Outer membrane proteins of Escherichia coli. VI. Protein alteration in bacteriophage-resistant mutants.
AUTOR(ES)
Bassford, P J
RESUMO
Protein 1 was shown to be the receptor for phage PA-2 by the observations that the purified protein inactivates the phage, mutants lacking the protein are resistant to the phage, and mutants selected for PA-2 resistance have altered protein. Protein 1 appears as two bands (1a and 1b) on high-resolution polyacrylamide gels. The most abundant classes of mutants (ParI and ParII) selected for PA-2 resistance were found to lack band 1b. The mutations responsible for the ParI and ParII phenotypes were mapped at a locus termed par, which is near nalA on the Escherichia coli chromosome. The cyanogen bromide peptides of proteins 1a and 1b are similar, suggesting that these bands represent modified forms of the same polypeptide. Strains carrying the tolF mutation produce only band 1b. When a par tolF double mutant was constructed, this strain produced only band 1a. These results suggest that genes at the par and tolF loci are involved in modification of protein 1, or regulation of such modification, and are not structural genes for protein 1.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=235470Documentos Relacionados
- Bacteriophage-Resistant Mutants in Escherichia Coli
- Bacteriophage-resistant mutants of Salmonella typhimurium deficient in two major outer membrane proteins.
- Further characterization of the recipient ability of Escherichia coli K-12 bacteriophage-resistant mutants.
- Lipopolysaccharide-deficient, bacteriophage-resistant mutants of Escherichia coli K-12.
- Recipient ability of bacteriophage-resistant mutants of Escherichia coli K-12.
