RT Journal Article SR Electronic(1) A1 Schulp, J. A. A1 Stouthamer, A. H.YR 1972 T1 Isolation and Characterization of Mutants Resistant against Chlorate of Bacillus licheniformis JF Microbiology, VO 73 IS 1 SP 95 OP 112 DO https://doi.org/10.1099/00221287-73-1-95 PB Microbiology Society, SN 1465-2080, AB SUMMARY: From Bacillus licheniformis s244, 45 chl deletion mutants have been isolated which belong to six groups. In four groups the identity of the auxotrophic markers deleted has been established: his-2, ura-I, arg-3 and trp-I. Furthermore, a leu and a glu marker were found in the two other groups of deletion mutants. From B. licheniformis S1026, derived from strain ATCC9945A, 36 single site mutants were obtained and classified into eight groups, chl A to H, by transformation and phage SP 15-mediated transduction. The glu deletion comprises the mutations chl A and B. In total, 13 chl mutations have been found and there may be up to 13 chl genes. Of the single-site chl mutations, only chl E is linked with a known reference marker, ura-I. All chl mutants are unable to form nitrate reductase under conditions of oxygen shortage. This nitrate reductase is mainly associated with the cytoplasmic membrane. Most mutations have pleiotropic effects: (i) retarded growth under anaerobic conditions; (ii) an increased sensitivity to penicillin and related antibiotics; (iii) completely altered membrane protein patterns on acrylamide-SDS gels. In the wild-types, II membrane protein bands are observed. There are only small, quantitative differences between membrane protein patterns of cells cultivated aerobically or anaerobically. Membrane protein patterns of the chl mutants are most different from those of the wild-types after anaerobic cultivation. Differences include appearance of a new protein band, disappearances, decreases, doublings and often large increases of other protein bands. Aerobically, the mutants have membrane protein patterns less different from those of the wild-types. Differences include appearance of a new protein band, decrease and disappearance of protein bands. An explanation for all these changes may be a wholesale disorganization of protoplasmic membrane biosynthesis., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-73-1-95