Distinct mutation sites in prlA suppressor mutant strains of Escherichia coli respond either to suppression of signal peptide mutations or to blockage of staphylokinase processing.
We have cloned and sequenced some prlA mutant alleles of the Escherichia coli secY gene. From the mutation sites determined, it is strongly suggested that distinct regions in the SecY (PrlA) protein are involved in the recognition of different structural features of a signal peptide as it functions.
Sako
T
T
Yakult Central Institute for Microbiological Research, Tokyo, Japan.
Iino
T
T
D000483:Alleles; D001426:Bacterial Proteins / Q000235:genetics*; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics*; D005796:Genes; D005798:Genes, Bacterial; D008666:Metalloendopeptidases / Q000235:genetics*; D009154:Mutation; D011487:Protein Conformation; D013489:Suppression, Genetic
D001426:Bacterial Proteins; D008666:Metalloendopeptidases; C022653:auR protein, Staphylococcus aureus