Mutations that detoxify an aberrant T4 membrane protein.
Mutations that detoxify an aberrant T4 membrane protein.
复制标题
使异常 T4 膜蛋白解毒的突变。
DOI：
10.1016/0022-2836(81)90478-2
复制
发表时间：
1981
影响因子：
5.6
通讯作者：
Pribnow,D
中科院分区：
文献类型：
--
作者：
Nelson,MA;Singer,BS;Gold,L;Pribnow,D
我们研究了由 rIIB 移码突变 FC238 编码的噬菌体 T4 rIIB 毒性多肽的抑制剂。我们发现了抑制因子，它们通过产生新的翻译终止密码子来消除毒性多肽，通过改变毒性蛋白的氨基酸序列来减少多肽的毒性，改变rIIA蛋白以影响毒性，并通过减少rIIB (FC238)基因的基因表达量来减少毒性多肽的量。我们认为FC238多肽的毒性源于其独特的二分结构和高膜亲合力。通过错义解毒 FC238 多肽的抑制剂可能会干扰二分结构和/或膜的亲和力。用各种诱变剂获得的过渡突变的分布有助于了解内在的突变性差异。最后，尽管 FC238 毒性的抑制因子可能出现在除 rIIB 和 rIIA 之外的噬菌体基因中，但尚未发现。
We have investigated suppressors of the bacteriophage T4 rIIB toxic polypeptide encoded by the rIIB frameshift mutation FC238. We have found suppressors that eliminate the toxic polypeptide by creating new translational termination codons, that diminish the toxicity of the polypeptide by altering the amino acid sequence of the toxic protein, that alter the rIIA protein so as to influence toxicity, and that diminish the amount of toxic polypeptide by reducing the quantity of gene expression from the rIIB (FC238) gene. We propose that the toxicity of the FC238 polypeptide derives from its peculiar, bipartite structure and high membrane avidity. Suppressors that detoxify the FC238 polypeptide by missense probably disturb the bipartite structure and/or the affinity for the membrane. The distribution of transition mutations obtained with a variety of mutagens contributes to an appreciation of intrinsic mutability differences. Lastly, although suppressors of FC238 toxicity might emerge in phage genes other than rIIB and rIIA, none have been found.