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

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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)


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


Dive into the research topics of 'Analysis of histidine-dependent antitermination in Bacillus subtilis hut operon.'. Together they form a unique fingerprint.

Cite this