Characterization of an endonuclease associated with the drug resistance plasmid pKM101.

Abstract:

:An endonuclease was detected in strains of Salmonella typhimurium containing the drug resistance plasmid pKM101. The enzyme was not detectable in strains lacking this plasmid, but it was present in strains containing mutants of pKM101 that were no longer able to enhance host cell mutagenesis. The endonuclease had a molecular weight of roughly 75,000 and, at pH 7.0, was equally active on single-stranded and duplex deoxyribonucleic acid (DNA). The reaction with single-stranded DNA was optimal at pH 5.5, whereas with duplex DNA the optimum was pH 6.8. The enzyme required a divalent cation for activity, and it had no detectable exonuclease activity with single-stranded or duplex DNA. The endonuclease extensively degraded DNA with no apparent base specificity, forming 5'-phosphomonoester termini. Although characterization of the endonuclease has not revealed its function, the enzyme does not appear to be a restriction endonuclease.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Lackey D,Walker GC,Keng T,Linn S

doi

10.1128/JB.131.2.583-588.1977

subject

Has Abstract

pub_date

1977-08-01 00:00:00

pages

583-8

issue

2

eissn

0021-9193

issn

1098-5530

journal_volume

131

pub_type

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