Solution structure of the helicase-interaction domain of the primase DnaG: a model for helicase activation.

ABSTRACT: 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 st

SUBMITTER: Syson K 

PROVIDER: S-EPMC3033578 | biostudies-literature | 2005 Apr

REPOSITORIES: biostudies-literature