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Plant and Cell Physiology 2004 45(7):845-854; doi:10.1093/pcp/pch101
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© 2004 Oxford University Press

VOZ; Isolation and Characterization of Novel Vascular Plant Transcription Factors with a One-Zinc Finger from Arabidopsis thaliana

Nobutaka Mitsuda1,4, Toru Hisabori3, Kunio Takeyasu2 and Masa H. Sato1,5

1 Graduate School of Human and Environmental Studies, Kyoto University, Yoshidanihonmatsu, Sakyo-ku, Kyoto, 606-8501 Japan
2 Graduate School of Biostudies, Kyoto University, Yoshidanihonmatsu, Sakyo-ku, Kyoto, 606-8501 Japan
3 Chemical Resources Laboratory, Tokyo Institute Technology, Nagatsuta 4259, Midori-ku, Yokohama, 226-8503 Japan

A 38-bp pollen-specific cis-acting region of the AVP1 gene is involved in the expression of the Arabidopsis thaliana V-PPase during pollen development. Here, we report the isolation and structural characterization of AtVOZ1 and AtVOZ2, novel transcription factors that bind to the 38-bp cis-acting region of A. thaliana V-PPase gene, AVP1. AtVOZ1 and AtVOZ2 show 53% amino acid sequence similarity. Homologs of AtVOZ1 and AtVOZ2 are found in various vascular plants as well as a moss, Physcomitrella patens. Promoter-ß-glucuronidase reporter analysis shows that AtVOZ1 is specifically expressed in the phloem tissue and AtVOZ2 is strongly expressed in the root. In vivo transient effector-reporter analysis in A. thaliana suspension-cultured cells demonstrates that AtVOZ1 and AtVOZ2 function as transcriptional activators in the Arabidopsis cell. Two conserved regions termed Domain-A and Domain-B were identified from an alignment of AtVOZ proteins and their homologs of O. sativa and P. patens. AtVOZ2 binds as a dimer to the specific palindromic sequence, GCGTNx7ACGC, with Domain-B, which is comprised of a functional novel zinc coordinating motif and a conserved basic region. Domain-B is shown to function as both the DNA-binding and the dimerization domains of AtVOZ2. From highly the conservative nature among all identified VOZ proteins, we conclude that Domain-B is responsible for the DNA binding and dimerization of all VOZ-family proteins and designate it as the VOZ-domain.

4 Present address: Central 4, Higashi 1-1-1, Tsukuba, Ibaraki 305-8562, Japan, Plant Gene Function Research Team, Gene Function Research Center, National Institute of Advanced Industrial Science and Technology (AIST).

5 Corresponding author: E-mail, mhsato{at}z04.mbox.media.kyoto-u.ac.jp; Fax, +81-75-753-6857.


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