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

Journal article (2015)
Department
BN/Bionanoscience (AS) (TU Delft)
Copyright: This is an open access article distributed under the terms of the Creative Commons Attribution License
DOI: https://doi.org/doi:10.1371/journal.pone.0115611
More Info
expand_more

Published Date

21-01-2015

Reuse Rights

Other than for strictly personal use, it is not permitted to download, forward or distribute the text or part of it, without the consent of the author(s) and/or copyright holder(s), unless the work is under an open content license such as Creative Commons.

Source:

PLoS ONE, 10 (1), 2015

Faculty

Applied Sciences

Department

BN/Bionanoscience

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.

Files

Joo_2015.pdf
(pdf | 0.52 Mb)