Analysis of isoniazid-resistant transposon mutants of Mycobacterium smegmatis.

Abstract

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.

• Authors: H Billman-Jacobe, J Sloan, R L Coppel
• Journal: FEMS microbiology letters (FEMS Microbiol Lett) Vol. 144 Issue 1 Pg. 47-52 (Oct 15 1996) ISSN: 0378-1097 [Print] England
• PMID: 8870251 (Publication Type: Comparative Study, Journal Article)

Chemical References

• Bacterial Proteins
• DNA Transposable Elements
• Genetic Markers
• Peroxidases
• catalase HPI
• Peroxidase
• Isoniazid

Topics

• Bacterial Proteins
• Chromosome Mapping
• DNA Transposable Elements
• Drug Resistance, Microbial (genetics)
• Genetic Markers
• Isoniazid (pharmacology)
• Mutagenesis, Insertional
• Mutation
• Mycobacterium (drug effects, genetics)
• Peroxidase (analysis)
• Peroxidases (genetics)
• Polymerase Chain Reaction
• Sequence Analysis, DNA