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Volume 158, Issue 8

Three inositol dehydrogenases involved in utilization and interconversion of inositol stereoisomers in a thermophile, HTA426 Free

Abstract

HTA426, a thermophilic -related species, utilizes some inositol stereoisomers, including -, -- and -inositols (MI, DCI and SI), as sole carbon sources. Within its genome are three paralogous genes that possibly encode inositol dehydrogenase. These genes are located in tandem within a large gene cluster containing an almost complete set of genes homologous to genes involved in inositol catabolism in . Each of the three plausible inositol dehydrogenases was purified as a His-tag fusion. The enzymes exhibited thermophilic activity, each with its own characteristic specificity for the inositol stereoisomers and cofactors. Northern blot and primer extension analyses revealed that the three enzymes were encoded by the same 5 kb polycistronic transcript and were induced simultaneously in the presence of MI. HTA426 was subjected to ethyl methanesulfonate (EMS) mutagenesis to isolate a mutant strain, PS8, which was not able to utilize MI. In PS8, inositol dehydrogenase activity was abolished along with the 5 kb transcript, suggesting that any of the three enzymes supports MI-dependent growth. Analysis of metabolites in HTA426 cells grown in the presence of MI revealed that substantial amounts of DCI and SI appeared intracellularly during the stationary phase, while only MI was present in PS8 cells, suggesting that interconversion of inositol stereoisomers may involve these three enzymes.

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  • Accepted:
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2012-08-01
2024-04-19
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Three inositol dehydrogenases involved in utilization and interconversion of inositol stereoisomers in a thermophile, Geobacillus kaustophilus HTA426
Microbiology 158, 1942 (2012); https://doi.org/10.1099/mic.0.059980-0
/content/journal/micro/10.1099/mic.0.059980-0
/content/journal/micro/10.1099/mic.0.059980-0
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