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. 1974 Dec;120(3):1219–1222. doi: 10.1128/jb.120.3.1219-1222.1974

Differential Thermolability of Exonuclease and Endonuclease Activities of the recBC Nuclease Isolated from Thermosensitive recB and recC Mutants

Sidney R Kushner a,1
PMCID: PMC245903  PMID: 4612008

Abstract

The recBC nuclease (also called exonuclease V) has been partially purified from Escherichia coli K-12 strains carrying the thermosensitive recB270, recC271, and recB270 recC271 mutations. Of the multiple activities associated with the enzyme, only the adenosine 5′-triphosphate-dependent exonucleolytic hydrolysis of duplex deoxyribonucleic acid (DNA) is abnormally thermolabile. The exo- and endonucleolytic degradation of single-stranded DNA is no more thermosensitive than that catalyzed by the wild-type enzyme. These results suggest that the defects in genetic recombination, DNA repair, and the maintenance of cell viability observed in recBC mutants in vivo result primarily from the specific loss of adenosine 5′-triphosphate-dependent exonuclease active on duplex DNA.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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