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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
The -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-Laser
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- 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- 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.
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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