Abstract
Rifampin-resistant mutants were isolated from Lactobacillus casei S1 and examined for possible simultaneous alteration in nutritional properties. Among the 36 mutants obtained either spontaneously or after mutagenesis with 2-aminopurine, 22 were found to be altered with respect to the specific growth requirements. The majority (20 of 22) of the latter mutants were shown to require L-glutamine in addition to the nutrients required by the parental strain for maximal growth, whereas the remaining mutants had apparently lost the requirement for L-aspartate. Further studies with one of the glutamine-requiring mutants revealed that the rifampin resistance of this strain is due to the resistance of ribonucleic acid polymerase itself and that a single mutation is responsible for both rifampin resistance and the glutamine requirement. These results strongly indicate that a structural alteration of the ribonucleic acid polymerase caused by the rifampin resistance mutation somehow affected glutamine metabolism, possibly through change in selective transcription of the genes involved.
MeSH Terms
2-Aminopurine
Carbohydrate Metabolism
Cell-Free System
DNA-Directed RNA Polymerases/biosynthesis,metabolism
Drug Resistance, Microbial
Fermentation
Glutamate-Ammonia Ligase/metabolism
Glutamine/metabolism
Lactobacillus casei/drug effects,enzymology,metabolism
Mutagens
Mutation
Rifampin/pharmacology
Stereoisomerism
Chemicals
Mutagens
Glutamine
2-Aminopurine
DNA-Directed RNA Polymerases
Glutamate-Ammonia Ligase
Rifampin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Morishita T
Yura T
References (15)
15 references, click to expand
-
Protein measurement with the Folin phenol reagent.
J Biol Chem. 1951 Nov;193(1):265-75
PMID: 14907713
-
Establishment of repression by lambdoid phage in catabolite activator protein and adenylate cyclase mutants of Escherichia coli.
Proc Natl Acad Sci U S A. 1972 Feb;69(2):366-70
PMID: 4333980
-
Structure and function of DNA-dependent RNA-polymerase.
Prog Biophys Mol Biol. 1971;23:67-101
PMID: 4400877
-
Adenosine 3':5'-cyclic monophosphate control of the enzymes of glutamine metabolism in Escherichia coli.
Proc Natl Acad Sci U S A. 1972 Oct;69(10):2922-6
PMID: 4404145
-
Rifamycins: a general view.
Annu Rev Microbiol. 1972;26:199-224
PMID: 4562808
-
An RNA polymerase mutant of Escherichia coli defective in the T4 viral transcription program.
Virology. 1972 Nov;50(2):396-403
PMID: 4564523
-
RNA polymerase mutants of Escherichia coli. Streptolydigin resistance and its relation to rifampicin resistance.
Mol Gen Genet. 1973 Mar 1;121(2):181-96
PMID: 4571524
-
RNA polymerase mutants blocked in sporulation.
Nature. 1970 Aug 29;227(5261):906-9
PMID: 4988656
-
RNA polymerase.
Annu Rev Biochem. 1971;40:711-40
PMID: 5001045
-
Actions of the rifamycins.
Bacteriol Rev. 1971 Sep;35(3):290-309
PMID: 5001420
-
Control of glutamine synthesis in Lactobacillus arabinosus.
Arch Biochem Biophys. 1965 Sep;111(3):720-6
PMID: 5862218
-
Comparative biochemical and immunological studies of bacterial glutamine synthetases.
J Bacteriol. 1973 Sep;115(3):858-68
PMID: 4125585
-
Genetic basis of nutritional requirements in Lactobacillus casei.
J Bacteriol. 1974 Dec;120(3):1078-84
PMID: 4215789
-
Adenosine 3':5'-cyclic monophosphate concentration in the bacterial host regulates the viral decision between lysogeny and lysis.
Proc Natl Acad Sci U S A. 1971 Sep;68(9):2258-62
PMID: 4332251
-
Cyclic AMP in prokaryotes.
Annu Rev Microbiol. 1974;28(0):353-69
PMID: 4372939