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Annu Rev Biophys. 2019 May 6;48:255-273. doi: 10.1146/annurev-biophys-052118-115418. Epub 2019 Mar 11.

Helicase Mechanisms During Homologous Recombination in Saccharomyces cerevisiae.

Author information

1
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA; email: brookscrickard@gmail.com , ecg2108@cumc.columbia.edu.

Abstract

Helicases are enzymes that move, manage, and manipulate nucleic acids. They can be subdivided into six super families and are required for all aspects of nucleic acid metabolism. In general, all helicases function by converting the chemical energy stored in the bond between the gamma and beta phosphates of adenosine triphosphate into mechanical work, which results in the unidirectional movement of the helicase protein along one strand of a nucleic acid. The results of this translocation activity can range from separation of strands within duplex nucleic acids to the physical remodeling or removal of nucleoprotein complexes. In this review, we focus on describing key helicases from the model organism Saccharomyces cerevisiae that contribute to the regulation of homologous recombination, which is an essential DNA repair pathway for fixing damaged chromosomes.

KEYWORDS:

Rad54; Sgs1; Srs2; helicase; homologous recombination

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