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RAD54 N-terminal domain is a DNA sensor that couples ATP hydrolysis with branch migration of Holliday junctions
Journal article   Open access   Peer reviewed

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
Nature communications, v 9(1), pp 34-34
02 Jan 2018
DOI: https://doi.org/10.1038/s41467-017-02497-x
PMID: 29295984
Featured in Collection :   UN Sustainable Development Goals @ Drexel
url
https://doi.org/10.1038/s41467-017-02497-xView
Published, Version of Record (VoR)CC BY V4.0,  Open

Abstract

Adenosine Triphosphatases - metabolism Amino Acid Sequence Animals Binding Sites - genetics Cell Line DNA Helicases - chemistry DNA Helicases - genetics DNA Helicases - metabolism DNA Repair DNA, Cruciform - chemistry DNA, Cruciform - genetics DNA, Cruciform - metabolism Humans Hydrolysis Nuclear Proteins - chemistry Nuclear Proteins - genetics Nuclear Proteins - metabolism Nucleic Acid Conformation Phosphorylation Protein Multimerization Recombination, Genetic Sequence Homology, Amino Acid Sf9 Cells Spodoptera
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.

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25 citations in Web of Science
24 citations in Scopus

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Collaboration types
Domestic collaboration
Web of Science research areas
Biochemistry & Molecular Biology
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