IS1转座酶的诱变：组氨酸-精氨酸-酪氨酸三联体对活性的重要性。
Mutagenesis of the IS1 transposase: importance of a His-Arg-Tyr triad for activity.
作者信息
Serre M C, Turlan C, Bortolin M, Chandler M
机构信息
Laboratoire de Microbiologie et Génétique Moléculaire, Centre National de la Recherche Scientifique, Toulouse, France.
出版信息
J Bacteriol. 1995 Sep;177(17):5070-7. doi: 10.1128/jb.177.17.5070-5077.1995.
Abstract
Inspection of the primary sequence of the IS1 transposase suggested that it carries residues which are characteristic of the active site of integrases of the bacteriophage lambda family (Int). In particular, these include a highly conserved triad: His-Arg-Tyr. The properties of mutants made at each of these positions were investigated in vivo. The results of several different assays confirm that each is important for transposase activity. Moreover, as in the case of members of the Int family, different mutations of the His residue exhibited different effects. In a particular, His-to-Leu mutation resulted in complete inactivation whereas the equivalent His-to-Gln mutation retained low but significant levels of activity.
摘要
对IS1转座酶一级序列的检查表明，它带有噬菌体λ家族整合酶（Int）活性位点所特有的残基。特别是，这些残基包括一个高度保守的三联体：组氨酸-精氨酸-酪氨酸。对在这些位置上产生的每个突变体的特性进行了体内研究。几种不同检测的结果证实，每个残基对转座酶活性都很重要。此外，与Int家族成员的情况一样，组氨酸残基的不同突变表现出不同的效应。特别是，组氨酸突变为亮氨酸导致完全失活，而等效的组氨酸突变为谷氨酰胺则保留了低但显著的活性水平。
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