Non-enzymatic roles of human RAD51 at stalled replication forks

Jennifer M. Mason (), Yuen-Ling Chan, Ralph W. Weichselbaum and Douglas K. Bishop ()
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Jennifer M. Mason: University of Chicago
Yuen-Ling Chan: University of Chicago
Ralph W. Weichselbaum: University of Chicago
Douglas K. Bishop: University of Chicago

Nature Communications, 2019, vol. 10, issue 1, 1-11

Abstract: Abstract The central recombination enzyme RAD51 has been implicated in replication fork processing and restart in response to replication stress. Here, we use a separation-of-function allele of RAD51 that retains DNA binding, but not D-loop activity, to reveal mechanistic aspects of RAD51’s roles in the response to replication stress. Here, we find that cells lacking RAD51’s enzymatic activity protect replication forks from MRE11-dependent degradation, as expected from previous studies. Unexpectedly, we find that RAD51’s strand exchange activity is not required to convert stalled forks to a form that can be degraded by DNA2. Such conversion was shown previously to require replication fork regression, supporting a model in which fork regression depends on a non-enzymatic function of RAD51. We also show RAD51 promotes replication restart by both strand exchange-dependent and strand exchange-independent mechanisms.

Date: 2019
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DOI: 10.1038/s41467-019-12297-0

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