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M004227200v1
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Papers In Press, published online ahead of print November 7, 2000
J. Biol. Chem, 10.1074/jbc.M004227200
Submitted on May 17, 2000
Revised on November 6, 2000
Accepted on November 7, 2000

Transcription factor BACH1 is recruited to the nucleus by its novel alternative spliced isoform

Rika Kanezaki, Tsutomu Toki, Masaru Yokoyama, Kentaro Yomogida, Kazuo Sugiyama, Masayuki Yamamoto, Kazuhiko Igarashi, and Etsuro Ito

Department of Pediatrics, Hirosaki University School Medicine, Hirosaki, Aomori 036-8562

Corresponding Author: eturou{at}cc.hirosaki-u.ac.jp

The transcription factor Bach1 is a member of a novel family of BTB/POZ-basic region leucine zipper (bZip) 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 (MARE), 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 kb downstream of the exon encoding the leucine zipper domain, and produced a protein that contained the conserved BTB/POZ, CNC, and basic region domains, but lacked the leucine zipper domain essential for NF-E2/MARE binding. Subcellular localization studies using green fluorescent protein (GFP) as a reporter showed that full length BACH1 localized to the cytoplasm, whereas BACH1t accumulated in the nucleus. Interestingly, co-expression 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.


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