The RNA-binding protein, TB-RBP, is the mouse homologue of translin, a recombination protein associated with chromosomal translocations.
The RNA-binding protein, TB-RBP, is the mouse homologue of translin, a recombination protein associated with chromosomal translocations.
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RNA 结合蛋白 TB-RBP 是易位蛋白的小鼠同源物，易位蛋白是一种与染色体易位相关的重组蛋白。
DOI：
10.1073/pnas.94.11.5640
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发表时间：
1997
影响因子：
11.1
通讯作者：
Hecht,NB
中科院分区：
文献类型：
--
作者：
Wu,XQ;Gu,W;Meng,X;Hecht,NB
小鼠rna结合蛋白TB-RBP在体外抑制翻译，并通过结合特定mrna 3 '非翻译区域的保守元件将mrna附着到微管上。目前，我们已经从睾丸和脑细胞质提取物中纯化了TB-RBP，并克隆了其cDNA。我们发现小鼠TB-RBP cdna包含228个氨基酸的开放阅读框，其C端有亮氨酸拉链结构域、跨膜螺旋和一组假定的磷酸化位点。TB-RBP与人类蛋白translin（一种与染色体易位相关的重组热点结合蛋白）具有99%的一致性[Aoki， K., Suzuki， K., Sugano， T., Tasaka， T., Nakahara， K., Kuge， O., Omori, a .和Kasai， M.(1995)]。Genet.10, 167 - 174]。如translin所示，TB-RBP还结合单链dna，其中包含广泛的共识序列，其中许多与Y和H rna结合序列相似。合成了重组TB-RBP蛋白，制备了针对重组蛋白的抗血清。通过证明睾丸提取物中TB-RBP的免疫沉淀可消除RNA-TB-RBP复合物的形成，证实了translin和TB-RBP之间的一致性。基于其与聚集断点区靶序列的DNA结合，我们提出TB-RBP可能参与了男性生殖细胞的DNA重组或DNA修复。
The mouse RNA-binding protein, TB-RBP, suppresses translationin vitroand attaches mRNAs to microtubules by binding to conserved elements in the 3′ untranslated regions of specific mRNAs. We have now purified TB-RBP from testicular and brain cytoplasmic extracts and cloned its cDNA. We find that the mouse TB-RBP cDNAs contain an open reading frame of 228 amino acids with a leucine zipper domain within its C terminus, a transmembrane helix, and a group of putative phosphorylation sites. TB-RBP shows 99% identity to the human protein, translin, a recombination hotspot-binding protein associated with chromosomal translocations [Aoki, K., Suzuki, K., Sugano, T., Tasaka, T., Nakahara, K., Kuge, O., Omori, A. & Kasai, M. (1995)Nat. Genet.10, 167–174]. As shown for translin, TB-RBP also binds to single-stranded DNAs containing a broad range of consensus sequences, many of which are similar to the Y and H RNA-binding sequences. Recombinant TB-RBP was synthesized and an antiserum was prepared against the recombinant protein. The identity between translin and TB-RBP was confirmed by demonstrating that immunoprecipitation of TB-RBP from testicular extracts abolished formation of the RNA-TB–RBP complex. Based upon its DNA binding to target sequences in clustered breakpoint regions, we propose that TB-RBP may be involved in DNA recombination or DNA repair in male germ cells.