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Originally published In Press as doi:10.1074/jbc.M210292200 on December 23, 2002

J. Biol. Chem., Vol. 278, Issue 10, 8786-8794, March 7, 2003
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The alpha -Helical D1 Domain of the Tobacco bZIP Transcription Factor BZI-1 Interacts with the Ankyrin-repeat Protein ANK1 and Is Important for BZI-1 Function, Both in Auxin Signaling and Pathogen Response*

Markus Kuhlmann, Katja Horvay, Anne Strathmann, Thorsten Heinekamp, Ute Fischer, Stefan Böttner, and Wolfgang Dröge-LaserDagger

From the Albrecht-von-Haller Institut, Universität Göttingen, Untere Karspüle 2, D-37073 Göttingen, Germany

The tobacco (Nicotiana tabacum) bZIP transcription factor BZI-1 is involved in auxin-mediated growth responses and in establishing pathogen defenses. Transgenic plants expressing a dominant-negative BZI-1-Delta N derivative, which lacks the N-terminal activation domain, showed altered vegetative growth. In particular auxin-induced rooting and formation of tobacco mosaic virus-induced hypersensitive response lesions are affected. BZI-1-related proteins described in various plant species share the conserved domains D1, D2, BD, and D4. To define those BZI-1 domains involved in transcription factor function, BZI-1 deletion derivatives were expressed in transgenic plants. The domains D1 or BD are crucial for BZI-1-Delta N function in planta. The basic BD domain is mediating DNA binding of BZI-1. Yeast two-hybrid and in vitro binding studies reveal the ankyrin-repeat protein ANK1, which specifically interacts with a part of the BZI-1 protein (amino acids 73-222) encoding the D1 domain. ANK1 does not bind DNA or act as a co-activator of BZI-1-mediated transcription. Moreover, green fluorescence protein localization studies propose that ANK1 is acting mainly inside the cytosol. Transcription analysis reveals that ANK1 is ubiquitously expressed, but after pathogen attack transcription is transiently down-regulated. Along these lines, ANK1 homologous proteins in Arabidopsis thaliana have been reported to function in pathogen defense. We therefore propose that the D1 domain serves as an interaction surface for ANK1, which appears to regulate BZI-1 function in auxin signaling as well as pathogen response.


* This research was supported, in part, by a grant of the Fond der Chemischen Industrie (to A. S.) and Deutsche Forschungsgemeinschaft Grant DR273/4.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.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF510035.

Dagger To whom correspondence should be addressed. Tel.: 49-0-551-39-19816; Fax: 49-0-551-39-7820; E-mail: wdroege@gwdg.de.


Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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