Dimerization of the testis brain RNA-binding protein (translin) is mediated through its C-terminus and is required for DNA- and RNA-binding

被引:42
作者
Wu, XQ
Xu, LH
Hecht, NB [1 ]
机构
[1] Univ Penn, Med Ctr, Ctr Res Reprod & Womens Hlth, Philadelphia, PA 19104 USA
[2] Univ Penn, Med Ctr, Dept Obstet & Gynecol, Philadelphia, PA 19104 USA
关键词
D O I
10.1093/nar/26.7.1675
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
Testis brain-RNA-binding protein (TB-RBP) is a single-stranded DNA- and RNA-binding protein that is involved in chromosomal translocations, mRNA transport and translational regulation. Here we show from in vitro and in vivo protein binding studies that TB-RBP dimers are the minimum structural unit needed for DNA- and RNA-binding. Truncation studies demonstrate that the C-terminus of 55 amino acids of TB-RBP is essential, but not sufficient for DNA- or RNA-binding, and deletion of the leucine zipper motif in the C-terminus abolishes DNA- and RNA-binding. Changing cysteine 225 in the C-terminus to alanine does not significantly reduce DNA- or RNA-binding, but reduces the stability of the dimer. We conclude that the leucine zipper motif is required to maintain two molecules of TB-RBP as a dimer which is stabilized by a disulfide bond involving cysteine 225.
引用
收藏
页码:1675 / 1680
页数:6
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