蛋白质TraD的羧基末端增加了F质粒接合转移的特异性和效率。
The carboxyl terminus of protein TraD adds specificity and efficiency to F-plasmid conjugative transfer.
作者信息
Sastre J I, Cabezón E, de la Cruz F
机构信息
Department of Molecular Biology, University of Cantabria, 39011 Santander, Spain.
出版信息
J Bacteriol. 1998 Nov;180(22):6039-42. doi: 10.1128/JB.180.22.6039-6042.1998.
Abstract
We isolated and characterized traD mutants with an altered specificity of interaction with relaxosomes of various conjugative (F and R388) and mobilizable (RSF1010 and ColE1) plasmids. The change in specificity was due to a loss of some amino acids in the carboxyl terminus of TraD that resulted in a broadening of the range of mobilizable relaxosomes at the expense of a decrease in the efficiency of F-plasmid transfer.
摘要
我们分离并鉴定了traD突变体，其与各种接合型（F和R388）和可移动型（RSF1010和ColE1）质粒的松弛体相互作用的特异性发生了改变。特异性的变化是由于TraD羧基末端一些氨基酸的缺失，这导致可移动松弛体范围变宽，但以F质粒转移效率降低为代价。
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