NDLI: ATPase Mechanism of the 5′-3′ DNA Helicase, RecD2

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ATPase Mechanism of the 5′-3′ DNA Helicase, RecD2

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ATPase Mechanism of the 5′-3′ DNA Helicase, RecD2

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Toseland, Christopher P. Webb, Martin R.
Description	Author Affiliation: Toseland CP ( MRC National Institute for Medical Research, London, United Kingdom.)
Abstract	The superfamily 1 helicase, RecD2, is a monomeric, bacterial enzyme with a role in DNA repair, but with 5′-3′ activity unlike most enzymes from this superfamily. Rate constants were determined for steps within the ATPase cycle of RecD2 in the presence of ssDNA. The fluorescent ATP analog, mantATP (2′(3′)-O-(N-methylanthraniloyl)ATP), was used throughout to provide a complete set of rate constants and determine the mechanism of the cycle for a single nucleotide species. Fluorescence stopped-flow measurements were used to determine rate constants for adenosine nucleotide binding and release, quenched-flow measurements were used for the hydrolytic cleavage step, and the fluorescent phosphate biosensor was used for phosphate release kinetics. Some rate constants could also be measured using the natural substrate, ATP, and these suggested a similar mechanism to that obtained with mantATP. The data show that a rearrangement linked to $Mg^{2+}$ coordination, which occurs before the hydrolysis step, is rate-limiting in the cycle and that this step is greatly accelerated by bound DNA. This is also shown here for the PcrA 3′-5′ helicase and so may be a general mechanism governing superfamily 1 helicases. The mechanism accounts for the tight coupling between translocation and ATPase activity.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	35
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-08-30
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Adenosine Triphosphate Chemistry Bacterial Proteins DNA Helicases DNA, Bacterial DNA, Single-Stranded Deinococcus Enzymology Genetics Metabolism Hydrolysis Magnesium Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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