Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Outten, C. E.
Right arrow Articles by O'Halloran, T. V.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Outten, C. E.
Right arrow Articles by O'Halloran, T. V.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J Biol Chem, Vol. 274, Issue 53, 37517-37524, December 31, 1999

DNA Distortion Mechanism for Transcriptional Activation by ZntR, a Zn(II)-responsive MerR Homologue in Escherichia coli*

Caryn E. OuttenDagger , F. Wayne Outten§, and Thomas V. O'HalloranDagger §

From the Dagger  Department of Chemistry and the § Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 60208

MerR-like DNA distortion mechanisms have been proposed for a variety of stress-responsive transcription factors. The Escherichia coli ZntR protein, a homologue of MerR, has recently been shown to mediate Zn(II)-responsive regulation of zntA, a gene involved in Zn(II) detoxification. To determine whether the MerR DNA distortion mechanism is conserved among MerR family members, we have purified ZntR to homogeneity and shown that it is a zinc receptor that is necessary and sufficient to stimulate Zn-responsive transcription at the zntA promoter. Biochemical, DNA footprinting, and in vitro transcription assays indicate that apo-ZntR binds in the atypical 20-base pair spacer region of the promoter and distorts the DNA in a manner that is similar to apo-MerR. The addition of Zn(II) to ZntR converts it to a transcriptional activator protein that introduces changes in the DNA conformation. These changes apparently make the promoter a better substrate for RNA polymerase. We propose that this zinc-sensing homologue of MerR restructures the target promoter in a manner similar to that of other stress-responsive transcription factors. The ZntR metalloregulatory protein is a direct Zn(II) sensor that catalyzes transcriptional activation of a zinc efflux gene, thus preventing intracellular Zn(II) from exceeding an optimal but as yet unknown concentration.


* This work was supported in part by National Institutes of Health Grants R01 GM38784 (to T. V. O.), and T32 GM08382 (to C. E. O.), and T32 GM08061 (to F. W. O.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Chemistry, Northwestern University, 2145 Sheridan Rd., Evanston, IL 60208. Tel.: 847-491-5060; Fax: 847-491-7713; E-mail: t-ohalloran@nwu.edu.


Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
J. Bacteriol.Home page
J. Collado-Vides, H. Salgado, E. Morett, S. Gama-Castro, V. Jimenez-Jacinto, I. Martinez-Flores, A. Medina-Rivera, L. Muniz-Rascado, M. Peralta-Gil, and A. Santos-Zavaleta
Bioinformatics Resources for the Study of Gene Regulation in Bacteria
J. Bacteriol., January 1, 2009; 191(1): 23 - 31.
[Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K. J. Newberry, J. L. Huffman, M. C. Miller, N. Vazquez-Laslop, A. A. Neyfakh, and R. G. Brennan
Structures of BmrR-Drug Complexes Reveal a Rigid Multidrug Binding Pocket and Transcription Activation through Tyrosine Expulsion
J. Biol. Chem., September 26, 2008; 283(39): 26795 - 26804.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
K. Helbig, C. Bleuel, G. J. Krauss, and D. H. Nies
Glutathione and Transition-Metal Homeostasis in Escherichia coli
J. Bacteriol., August 1, 2008; 190(15): 5431 - 5438.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
S. Watanabe, A. Kita, K. Kobayashi, and K. Miki
Crystal structure of the [2Fe-2S] oxidative-stress sensor SoxR bound to DNA
PNAS, March 18, 2008; 105(11): 4121 - 4126.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
A. A. Gorodetsky, L. E. P. Dietrich, P. E. Lee, B. Demple, D. K. Newman, and J. K. Barton
DNA binding shifts the redox potential of the transcription factor SoxR
PNAS, March 11, 2008; 105(10): 3684 - 3689.
[Abstract] [Full Text] [PDF]


Home page
MicrobiologyHome page
M. Espariz, S. K. Checa, M. E. P. Audero, L. B. Pontel, and F. C. Soncini
Dissecting the Salmonella response to copper
Microbiology, September 1, 2007; 153(9): 2989 - 2997.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
M. Pruteanu, S. B. Neher, and T. A. Baker
Ligand-Controlled Proteolysis of the Escherichia coli Transcriptional Regulator ZntR
J. Bacteriol., April 15, 2007; 189(8): 3017 - 3025.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
L. V. Wray Jr. and S. H. Fisher
Functional Analysis of the Carboxy-Terminal Region of Bacillus subtilis TnrA, a MerR Family Protein
J. Bacteriol., January 1, 2007; 189(1): 20 - 27.
[Abstract] [Full Text] [PDF]


