NDLI: Defective dissociation of a 'slow' RecA mutant protein imparts an Escherichia coli growth defect.

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Defective dissociation of a 'slow' RecA mutant protein imparts an Escherichia coli growth defect.

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Defective dissociation of a 'slow' RecA mutant protein imparts an Escherichia coli growth defect.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Inman, Ross B. Cox, Julia M. Chitteni-pattu, Sindhu Cox, Michael M. Li, Hao Wood, Elizabeth A.
Description	Author Affiliation: Cox JM ( Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706-1544, USA.)
Abstract	The RecA and some related proteins possess a simple motif, called (KR)X(KR), that (in RecA) consists of two lysine residues at positions 248 and 250 at the subunit-subunit interface. This study and previous work implicate this RecA motif in the following: (a) catalyzing ATP hydrolysis in trans,(b) coordinating the ATP hydrolytic cycles of adjacent subunits, (c) governing the rate of ATP hydrolysis, and (d) coupling the ATP hydrolysis to work (in this case DNA strand exchange). The conservative K250R mutation leaves RecA nucleoprotein filament formation largely intact. However, ATP hydrolysis is slowed to less than 15% of the wild-type rate. DNA strand exchange is also slowed commensurate with the rate of ATP hydrolysis. The results reinforce the idea of a tight coupling between ATP hydrolysis and DNA strand exchange. When a plasmid-borne RecA K250R protein is expressed in a cell otherwise lacking RecA protein, the growth of the cells is severely curtailed. The slow growth defect is alleviated in cells lacking RecFOR function, suggesting that the defect reflects loading of RecA at stalled replication forks. Suppressors occur as recA gene alterations, and their properties indicate that limited dissociation by RecA K250R confers the slow growth phenotype. Overall, the results suggest that recombinational DNA repair is a common occurrence in cells. RecA protein plays a sufficiently intimate role in the bacterial cell cycle that its properties can limit the growth rate of a bacterial culture.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	36
Volume Number	283
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2008-09-05
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Amino Acid Substitution Escherichia Coli Proteins Metabolism Escherichia Coli Growth & Development Mutation, Missense Rec A Recombinases Adenosine Triphosphate Genetics Amino Acid Motifs Catalytic Domain Cell Cycle DNA Repair DNA Replication DNA, Bacterial Enzymology Hydrolysis Research Support, N.I.H., Extramural Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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