1887

Abstract

HTA426, a thermophilic Gram-positive bacterium, feeds on inositol as its sole carbon source, and an gene cluster required for inositol catabolism has been postulated with reference to the genes in . The gene cluster of comprises two tandem operons induced in the presence of inositol; however, the mechanism underlying this induction remains unclear. is known to be involved in the regulation of encoding -inositol dehydrogenase, and its homologue in HTA426 was found two genes upstream of the first gene () of the gene cluster and was termed in . When was inactivated in , not only cellular -inositol dehydrogenase activity due to expression but also the transcription of the two operons became constitutive. IolQ was produced and purified as a C-terminal histidine (His)-tagged fusion protein in and subjected to an gel electrophoresis mobility shift assay to examine its DNA-binding property. It was observed that IolQ bound to the DNA fragments containing each of the two promoter regions and that DNA binding was antagonized by -inositol. Moreover, DNase I footprinting analyses identified two tandem binding sites of IolQ within each of the promoter regions. By comparing the sequences of the binding sites, a consensus sequence for IolQ binding was deduced to form a palindrome of 5′-RGWAAGCGCTTSCY-3′ (where R=A or G, W=A or T, S=G or C, and Y=C or T). IolQ functions as a transcriptional repressor regulating the induction of the two operons responding to -inositol.

Funding
This study was supported by the:
  • Japan Society for the Promotion of Science (Award KAKENHI (18H02128))
    • Principle Award Recipient: Ken-ichiYoshida
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2020-12-15
2024-04-25
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