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

Proc Natl Acad Sci U S A. 1993 Jan 1;90(1):128-32. doi: 10.1073/pnas.90.1.128.

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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Bacillus subtilis / drug effects
  • Bacillus subtilis / genetics*
  • Bacillus subtilis / metabolism*
  • Bacterial Proteins*
  • Cloning, Molecular
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli / genetics
  • Kinetics
  • Operon*
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism*
  • RNA-Binding Proteins / genetics
  • RNA-Binding Proteins / isolation & purification
  • RNA-Binding Proteins / metabolism*
  • Restriction Mapping
  • Saccharomyces cerevisiae / genetics
  • Substrate Specificity
  • Transcription Factors / genetics
  • Transcription Factors / isolation & purification
  • Transcription Factors / metabolism*
  • Transcription, Genetic
  • Tryptophan / genetics*
  • Tryptophan / pharmacology*

Substances

  • Bacterial Proteins
  • MtrB protein, Bacteria
  • RNA, Messenger
  • RNA-Binding Proteins
  • Transcription Factors
  • Tryptophan