RAD54 N-terminal domain is a DNA sensor that couples ATP hydrolysis with branch migration of Holliday junctions

Nadish Goyal, Matthew J. Rossi, Olga M. Mazina, Yong Chi, Robert L. Moritz, Bruce E. Clurman and Alexander V. Mazin ()
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Nadish Goyal: Drexel University College of Medicine
Matthew J. Rossi: Drexel University College of Medicine
Olga M. Mazina: Drexel University College of Medicine
Yong Chi: Fred Hutchinson Cancer Research Center
Robert L. Moritz: Institute for Systems Biology
Bruce E. Clurman: Fred Hutchinson Cancer Research Center
Alexander V. Mazin: Drexel University College of Medicine

Nature Communications, 2018, vol. 9, issue 1, 1-10

Abstract: Abstract In eukaryotes, RAD54 catalyzes branch migration (BM) of Holliday junctions, a basic process during DNA repair, replication, and recombination. RAD54 also stimulates RAD51 recombinase and has other activities. Here, we investigate the structural determinants for different RAD54 activities. We find that the RAD54 N-terminal domain (NTD) is responsible for initiation of BM through two coupled, but distinct steps; specific binding to Holliday junctions and RAD54 oligomerization. Furthermore, we find that the RAD54 oligomeric state can be controlled by NTD phosphorylation at S49, a CDK2 consensus site, which inhibits RAD54 oligomerization and, consequently, BM. Importantly, the effect of phosphorylation on RAD54 oligomerization is specific for BM, as it does not affect stimulation of RAD51 recombinase by RAD54. Thus, the transition of the oligomeric states provides an important control of the biological functions of RAD54 and, likely, other multifunctional proteins.

Date: 2018
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DOI: 10.1038/s41467-017-02497-x

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