Home page
MicrobiologyHome page
M. Ventura, J. G. Kenny, Z. Zhang, G. F. Fitzgerald, and D. van Sinderen
The clpB gene of Bifidobacterium breve UCC 2003: transcriptional analysis and first insights into stress induction
Microbiology, September 1, 2005; 151(9): 2861 - 2872.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. Chander and B. Demple
Functional Analysis of SoxR Residues Affecting Transduction of Oxidative Stress Signals into Gene Expression
J. Biol. Chem., October 1, 2004; 279(40): 41603 - 41610.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K. J. Newberry and R. G. Brennan
The Structural Mechanism for Transcription Activation by MerR Family Member Multidrug Transporter Activation, N Terminus
J. Biol. Chem., May 7, 2004; 279(19): 20356 - 20362.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
L. Song, J. Caguiat, Z. Li, J. Shokes, R. A. Scott, L. Olliff, and A. O. Summers
Engineered Single-Chain, Antiparallel, Coiled Coil Mimics the MerR Metal Binding Site
J. Bacteriol., March 15, 2004; 186(6): 1861 - 1868.
[Abstract] [Full Text] [PDF]


Home page
MicrobiologyHome page
A. Gaballa, M. Cao, and J. D. Helmann
Two MerR homologues that affect copper induction of the Bacillus subtilis copZA operon
Microbiology, December 1, 2003; 149(12): 3413 - 3421.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. H. Godsey, E. E. Zheleznova Heldwein, and R. G. Brennan
Structural Biology of Bacterial Multidrug Resistance Gene Regulators
J. Biol. Chem., October 18, 2002; 277(43): 40169 - 40172.
[Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J. J. Lopez-Rubio, M. Elias-Arnanz, S. Padmanabhan, and F. J. Murillo
A Repressor-Antirepressor Pair Links Two Loci Controlling Light-induced Carotenogenesis in Myxococcus xanthus
J. Biol. Chem., February 22, 2002; 277(9): 7262 - 7270.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. Basak and V. Nagaraja
DNA Unwinding Mechanism for the Transcriptional Activation of momP1 Promoter by the Transactivator Protein C of Bacteriophage Mu
J. Biol. Chem., December 7, 2001; 276(50): 46941 - 46945.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. H. Godsey, N. N. Baranova, A. A. Neyfakh, and R. G. Brennan
Crystal Structure of MtaN, a Global Multidrug Transporter Gene Activator
J. Biol. Chem., December 7, 2001; 276(50): 47178 - 47184.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
D. P. Giedroc, X. Chen, M. A. Pennella, and A. C. LiWang
Conformational Heterogeneity in the C-terminal Zinc Fingers of Human MTF-1. AN NMR AND ZINC-BINDING STUDY
J. Biol. Chem., November 2, 2001; 276(45): 42322 - 42332.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
G. Grass, B. Fan, B. P. Rosen, S. Franke, D. H. Nies, and C. Rensing
ZitB (YbgR), a Member of the Cation Diffusion Facilitator Family, Is an Additional Zinc Transporter in Escherichia coli
J. Bacteriol., August 1, 2001; 183(15): 4664 - 4667.
[Abstract] [Full Text] [PDF]


Home page
Appl. Environ. Microbiol.Home page
S.-W. Lee, E. Glickmann, and D. A. Cooksey
Chromosomal Locus for Cadmium Resistance in Pseudomonas putida Consisting of a Cadmium-Transporting ATPase and a MerR Family Response Regulator
Appl. Envir. Microbiol., April 1, 2001; 67(4): 1437 - 1444.
[Abstract] [Full Text]


Home page
J. Bacteriol.Home page
T. A. Slieman, R. Rebeil, and W. L. Nicholson
Spore Photoproduct (SP) Lyase from Bacillus subtilis Specifically Binds to and Cleaves SP (5-Thyminyl-5,6-Dihydrothymine) but Not Cyclobutane Pyrimidine Dimers in UV-Irradiated DNA
J. Bacteriol., November 15, 2000; 182(22): 6412 - 6417.
[Abstract] [Full Text]


Home page
J. Biol. Chem.Home page
F. W. Outten, C. E. Outten, J. Hale, and T. V. O'Halloran
Transcriptional Activation of an Escherichia coli Copper Efflux Regulon by the Chromosomal MerR Homologue, CueR
J. Biol. Chem., September 29, 2000; 275(40): 31024 - 31029.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1999 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement