Escherichia coli PriA protein, two modes of DNA binding and activation of ATP hydrolysis

Taku Tanaka, Toshimi Mizukoshi, Kaori Tabata, Daisuke Kohda, Hisao Masai

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

Escherichia coli PriA protein plays crucial roles in processing of arrested replication forks. PriA serves as a sensor/stabilizer for an arrested replication fork and eventually promotes restart of DNA replication through assembly of a primosome. PriA carries a 3′ terminus binding pocket required for its high affinity binding to a specific arrested fork as well as for its biological functions. We show here that PriA binds to DNA in a manner either dependent on or independent of 3′ terminus recognition. The former mode of binding requires the 3′ terminus binding pocket present at the N-terminal half of the 181-residue DNA binding domain and exhibits specific bipartite interaction on the template DNA. The latter mode is independent of the pocket function, but requires the C-terminal half of the same domain. ATP hydrolysis activity of PriA can be stimulated in vitro by either of the two binding modes. We propose architecture of PriA bound to various arrested replication fork structures and discuss its implication in helicase activation and ATP hydrolysis.

Original languageEnglish
Pages (from-to)19917-19927
Number of pages11
JournalJournal of Biological Chemistry
Volume282
Issue number27
DOIs
Publication statusPublished - Jul 6 2007

All Science Journal Classification (ASJC) codes

  • Biochemistry

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