The MerR heavy metal receptor mediates positive activation in a topologically novel transcription complex

Thomas V. O'Halloran*, Betsy Frantz, Myung K. Shin, Diana M. Ralston, Jeffrey G. Wright

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

190 Scopus citations

Abstract

Several physical and chemical signals from the extracellular environment are known to be transduced into changes in gene expression through multiple step pathways; however, mechanisms for triggering cellular responses to heavy metal stress have yet to be elucidated. We demonstrate here one such mechanism that employs a single heavy metal receptor protein, MerR, to directly activate transcription of the bacterial mercuric ion resistance operon. The mercuric ion-MerR complex and E. coli RNA polymerase holoenzyme synergistically bind to the metal responsive promoter in an unprecedented spatial relationship to form transcriptionally competent complexes. The activator binds adjacent to and overlaps with the polymerase molecule between the consensus -35 and -10 promoter regions. Our results support a model for transcriptional activation that includes both effector-induced protein-protein interactions and activator-induced alteration in DNA structure.

Original languageEnglish (US)
Pages (from-to)119-129
Number of pages11
JournalCell
Volume56
Issue number1
DOIs
StatePublished - Jan 13 1989

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Fingerprint Dive into the research topics of 'The MerR heavy metal receptor mediates positive activation in a topologically novel transcription complex'. Together they form a unique fingerprint.

Cite this