Redβ177 annealase structure reveals details of oligomerization and λ Red-mediated homologous DNA recombination

Timothy P. Newing; Jodi L. Brewster; Lucy J. Fitschen; James C. Bouwer; Nikolas P. Johnston; Haibo Yu; Gökhan Tolun

doi:10.1038/s41467-022-33090-6

Nature Communications (Sep 2022)

Redβ177 annealase structure reveals details of oligomerization and λ Red-mediated homologous DNA recombination

Timothy P. Newing,
Jodi L. Brewster,
Lucy J. Fitschen,
James C. Bouwer,
Nikolas P. Johnston,
Haibo Yu,
Gökhan Tolun

Affiliations

Timothy P. Newing: School of Chemistry and Molecular Bioscience, and Molecular Horizons, University of Wollongong
Jodi L. Brewster: School of Chemistry and Molecular Bioscience, and Molecular Horizons, University of Wollongong
Lucy J. Fitschen: School of Chemistry and Molecular Bioscience, and Molecular Horizons, University of Wollongong
James C. Bouwer: School of Chemistry and Molecular Bioscience, and Molecular Horizons, University of Wollongong
Nikolas P. Johnston: School of Chemistry and Molecular Bioscience, and Molecular Horizons, University of Wollongong
Haibo Yu: School of Chemistry and Molecular Bioscience, and Molecular Horizons, University of Wollongong
Gökhan Tolun: School of Chemistry and Molecular Bioscience, and Molecular Horizons, University of Wollongong

DOI: https://doi.org/10.1038/s41467-022-33090-6
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 14

Abstract

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Redβ annealase catalyses single-strand annealing homologous DNA recombination. Here, the authors present a cryo-EM structure of a Redβ annealing intermediate bound to two complementary 27mer oligonucleotides.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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