THE PRIMARY STRUCTURE OF THE PUTATIVE ONCOGENE PIM-1 SHOWS EXTENSIVE HOMOLOGY WITH PROTEIN-KINASES
THE PRIMARY STRUCTURE OF THE PUTATIVE ONCOGENE PIM-1 SHOWS EXTENSIVE HOMOLOGY WITH PROTEIN-KINASES
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DOI：
10.1016/0092-8674(86)90886-x
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发表时间：
1986-08-15
期刊：
影响因子：
64.5
通讯作者：
BERNS, A
中科院分区：
文献类型：
--
作者：
SELTEN, G;CUYPERS, HT;BERNS, A
我们之前已经证明，在鼠白血病病毒诱导的 T 细胞淋巴瘤中，假定的癌基因 pim-1 经常被原病毒插入激活。在这里，我们描述了通过基因组和 cDNA 克隆测序确定的 pim-1 基因的结构。该基因有一个开放阅读框，编码 313 个氨基酸的蛋白质，延伸超过 6 个外显子，所有阅读框中前后都有终止密码子。原病毒总是整合在蛋白质编码结构域之外，表现出对 3'' 末端外显子中的小区域的高度偏好； 3'' 外显子中的整合导致 pim-1 mRNA 水平相对较高。计算机搜索揭示了 pim-1 和蛋白激酶之间的同源性：蛋白激酶的所有特征结构域在 pim-1 氨基酸序列中都是保守的。观察到蛋白丝氨酸激酶具有最高的同源性。
We have shown previously that the putative oncogene pim-1 is frequently activated by provirus insertion in murine leukemia virus-induced T cell lymphomas. Here we describe the structure of the pim-1 gene as determined by sequencing genomic and cDNA clones. The gene has an open reading frame, encoding a protein of 313 amino acids, extending over six exons and preceded and followed by stop codons in all reading frames. Proviruses always integrate outside the protein-encoding domain, showing a high preference for a small region in the 3''-terminal exon; integration in the 3'' exon results in relatively high levels of pim-1 mRNA. Computer search reveals homology between pim-1 and protein kinases: all the domains characteristic of protein kinases are conserved in the pim-1 amino acid sequence. The highest homologies were observed with the protein-serine kinases.