Action of RecBCD enzyme on Holliday structures made by RecA

In vitro, Escherichia coli RecA protein acts upon gapped and partially homologous linear duplex DNA to generate recombination products linked by Holliday junctions. When strand exchange reactions are supplemented with purified RecBCD enzyme, we observe the formation of products that resemble "p...

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Bibliographic Details
Published in:The Journal of biological chemistry 1991-10, Vol.266 (28), p.19028-19033
Main Authors: MÜLLER, B, BOEHMER, P. E, EMMERSON, P. T, WEST, S. C
Format: Article
Language:English
Subjects:
Biological and medical sciences
Crossing Over, Genetic
DNA - chemistry
DNA - metabolism
Escherichia coli - metabolism
Escherichia coli Proteins
Exodeoxyribonuclease V
Exodeoxyribonucleases - metabolism
Fundamental and applied biological sciences. Psychology
Genic rearrangement. Recombination. Transposable element
Molecular and cellular biology
Molecular genetics
Molecular Structure
Rec A Recombinases - chemistry
Rec A Recombinases - metabolism
Substrate Specificity
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Summary:In vitro, Escherichia coli RecA protein acts upon gapped and partially homologous linear duplex DNA to generate recombination products linked by Holliday junctions. When strand exchange reactions are supplemented with purified RecBCD enzyme, we observe the formation of products that resemble "patch" recombinants. The formation of "splice" recombinant products was not observed. The individual subunits, RecB, RecC, or RecD, had no effect on RecA protein-mediated strand exchange nor on the Holliday junctions formed in the reaction. Analysis of the way in which patch products arise indicates exonucleolytic digestion of the linear arms of the recombination intermediates (alpha-structures) by RecBCD enzyme. We find no evidence for specific resolution events at the site of the Holliday junction by RecBCD enzyme using these DNA substrates.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)55167-X