Okuda T, Cleveland J L, Downing J R
Department of Pathology, St Jude Children's Research Hospital, Memphis, Tennessee 38105.
Oncogene. 1992 Nov;7(11):2249-58.
We have isolated two murine cDNAs designated PCTAIRE-1 and -3 which encode putative serine/threonine-specific protein kinases. The predicted products of PCTAIRE-1 and -3 are 65% homologous and are organized into a core 295-residue kinase domain flanked by unique 161 and 117 amino acid N-terminal and 40 and 39 amino acid C-terminal domains respectively. The kinase domains are approximately 50-55% homologous to members of the cdc2/CDC28 kinase gene family, and each contains a cysteine-for-serine substitution within the conserved PSTAIRE motif. PCTAIRE-1 was ubiquitously expressed as a predominant 3.0-kb transcript and a minor 2.2-kb mRNA resulting from differential polyadenylation. In contrast, PCTAIRE-3 exhibited a more restricted pattern of expression with a single 3.0-kb mRNA detected in brain, kidney and intestine. The PCTAIRE-1 and -3 products produced by in vitro transcription-translation failed to bind to p13suc1 but were precipitated by antibodies directed to Schizosaccharomyces pombe p34cdc2 or to the human PSTAIRE motif. Thus, PCTAIRE-1 and -3 are members of a novel subfamily of cdc2/CDC28-related protein kinases.
我们分离出了两个小鼠cDNA，分别命名为PCTAIRE-1和-3，它们编码假定的丝氨酸/苏氨酸特异性蛋白激酶。PCTAIRE-1和-3的预测产物具有65%的同源性，被组织成一个由295个残基组成的核心激酶结构域，两侧分别是独特的161个和117个氨基酸的N端结构域以及40个和39个氨基酸的C端结构域。激酶结构域与cdc2/CDC28激酶基因家族成员的同源性约为50-55%，并且每个结构域在保守的PSTAIRE基序内都有一个丝氨酸被半胱氨酸取代的情况。PCTAIRE-1以一种主要的3.0-kb转录本和一种由差异多聚腺苷酸化产生的次要2.2-kb mRNA的形式普遍表达。相比之下，PCTAIRE-3表现出更受限的表达模式，在脑、肾和肠中检测到单一的3.0-kb mRNA。通过体外转录-翻译产生的PCTAIRE-1和-3产物不能与p13suc1结合，但能被针对粟酒裂殖酵母p34cdc2或人类PSTAIRE基序的抗体沉淀。因此，PCTAIRE-1和-3是cdc2/CDC28相关蛋白激酶新亚家族的成员。
