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 twohybrid and in vitro binding studies reveal the ankyrinrepeat 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.The tobacco bZIP protein BZI-1 displays all the characteristic features of a transcription factor. It binds DNA, in particular ACGT containing cis-elements (ACEs), 1 it is localized inside the nucleus, and its N-terminal domain acts as a trans-activation domain in plant cells (1). Like CPRF2, a highly homologous bZIP protein from parsley, BZI-1 has been isolated by virtue of its in vitro binding to chalcone synthase promoter cis-elements (1-4). However, using various transgenic approaches that modulate the amount or the activation potential of BZI-1, we were not able to show any influence on transcription of phenylpropanoid pathway genes, such as chalcone synthase or phenylalanine ammonia lyase in vivo (1).Functional analysis has been performed in transgenic plants expressing a dominant-negative BZI-1 derivative lacking the N-terminal activation domain (BZI-1-⌬N). These plants display reduced internodes, small curly leaves, enhanced lateral shoot formation, and flowers that are reduced in size. In particular auxin responses appeared to be reduced with respect to auxininduced rooting and regulation of a GH3 target gene. Moreover, BZI-1 transcription is up-regulated in response to pathogen attack and pathogen-induced phosphorylation of BZI-1-related proteins has been described (1, 3, 4).BZI-1-related transcription factors have been isolated from various plant species, e.g. CPRF2, (2), OHP1/2 (5), BLZ1 (6), or bZIP63 (7). Apart from the N...