Journal
STRUCTURE
Volume 13, Issue 4, Pages 609-616Publisher
CELL PRESS
DOI: 10.1016/j.str.2005.01.022
Keywords
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Funding
- Biotechnology and Biological Sciences Research Council [BB/E004717/1, C18024] Funding Source: Medline
- Biotechnology and Biological Sciences Research Council [C18024] Funding Source: researchfish
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The helicase-primase interaction is a critical event in DNA replication and is mediated by a putative helicase-interaction domain within the primase. The solution structure of the helicase-interaction domain of DnaG reveals that it is made up of two independent subdomains: an N-terminal six-helix module and a C-terminal two-helix module that contains the residues of the primase previously identified as important in the interaction with the helicase. We show that the two-helix module alone is sufficient for strong binding between the primase and the helicase but fails to activate the helicase; both subdomains are required for helicase activation. The six-helix module of the primase has only one close structural homolog, the N-terminal domain of the corresponding helicase. This surprising structural relationship, coupled with the differences in surface properties of the two molecules, suggests how the helicase-interaction domain may perturb the structure of the helicase and lead to activation.
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