The primary structure of rat ribosomal protein L10: Relationship to a jun-binding protein and to a putative Wilms' tumor suppressor
The primary structure of rat ribosomal protein L10: Relationship to a jun-binding protein and to a putative Wilms' tumor suppressor
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DOI：
10.1006/bbrc.1996.1277
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发表时间：
1996-08-23
影响因子：
3.1
通讯作者：
Wool, IG
中科院分区：
文献类型：
--
作者：
Chan, YL;Diaz, JJ;Wool, IG
大鼠60S核糖体亚基蛋白L10的氨基酸序列是从两个重组DNA中的核苷酸序列推导出来的，并通过蛋白质中NH2末端氨基酸序列的测定得到了证实。核糖体蛋白L10有213个氨基酸(翻译后NH2末端的蛋氨酸被去除)；分子量为24,456。与核DNA的DNA杂交表明，L10基因有8到10个拷贝。该蛋白的信使核糖核酸长度约为900个核苷酸。大鼠L10与其他真核生物的核糖体蛋白相关。此外，核糖体蛋白L10是鸡Jun结合蛋白的哺乳动物同源蛋白，与推测的Wilms‘s肿瘤抑制因子几乎相同。这是一个核糖体蛋白的体外功能的推定例子，还有许多其他例子。(C)1996年学术出版社。
The amino acid sequence of the rat 60S ribosomal subunit protein L10 was deduced from the sequence of nucleotides in two recombinant cDNAs and confirmed by determination of the NH2-terminal amino acid sequence in the protein. Ribosomal protein L10 has 213 amino acids (the NH2-terminal methionine is removed after translation of the mRNA); the molecular weight is 24,456. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 8 to 10 copies of the L10 gene. The mRNA for the protein is about 900 nucleotides in length. Rat L10 is related to ribosomal proteins from other eukaryotes. Ribosomal protein L10 is, in addition, the mammalian homolog of the chicken Jun-binding protein and is nearly identical to a putative Wilms' tumor suppressor. This is a presumptive example, of which there are many others, of an extraribosomal function of a ribosomal protein. (C) 1996 Academic Press, Inc.