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Originally published In Press as doi:10.1074/jbc.M004227200 on November 7, 2000

J. Biol. Chem., Vol. 276, Issue 10, 7278-7284, March 9, 2001
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Transcription Factor BACH1 Is Recruited to the Nucleus by Its Novel Alternative Spliced Isoform*

Rika KanezakiDagger §, Tsutomu TokiDagger , Masaru YokoyamaDagger , Kentaro Yomogida, Kazuo Sugiyama§, Masayuki Yamamoto||, Kazuhiko Igarashi**, and Etsuro ItoDagger Dagger Dagger

From the Dagger  Department of Pediatrics, School of Medicine and § Department of Biology, Faculty of Sciences, Hirosaki University, Hirosaki 036-8563, the  Department of Science for Laboratory Animal Experimentation, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamadaoka, Suita City, Osaka 565-0871, the || Center for Tsukuba Advanced Research Alliance and Institute of Basic Medical Sciences, University of Tsukuba, Tsukuba 305-8575, and the ** Department of Biochemistry, Hiroshima University School of Medicine, Kasumi 1-2-3, Minami-Ku, Hiroshima 734-8551, Japan

The transcription factor Bach1 is a member of a novel family of broad complex, tramtrack, bric-a-brac/poxvirus and zinc finger (BTB/POZ) basic region leucine zipper factors. Bach1 forms a heterodimer with MafK, a member of the small Maf protein family (MafF, MafG, and MafK), which recognizes the NF-E2/Maf recognition element, a cis-regulatory motif containing a 12-O-tetradecanoylphorbol-13-acetate-responsive element. Here we describe the gene structure of human BACH1, including a newly identified promoter and an alternatively RNA-spliced truncated form of BACH1, designated BACH1t, abundantly transcribed in human testis. The alternate splicing originated from the usage of a novel exon located 5.6 kilobase pairs downstream of the exon encoding the leucine zipper domain, and produced a protein that contained the conserved BTB/POZ, Cap'n collar, and basic region domains, but lacked the leucine zipper domain essential for NF-E2/Maf recognition element binding. Subcellular localization studies using green fluorescent protein as a reporter showed that full-length BACH1 localized to the cytoplasm, whereas BACH1t accumulated in the nucleus. Interestingly, coexpression of BACH1 and BACH1t demonstrated interaction between the molecules and the induction of nuclear import of BACH1. These results suggested that BACH1t recruits BACH1 to the nucleus through BTB domain-mediated interaction.

* This work was supported by grants-in-aid for scientific research, grants-in-aid for scientific research on priority areas (to E. I. and K. I.) and a grant-in-aid for encouragement of young scientists (to T. T.) from the Ministry of Education, Science, Sports and Culture of Japan, and by a grant from the Karouji Memorial Foundation (to E. I.).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/EMBL Data Bank with accession number(s) AF317902 and AF317903.

Dagger Dagger To whom correspondence should be addressed. Tel.: 81-172-39-5070; Fax: 81-172-39-5071; E-mail: eturou@cc.hirosaki-u.ac.jp.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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