Isolation and characterization of autolysis-defective mutants of Escherichia coli that are resistant to the lytic activity of seminalplasmin.
Two temperature-sensitive autolysis-defective mutants of Escherichia coli were isolated and shown to be resistant to lysis induced by seminalplasmin, an antimicrobial protein from bovine seminal plasma, as well as to lysis induced by ampicillin, D-cycloserine and nocardicin, at 37 or 42 degrees C but not at 30 degrees C. The mutants were, however, sensitive to inhibition of RNA synthesis by seminalplasmin even at the nonpermissive temperature. Temperature-resistant revertants of the mutants were sensitive to lysis induced by the various antibiotics at 37 or 42 degrees C. The mutations in both strains were mapped at 58 min on the E. coli linkage map. The lysis resistance of the mutants was phenotypically suppressed by the addition of NaCl. Partial suppression of the lysis-resistant phenotype was also observed in a relA genetic background.
Centre for Cellular and Molecular Biology, Hyderabad, India.
S N
SN
Chitnis
K S
KS
Prasad
P M
PM
Bhargava
D000668:Ampicillin Resistance; D000900:Anti-Bacterial Agents / Q000494:pharmacology; D001329:Autolysis; D002874:Chromosome Mapping; D003523:Cycloserine / Q000494:pharmacology; D004251:DNA Transposable Elements; D004352:Drug Resistance, Microbial; D004926:Escherichia coli / Q000187:drug effects / Q000235:genetics* / Q000502:physiology; D007769:Lactams; D009154:Mutation; D010641:Phenotype; D011506:Proteins / Q000494:pharmacology*; D012329:RNA, Bacterial / Q000096:biosynthesis; D029607:Seminal Vesicle Secretory Proteins; D012965:Sodium Chloride / Q000494:pharmacology
D000900:Anti-Bacterial Agents; D004251:DNA Transposable Elements; D007769:Lactams; D011506:Proteins; D012329:RNA, Bacterial; D029607:Seminal Vesicle Secretory Proteins; D012965:Sodium Chloride; C027318:nocardicin; D003523:Cycloserine