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

被引:43
作者
Kanezaki, R
Toki, T
Yokoyama, M
Yomogida, K
Sugiyama, K
Yamamoto, M
Igarashi, K
Ito, E [1 ]
机构
[1] Hirosaki Univ, Sch Med, Dept Pediat, Hirosaki, Aomori 0368563, Japan
[2] Hirosaki Univ, Fac Sci, Dept Biol, Hirosaki, Aomori 0368563, Japan
[3] Osaka Univ, Dept Sci, Lab Anim Experimentat, Microbial Dis Res Inst, Suita, Osaka 5650871, Japan
[4] Univ Tsukuba, Ctr Tsukuba Adv Res Alliance, Tsukuba, Ibaraki 3058575, Japan
[5] Univ Tsukuba, Inst Basic Med Sci, Tsukuba, Ibaraki 3058575, Japan
[6] Hiroshima Univ, Sch Med, Dept Biochem, Minami Ku, Hiroshima 7348551, Japan
关键词
D O I
10.1074/jbc.M004227200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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-tetra-decanoylphorbol-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.
引用
收藏
页码:7278 / 7284
页数:7
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