The linker domain of the initiator DnaA contributes to its ATP binding and membrane association in E. coli chromosomal replication.

ABSTRACT: DnaA, the initiator of Escherichia coli chromosomal replication, has in its adenosine triphosphatase (ATPase) domain residues required for adenosine 5'-triphosphate (ATP) binding and membrane attachment. Here, we show that D118Q substitution in the DnaA linker domain, a domain known to be without major regulatory functions, influences ATP binding of DnaA and replication initiation in vivo. Although initiation defective by itself, overexpression of DnaA(D118Q) caused overinitiation of replication in dnaA46ts cells and prevented cell growth. The growth defect was rescued by overexpressing the initiation inhibitor, SeqA, indicating that the growth inhibition resulted from overinitiation. Small deletions within the linker showed another unexpected phenotype: cellular growth witho

SUBMITTER: Hou Y 

PROVIDER: S-EPMC9534497 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature