Dynamic growth and shrinkage govern the pH dependence of RecA filament stability

Sung Hyun Kim, Jeehae Park, Chirlmin Joo, Doseok Kim, Taekjip Ha

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

RecA proteins form a long stable filament on a single-stranded DNA and catalyze strand exchange reaction. The stability of RecA filament changes dramatically with pH, yet its detailed mechanism is not known. Here, using a single molecule assay, we determined the binding and dissociation rates of RecA monomers at the filament ends at various pH. The pH-induced rate changes were moderate but occurred in opposite directions for binding and dissociation, resulting in a substantial increase in filament stability in lower pH. The highly charged residues in C-terminal domain do not contribute to the pH dependent stability. The stability enhancement of RecA filament in low pH may help the cell to cope with acidic stress by fine-tuning of the binding and dissociation rates without losing the highly dynamic nature of the filament required for strand exchange.

Original languageEnglish (US)
Article numbere0115611
JournalPloS one
Volume10
Issue number1
DOIs
StatePublished - Jan 21 2015
Externally publishedYes

ASJC Scopus subject areas

  • General

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