Conserved residues of the C-terminal p16 domain of primase are involved in modulating the activity of the bacterial primosome.

ABSTRACT: The bacterial primosome comprises the replicative homo-hexameric ring helicase DnaB and the primase DnaG. It is an integral component of the replisome as it unwinds the parental DNA duplex to allow progression of the replication fork, synthesizes the initiation primers at the replication origin, oriC, and the primers required for Okazaki fragment synthesis during lagging strand replication. The interaction between the two component proteins is mediated by a distinct C-terminal domain (p16) of the primase. Both proteins mutually regulate each other's activities and a putative network of conserved residues has been proposed to mediate these effects. We have targeted 10 residues from this network. To investigate the functional contributions of these residues to the primase, ATPase and helicas

SUBMITTER: Chintakayala K 

PROVIDER: S-EPMC3035050 | biostudies-literature | 2008 Apr

REPOSITORIES: biostudies-literature