JBC

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


     

Originally published In Press as doi:10.1074/jbc.M505217200 on June 4, 2005 Originally published In Press as doi:10.1074/jbc.M505217200 on May 31, 2005

J. Biol. Chem., Vol. 280, Issue 31, 28529-28540, August 5, 2005
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
280/31/28529    most recent
M505217200v2
M505217200v1
Right arrow Alert me when this article is cited
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 arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Potter, B. M.
Right arrow Articles by Laity, J. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Potter, B. M.
Right arrow Articles by Laity, J. H.
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?

The Six Zinc Fingers of Metal-responsive Element Binding Transcription Factor-1 Form Stable and Quasi-ordered Structures with Relatively Small Differences in Zinc Affinities*

Belinda M. Potter{ddagger}, Linda S. Feng{ddagger}, Priya Parasuram{ddagger}, Viktor A. Matskevich{ddagger}, Jed A. Wilson{ddagger}, Glen K. Andrews§, and John H. Laity{ddagger}

From the {ddagger}Division of Cell Biology and Biophysics, School of Biological Sciences, University of Missouri-Kansas City, Kansas City, Missouri 64110 and the §Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, Kansas 66160

Six Cys2His2 zinc fingers (F1–6) comprise the DNA binding domain of metal-responsive element binding transcription factor-1 (MTF-1). F1–6 is necessary for basal and zinc-induced expression of metallothionein genes. Analysis of NMR structural and dynamic data for an F1–6 protein construct demonstrates that each zinc finger adopts a stable {beta}{beta}{alpha} fold in the presence of stoichiometric Zn(II), provided that all cysteine ligands are in a reduced state. Parallel studies of protein constructs spanning the four N-terminal core DNA binding fingers (F1–4) and two C-terminal low DNA affinity fingers (F5–6) reveal similar stable zinc finger structures. In both the F1–6 and F5–6 proteins, the finger 5 cysteines were found to readily oxidize at neutral pH. Detailed spectral density and hydrodynamic analysis of 15N relaxation data revealed quasi-ordered anisotropic rotational diffusion properties of the six F1–6 zinc fingers that could influence MTF-1 DNA binding function. A more general effect on the rotational diffusion properties of Cys2His2 zinc fingers was also uncovered that is dependent upon the position of each finger within multifinger domains. Analysis of NMR 1H-15N-heteronuclear single quantum coherence spectral peak intensities measured as a function of added Zn(II) in conjunction with Zn(II) binding modeling studies indicated that the Zn(II) affinities of all MTF-1 zinc fingers are within ~10–50-fold. These analyses further suggested that metal sensing by MTF-1 in eukaryotic cells involves multiple zinc fingers and occurs over a 100-fold or less range of accessible Zn(II) concentration.

Received for publication, May 31, 2005

The NMR resonance assignments for MTF-1 F1-6, F1-4, and F5-6 have been deposited in the BioMagResBank database under accession numbers 6275, 6409, and 6408, respectively.

* This work was supported in part by National Institutes of Health Grant ES05704 (to G. K. A.). The costs of publication of this article were defrayed in part by the payment of page charges. This 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: UMKC, 103 BSB, 5007 Rockhill Rd., Kansas City, MO 64110. Tel.: 816-235-5345; Fax: 816-235-6584; E-mail: laityj{at}umkc.edu.


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
 Mol. Cell. Biol.Home page
Y. Li, T. Kimura, R. W. Huyck, J. H. Laity, and G. K. Andrews
Zinc-Induced Formation of a Coactivator Complex Containing the Zinc-Sensing Transcription Factor MTF-1, p300/CBP, and Sp1
Mol. Cell. Biol., July 1, 2008; 28(13): 4275 - 4284.
[Abstract] [Full Text] [PDF]

Home page
 Mol Cancer ResHome page
B. J. Murphy, T. Kimura, B. G. Sato, Y. Shi, and G. K. Andrews
Metallothionein Induction by Hypoxia Involves Cooperative Interactions between Metal-Responsive Transcription Factor-1 and Hypoxia-Inducible Transcription Factor-1{alpha}
Mol. Cancer Res., March 1, 2008; 6(3): 483 - 490.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. S. Hontz, M. T. Villar-Lecumberri, B. M. Potter, M. D. Yoder, L. A. Dreyfus, and J. H. Laity
Differences in Crystal and Solution Structures of the Cytolethal Distending Toxin B Subunit: RELEVANCE TO NUCLEAR TRANSLOCATION AND FUNCTIONAL ACTIVATION
J. Biol. Chem., September 1, 2006; 281(35): 25365 - 25372.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
Y. Li, T. Kimura, J. H. Laity, and G. K. Andrews
The Zinc-Sensing Mechanism of Mouse MTF-1 Involves Linker Peptides between the Zinc Fingers
Mol. Cell. Biol., August 1, 2006; 26(15): 5580 - 5587.
[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 © 2005 by the American Society for Biochemistry and Molecular Biology.