与耐药性质粒pKM101相关的一种核酸内切酶的特性分析。
Characterization of an endonuclease associated with the drug resistance plasmid pKM101.
作者信息
Lackey D, Walker G C, Keng T, Linn S
出版信息
J Bacteriol. 1977 Aug;131(2):583-8. doi: 10.1128/jb.131.2.583-588.1977.
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.
摘要
在含有耐药性质粒pKM101的鼠伤寒沙门氏菌菌株中检测到一种核酸内切酶。在缺乏该质粒的菌株中未检测到这种酶，但在含有不再能够增强宿主细胞诱变作用的pKM101突变体的菌株中存在该酶。该核酸内切酶的分子量约为75,000，在pH 7.0时，对单链和双链脱氧核糖核酸（DNA）具有同等活性。与单链DNA的反应在pH 5.5时最佳，而与双链DNA的最佳反应pH为6.8。该酶的活性需要二价阳离子，并且对单链或双链DNA均未检测到外切核酸酶活性。该核酸内切酶广泛降解DNA，没有明显的碱基特异性，形成5'-磷酸单酯末端。尽管对该核酸内切酶的表征尚未揭示其功能，但该酶似乎不是限制性核酸内切酶。
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