Novel selection for isoniazid (INH) resistance genes supports a role for NAD+-binding proteins in mycobacterial INH resistance.

ABSTRACT: The genetic basis of isoniazid (INH) resistance remains unknown for a significant proportion of clinical isolates. To identify genes which might confer resistance by detoxifying or sequestering INH, we transformed the Escherichia coli oxyR mutant, which is relatively sensitive to INH, with a Mycobacterium tuberculosis plasmid library and selected for INH-resistant clones. Three genes were identified and called ceo for their ability to complement the Escherichia coli oxyR mutant. ceoA was the previously identified M. tuberculosis glf gene, which encodes a 399-amino-acid NAD+- and flavin adenine dinucleotide-requiring enzyme responsible for catalyzing the conversion of UDP-galactopyranose to UDP-galactofuranose. The proteins encoded by the ceoBC pair were homologous with one another and with

SUBMITTER: Chen P 

PROVIDER: S-EPMC108635 | biostudies-literature | 1998 Nov

REPOSITORIES: biostudies-literature