Tessman E S, Peterson P K
J Virol. 1976 Nov;20(2):400-12. doi: 10.1128/JVI.20.2.400-412.1976.
Several related mutants of Escherichia coli C have been isolated that block the growth of the small icosahedral DNA phages phiX174 and S13 late in infection. Phage G6 is also blocked, at a stage not yet known. Growth of the filamentous phage M13, though not blocked, is affected in these strains. These host mutations co-transduce with ilv at high frequency, as do rep- mutations. However, the new mutants, designated groL-, differ from previously studied rep- mutants in that they permit synthesis of progeny replicative-form DNA. The groL- mutants are blocked in synthesis of stable single-stranded DNA of phiX174 and related phages. They are gro+ for P2. Evidence that groL- mutations and rep- mutations are in the same gene is presented. Spontaneous mutants (ogr) of phiX174, S13, and the G phages can grow on groL- strains. The ogr mutations are located in the phage's major capsid gene, F, as determined by complementation tests. There are numerous sites for mutation to ogr. Some mutations in genes A and F interfere with the ogr property when combined with an ogr mutation on the same genome. The ogr mutations are cis acting in a groL- cell; i.e., an ogr mutant gives very poor rescue of a non-ogr mutant. The wild-type form of each G phage appears to be naturally in the ogr mutant state for one or more groL- strains. It is suggested that a complex between F and rep proteins is involved in phage maturation. The A protein appears to interact with this complex.
已分离出几种大肠杆菌C的相关突变体,这些突变体在感染后期阻断了小型二十面体DNA噬菌体φX174和S13的生长。噬菌体G6在一个尚不清楚的阶段也被阻断。丝状噬菌体M13的生长虽然未被阻断,但在这些菌株中受到影响。这些宿主突变与ilv高频共转导,rep-突变也是如此。然而,新的突变体,命名为groL-,与先前研究的rep-突变体不同,因为它们允许子代复制型DNA的合成。groL-突变体在φX174和相关噬菌体的稳定单链DNA合成中被阻断。它们对P2是gro+。本文提供了groL-突变和rep-突变位于同一基因的证据。φX174、S13和G噬菌体的自发突变体(ogr)可以在groL-菌株上生长。通过互补试验确定,ogr突变位于噬菌体的主要衣壳基因F中。有许多位点可突变为ogr。基因A和F中的一些突变与同一基因组上的ogr突变结合时会干扰ogr特性。ogr突变在groL-细胞中是顺式作用的;即,ogr突变体对非ogr突变体的拯救能力很差。每种G噬菌体的野生型形式似乎对一种或多种groL-菌株自然处于ogr突变状态。有人提出F蛋白和rep蛋白之间的复合物参与噬菌体成熟。A蛋白似乎与这种复合物相互作用。