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MtrB from Bacillus subtilis binds specifically to trp leader RNA in a tryptophan-dependent manner

  • SUNY Buffalo

Research output: Contribution to journalArticlepeer-review

94 Scopus citations

Abstract

MtrB regulates transcription attenuation of the Bacillus subtilis trp operon. We have shown that MtrB, either from B. subtilis or overexpressed in Escherichia coli, binds specifically to RNA from the leader region of the trp operon by a gel mobility-shift assay. This binding is tryptophan dependent. MtrB binds to a transcript terminated at the trp attenuator (-2 to +138) or a read-through transcript (-2 to +318). MtrB does not bind antisense trp leader RNA or single-stranded trp leader DNA. These results support the model in which attenuation is controlled by tryptophan-activated MtrB influencing the secondary structure of the leader region transcript to form a terminator structure.

Original languageEnglish
Pages (from-to)128-132
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume90
Issue number1
StatePublished - Jan 1 1993

Keywords

  • RNA mobility-shift assay
  • RNA-binding protein
  • Transcription regulator

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