of Escherichia coli requires the participation of the replicative helicase DnaB for optimal synthesis of primer RNA for lagging strand replication. However, previous studies had not determined whether the activation of the primase or its loading on the template was accomplished by a helicase-mediated structural alteration of the single-stranded DNA or by a direct physical interaction between the DnaB and the DnaG proteins. In this paper we present evidence supporting direct interaction between the two proteins. We have mapped the surfaces of interaction on both DnaG and DnaB and show further that mutations that reduce the physical interaction also cause a significant reduction in primer synthesis. Thus, the physical interaction reported here appears to be physiologically significant.
Footnotes
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↵ To whom reprint requests should be addressed.
-
Wolfgang K. Joklik, Duke University Medical Center, Durham, NC
-
Abbreviations: wt, wild type; GST, glutathione S-transferase, tr.BC3, truncated BC3; ssDNA, single-stranded DNA.
- Received July 2, 1996.
- Accepted September 3, 1996.
- Copyright © 1996, The National Academy of Sciences of the USA
Direct physical interaction between DnaG primase and DnaB
helicase of Escherichia coli is necessary for
optimal synthesis of primer RNA
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