Analysis of histidine-dependent antitermination in Bacillus subtilis hut operon | Zendy

Masayuki Oda | Zendy; Naoko Kobayashi | Zendy; Yasurou Kurusu | Zendy; Masaya Fujita | Zendy

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Analysis of histidine-dependent antitermination in Bacillus subtilis hut operon

Author(s) -

Masayuki Oda,

Naoko Kobayashi,

Yasurou Kurusu,

Masaya Fujita

Publication year - 2000

Publication title -

nucleic acids symposium series

Language(s) - English

Resource type - Journals

eISSN - 1746-8272

pISSN - 0261-3166

DOI - 10.1093/nass/44.1.5

Subject(s) - antitermination , operon , bacillus subtilis , histidine , transcription (linguistics) , biology , rna , binding site , response regulator , microbiology and biotechnology , transcription factor , biochemistry , chemistry , genetics , gene , bacteria , escherichia coli , amino acid , bacterial protein , linguistics , philosophy

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.

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