Analysis of isoniazid-resistant transposon mutants of Mycobacterium smegmatis

Helen Billman-Jacobe; Joan Sloan; Ross L. Coppel

doi:10.1016/0378-1097(96)00336-9

Analysis of isoniazid-resistant transposon mutants of Mycobacterium smegmatis

Helen Billman-Jacobe, Joan Sloan, Ross L. Coppel

Microbiology

Research output: Contribution to journal › Article › Research › peer-review

15 Citations (Scopus)

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.

Original language	English
Pages (from-to)	47-52
Number of pages	6
Journal	FEMS Microbiology Letters
Volume	144
Issue number	1
DOIs	https://doi.org/10.1016/0378-1097(96)00336-9
Publication status	Published - 15 Oct 1996

Keywords

catalase/peroxidase
isoniazid
katG
mycobacteria

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10.1016/0378-1097(96)00336-9

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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.",

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AU - Sloan, Joan

AU - Coppel, Ross L.

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Y1 - 1996/10/15

N2 - 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.

AB - 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.

KW - catalase/peroxidase

KW - isoniazid

KW - katG

KW - mycobacteria

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Analysis of isoniazid-resistant transposon mutants of Mycobacterium smegmatis

Abstract

Keywords

UN SDGs

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