Second-site rho mutation: genetic linkage and polyC-dependent ATPase.
Rho has been purified to homogeneity from Escherichia coli double mutant rho-115 sur-38 cells, and from rho6 and rho-115 cells. The sur-38 mutation suppresses the original rho-115 phenotype. We observe that the polyC-dependent ATPases of these three rho preparations have the same specific activities. However, the ATPase of rho from the double rho-115 sur-38 mutant is extremely heat labile, while that from rho-115 shows a heat lability intermediate between the wild type and the double mutant. Transduction analysis suggests that sur-38 is closely linked to rho-115 in the order ilv--sur-38--rho-115--metE. These data are consistent with the model that the sur-38 mutation affects the structural gene for rho.
D000251:Adenosine Triphosphatases / Q000235:genetics*; D010582:Bacteriophage lambda / Q000235:genetics; D002874:Chromosome Mapping; D002876:Chromosomes, Bacterial; D004926:Escherichia coli / Q000235:genetics*; D005796:Genes; D006358:Hot Temperature; D009154:Mutation; D010641:Phenotype; D012234:Rho Factor; D014157:Transcription Factors; D014161:Transduction, Genetic
D012234:Rho Factor; D014157:Transcription Factors; D000251:Adenosine Triphosphatases