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

doi:10.1016/0092-8674(89)90990-2

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

Chemistry

Research output: Contribution to journal › Article › peer-review

224 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 language	English (US)
Pages (from-to)	119-129
Number of pages	11
Journal	Cell
Volume	56
Issue number	1
DOIs	https://doi.org/10.1016/0092-8674(89)90990-2
State	Published - Jan 13 1989

Funding

This work was supported by research grants from the National Instr-tutes of Health (GM-38784), the National Scrence Foundation Presr-dential Young lnvestrgator Award to T V 0, the General Electric Cor-poratron, and the Searle Scholars Program, The Chrcago Community Trust We acknowledge ARCS Foundatron Inc for a predoctoral scholarshrp to D. M. R. We thank Dr R Burgess and co-workers for generously supplyrng samples of E co11 RNA polymerase holoenzyme. core enzyme. and a”‘. We thank Dr. I. M. Klotz for helpful advice, M. Chael for helpful discussrons, and S Watton for expert assistance with artwork. We also thank Dr. T. Tull~us. R. Burgess, and P. Von Htppel for crrtical reading of the manuscrrpt The costs of publrcatron of thus article were defrayed rn part by the payment of page charges. Thrs article must therefore be hereby marked “adverhsement” in accordance wrth 18 U S.C Sectron 1734 solely to rndrcate this fact

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology

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10.1016/0092-8674(89)90990-2

Cite this

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title = "The MerR heavy metal receptor mediates positive activation in a topologically novel transcription complex",

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.",

author = "O'Halloran, {Thomas V.} and Betsy Frantz and Shin, {Myung K.} and Ralston, {Diana M.} and Wright, {Jeffrey G.}",

note = "Funding Information: This work was supported by research grants from the National Instr-tutes of Health (GM-38784), the National Scrence Foundation Presr-dential Young lnvestrgator Award to T V 0, the General Electric Cor-poratron, and the Searle Scholars Program, The Chrcago Community Trust We acknowledge ARCS Foundatron Inc for a predoctoral scholarshrp to D. M. R. We thank Dr R Burgess and co-workers for generously supplyrng samples of E co11 RNA polymerase holoenzyme. core enzyme. and a”{\textquoteleft}. We thank Dr. I. M. Klotz for helpful advice, M. Chael for helpful discussrons, and S Watton for expert assistance with artwork. We also thank Dr. T. Tull~us. R. Burgess, and P. Von Htppel for crrtical reading of the manuscrrpt The costs of publrcatron of thus article were defrayed rn part by the payment of page charges. Thrs article must therefore be hereby marked “adverhsement” in accordance wrth 18 U S.C Sectron 1734 solely to rndrcate this fact",

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AU - Wright, Jeffrey G.

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N2 - 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.

AB - 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.

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

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