Restart of DNA replication in Gram-positive bacteria: functional characterisation of the Bacillus subtilis PriA initiator

Nucleic Acids Research
Patrice PolardC Bruand

Abstract

The PriA protein was identified in Escherichia coli as a factor involved in the replication of extrachromosomal elements such as bacteriophage phiX174 and plasmid pBR322. Recent data show that PriA plays an important role in chromosomal replication, by promoting reassembly of the replication machinery during reinitiation of inactivated forks. A gene encoding a product 32% identical to the E.coli PriA protein has been identified in Bacillus subtilis. To characterise this protein, designated PriA(Bs), we constructed priA(Bs) mutants. These mutants are poorly viable, filamentous and sensitive to rich medium and UV irradiation. Replication of pAMbeta1-type plasmids, which is initiated through the formation of a D-loop structure, and the activity of the primosome assembly site ssiA of plasmid pAMbeta1 are strongly affected in the mutants. The purified PriA(Bs) protein binds preferentially to the active strand of ssiA, even in the presence of B.subtilis SSB protein (SSB(Bs)). PriA(Bs) also binds stably and specifically to an artificial D-loop structure in vitro. These data show that PriA(Bs) recognises two specific substrates, ssiA and D-loops, and suggest that it triggers primosome assembly on them. PriA(Bs) also displays a single-s...Continue Reading

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Citations

Nov 25, 2003·Nucleic Acids Research·Rajesh K SoniSuman Kumar Dhar
Jun 17, 2004·Nucleic Acids Research·Syam P Anand, Saleem A Khan
Nov 26, 2010·Journal of Bacteriology·Wiep Klaas SmitsAlan D Grossman
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Jun 24, 2021·Physical Chemistry Chemical Physics : PCCP·Tzu-Yu LeeHung-Wen Li

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