Analysis of isoniazid-resistant transposon mutants of Mycobacterium smegmatis.
The emergence of multidrug-resistant tuberculosis has renewed interest in the study of drug resistance in mycobacteria with the objective of improved chemotherapy. The genetic basis of isoniazid resistance in a model mycobacterium was studied. Eleven isoniazid-resistant mutants of Mycobacterium smegmatis were created using transposon mutagenesis. Genetic and enzymatic characterisation of the mutants showed that katG, encoding T-catalase, was inactivated. The nucleotide sequence of M. smegmatis katG was determined and the mutation sites mapped demonstrating that both the amino and carboxyl halves of T-catalase are important for enzymatic activity.
Billman-Jacobe
H
H
Department of Microbiology, Monash University, Clayton, Vic., Australia.
Sloan
J
J
Coppel
R L
RL
D001426:Bacterial Proteins; D002874:Chromosome Mapping; D004251:DNA Transposable Elements; D004352:Drug Resistance, Microbial / Q000235:genetics; D005819:Genetic Markers; D007538:Isoniazid / Q000494:pharmacology*; D016254:Mutagenesis, Insertional; D009154:Mutation; D009161:Mycobacterium / Q000187:drug effects* / Q000235:genetics*; D009195:Peroxidase / Q000032:analysis; D010544:Peroxidases / Q000235:genetics*; D016133:Polymerase Chain Reaction; D017422:Sequence Analysis, DNA
D001426:Bacterial Proteins; D004251:DNA Transposable Elements; D005819:Genetic Markers; D010544:Peroxidases; C076136:catalase HPI; D009195:Peroxidase; D007538:Isoniazid