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Dynamic Growth and Shrinkage Govern the pH Dependence of RecA Filament Stability

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

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.

Suggested Citation

  • Sung Hyun Kim & Jeehae Park & Chirlmin Joo & Doseok Kim & Taekjip Ha, 2015. "Dynamic Growth and Shrinkage Govern the pH Dependence of RecA Filament Stability," PLOS ONE, Public Library of Science, vol. 10(1), pages 1-8, January.
  • Handle: RePEc:plo:pone00:0115611
    DOI: 10.1371/journal.pone.0115611
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    References listed on IDEAS

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    1. Roberto Galletto & Ichiro Amitani & Ronald J. Baskin & Stephen C. Kowalczykowski, 2006. "Direct observation of individual RecA filaments assembling on single DNA molecules," Nature, Nature, vol. 443(7113), pages 875-878, October.
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