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Originally published In Press as doi:10.1074/jbc.M107496200 on February 26, 2002

J. Biol. Chem., Vol. 277, Issue 18, 16153-16159, May 3, 2002
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DNA Binding and Gene Activation Properties of the Nmp4 Nuclear Matrix Transcription Factors*

Kitti TorrungruangDagger §, Marta Alvarez§, Rita ShahDagger , Jude E. Onyia||, Simon J. Rhodes**, and Joseph P. BidwellDagger Dagger Dagger

From the Dagger  Department of Periodontics, Indiana University School of Dentistry, Indianapolis, Indiana 46202, the  Department of Anatomy and Cell Biology, Indiana University School of Medicine, Indianapolis, Indiana 46202, the || Gene Regulation, Bone, and Inflammation Research Division, Lilly Research Laboratories, Indianapolis, Indiana 46285, and the ** Department of Biology, Indiana University-Purdue University, Indianapolis, Indiana 46202

Splice variants of the Nmp4 gene include nuclear matrix transcription factors that regulate the type I collagen alpha 1(I) polypeptide chain (COL1A1) promoter and several matrix metalloproteinase (MMP) genes. To date, these are the only Cys2His2 zinc finger proteins known to bind within the minor groove of homopolymeric (dA·dT) DNA. Nmp4 isoforms contain from 5 to 8 Cys2His2 zinc fingers, an SH3-binding domain that overlaps with a putative AT-hook and a polyglutamine-alanine repeat (poly(QA)). To determine the mechanistic significance of Cys2His2 zinc finger association with this unusual consensus DNA binding element, we identified the Nmp4 DNA-binding and transcriptional activation domains. Zinc fingers 2, 3, and 6 mediated association with the homopolymeric (dA·dT) COL1A1/MMP DNA consensus element. The N terminus of the Nmp4 protein exhibited a strong trans-activation capacity when fused to the GAL4 DNA-binding domain, but this activity was masked within the context of the full-length Nmp4-GAL4 DNA-binding domain chimera. However, upon binding to the COL1A1/MMP homopolymeric (dA·dT) element, the native Nmp4 protein up-regulated transcription, and the poly(QA) domain acquired a significant role in trans-activation. We propose that allosteric effects induced upon zinc finger association with the homopolymeric (dA·dT) minor groove confer context-specific functionality to this unusual family of Cys2His2 transcription factors.

* This work was supported by National Institutes of Health Grant DK53796-01A1 (to J. P. B.) and National Science Foundation Grant 9729669 (S. J. R.).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.

§ Both authors contributed equally to this work.

Dagger Dagger To whom correspondence should be addressed: Dept. of Anatomy and Cell Biology, Medical Science Bldg. 5035, Indiana University School of Medicine, 635 Barnhill Dr., Indianapolis, IN 46202. E-mail: jbidwell@iupui.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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