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Biochemical and Genetic Conservation of Fission Yeast Dsk1 and Human SR Protein-Specific Kinase 1

机译：裂变酵母Dsk1和人类SR蛋白特异性激酶1的生化和遗传保护。

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Arginine/serine-rich (RS) domain-containing proteins and their phosphorylation by specific protein kinases constitute control circuits to regulate pre-mRNA splicing and coordinate splicing with transcription in mammalian cells. We present here the finding that similar SR networks exist in Schizosaccharomyces pombe. We previously showed that Dsk1 protein, originally described as a mitotic regulator, displays high activity in phosphorylating S. pombe Prp2 protein (spU2AF59), a homologue of human U2AF65. We now demonstrate that Dsk1 also phosphorylates two recently identified fission yeast proteins with RS repeats, Srp1 and Srp2, in vitro. The phosphorylated proteins bear the same phosphoepitope found in mammalian SR proteins. Consistent with its substrate specificity, Dsk1 forms kinase-competent complexes with those proteins. Furthermore,dsk1 + gene determines the phenotype ofprp2 + overexpression, providing in vivo evidence that Prp2 is a target for Dsk1. The dsk1-null mutant strain became severely sick with the additional deletion of a related kinase gene. Significantly, human SR protein-specific kinase 1 (SRPK1) complements the growth defect of the double-deletion mutant. In conjunction with the resemblance of dsk1 + andSRPK1 in sequence homology, biochemical properties, and overexpression phenotypes, the complementation result indicates that SRPK1 is a functional homologue of Dsk1. Collectively, our studies illustrate the conserved SR networks in S. pombe consisting of RS domain-containing proteins and SR protein-specific kinases and thus establish the importance of the networks in eucaryotic organisms.
机译：含精氨酸/丝氨酸（RS）域的蛋白质及其通过特定蛋白激酶的磷酸化构成控制电路，以调节mRNA前的剪接并与哺乳动物细胞中的转录协调剪接。在这里，我们发现在粟酒裂殖酵母中存在类似的SR网络。我们先前显示，最初称为有丝分裂调节剂的Dsk1蛋白在磷酸化 S中显示出高活性。 pombe Prp2蛋白（spU2AF59），是人U2AF65的同源物。现在，我们证明Dsk1还可以在体外用RS重复序列Srp1和Srp2将两个最近鉴定的裂变酵母蛋白磷酸化。磷酸化的蛋白具有与哺乳动物SR蛋白相同的磷酸表位。与其底物特异性一致，Dsk1与那些蛋白质形成激酶活性复合物。此外， dsk1 + 基因决定了 prp2 + 过表达的表型，提供了体内证据表明Prp2是靶标对于Dsk1。 dsk1 -null突变株因相关激酶基因的额外缺失而病重。重要的是，人SR蛋白特异性激酶1（SRPK1）弥补了双缺失突变体的生长缺陷。结合 dsk1 + 和 SRPK1 在序列同源性，生化特性和过表达表型方面的相似性，互补结果表明SRPK1是一个Dsk1的功能同源物。我们的研究共同说明了 S中保守的SR网络。 Pombe 由含RS结构域的蛋白和SR蛋白特异性激酶组成，因此确立了网络在真核生物中的重要性。

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