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- W2041517388 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." @default.
- W2041517388 created "2016-06-24" @default.
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- W2041517388 date "1974-12-01" @default.
- W2041517388 modified "2023-09-23" @default.
- W2041517388 title "Differential Thermolability of Exonuclease and Endonuclease Activities of the recBC Nuclease Isolated from Thermosensitive recB and recC Mutants" @default.
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- W2041517388 doi "https://doi.org/10.1128/jb.120.3.1219-1222.1974" @default.
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