Molecular cloning of a novel human cdc2/CDC28-like protein kinase.
Molecular cloning of a novel human cdc2/CDC28-like protein kinase.
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DOI：
10.1016/s0021-9258(19)67807-5
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发表时间：
1991-02
期刊：
影响因子：
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通讯作者：
K. Johnson;K. Smith
中科院分区：
文献类型：
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作者：
K. Johnson;K. Smith
利用同源探针法分离了一种新的人蛋白激酶。脱氧寡核苷酸探针识别蛋白激酶的COOH-末端部分中的保守亚结构域，鉴定了编码具有预测的丝氨酸/苏氨酸磷酸化特异性的推定激酶的cDNA克隆。全长1.7-β-淀粉酶对cDNA与许多组织中的1.7-β-淀粉酶和3.4-β-淀粉酶mRNA转录本杂交。编码的蛋白质的大小为454个氨基酸，并且由NH 2末端130个残基的区段组成，其可能代表调节区，随后是324个残基的催化结构域。催化区的一级序列和预测的二级结构与其它已知激酶的比较和比对揭示，新的激酶，表示为“CLK”（CDC样激酶），代表了与调节细胞周期的酵母cdc 2/CDC 28激酶具有显著同源性的人蛋白激酶新家族的原型。
A homology probing approach was utilized to isolate a new human protein kinase. Deoxyoligonucleotide probes recognizing a conserved subdomain in the COOH-terminal portion of protein kinases identified a cDNA clone encoding a putative kinase with predicted serine/threonine phosphorylation specificity. The full-length, 1.7-kilobase pair cDNA hybridizes to 1.7- and 3.4-kilobase mRNA transcripts in a number of tissues. The size of the encoded protein is 454 amino acids and consists of an NH2-terminal 130-residue segment, which may represent a regulatory region, followed by a 324-residue catalytic domain. Comparisons and alignments of the primary sequence and predicted secondary structure of the catalytic region to other known kinases reveal that the new kinase, denoted “CLK” (for CDC-like kinase), represents a prototype for a new family of human protein kinases bearing significant homology to the yeast cdc2/CDC28 kinases that regulate the cell cycle.