Analysis of histidine-dependent antitermination in Bacillus subtilis hut operon.

M. Oda, Naoto Kobayashi, Y. Kurusu, M. Fujita

Research output: Contribution to journalArticle

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Abstract

We have previously shown that a positive regulator, HutP, of Bacillus subtilis hut operon is a RNA binding protein. Here, we report precise binding site of HutP in cis-regulatory region on hut mRNA and the role of HutP in histidine-dependent antitermination of hut expression. Ethylnitrosourea modification interference assay showed that four binding sites of HutP were found in the cis-regulatory sequences and were located at the stem and the internal loop of an antiterminator structure. In vitro transcription assay indicated that HutP suppressed transcription termination in the presence of histidine. These results suggest that HutP function as an antiterminator in response to the presence of histidine.

Original languageEnglish
Pages (from-to)5-6
Number of pages2
JournalNucleic acids symposium series
Issue number44
Publication statusPublished - 2000
Externally publishedYes

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Operon
Bacillus subtilis
Histidine
Binding Sites
Ethylnitrosourea
RNA-Binding Proteins
Nucleic Acid Regulatory Sequences
Messenger RNA

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Analysis of histidine-dependent antitermination in Bacillus subtilis hut operon. / Oda, M.; Kobayashi, Naoto; Kurusu, Y.; Fujita, M.

In: Nucleic acids symposium series, No. 44, 2000, p. 5-6.

Research output: Contribution to journalArticle

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