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

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.

SUBMITTER: Kim SH

PROVIDER: S-EPMC4301630 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature

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

Kim Sung Hyun SH Park Jeehae J Joo Chirlmin C Kim Doseok D Ha Taekjip T

PloS one 20150121 1

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 filame ...[more]

PMID: 25608006

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