Arg-Pro-X-Ser/Thr is a consensus phosphoacceptor sequence for the meiosis-specific Ime2 protein kinase in Saccharomyces cerevisiae
Arg-Pro-X-Ser/Thr is a consensus phosphoacceptor sequence for the meiosis-specific Ime2 protein kinase in Saccharomyces cerevisiae
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DOI：
10.1021/bi061858p
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发表时间：
2007-01-09
期刊：
影响因子：
2.9
通讯作者：
Winter, Edward
中科院分区：
文献类型：
--
作者：
Moore, Michael;Shin, Marcus E.;Winter, Edward
IME2是酿酒酵母中一种减数分裂特异的蛋白激酶，与细胞周期蛋白依赖性激酶功能相关。虽然IME2调节减数分裂的多个步骤，但只有几种底物被鉴定出来。在这里，我们证明了IME2磷酸化Sum1，一个减数分裂基因转录的抑制因子，在Thr-306上。用Sum1突变体和合成肽对IME2蛋白激酶进行分析，确定了一个一致的Arg-Pro-X-Ser/Thr基序，这是IME2有效磷酸化所必需的。靠近磷受体(+1位)的羧基残基也影响IME2的磷酸化效率，丙氨酸是首选残基。这一信息在识别新的潜在的IME2靶点方面具有预测价值，如IME2在体外对SGS1和Gip1进行磷酸化的能力所表明的，并且在区分有丝分裂和减数分裂调控途径方面可能是重要的。
Ime2 is a meiosis-specific protein kinase in Saccharomyces cerevisiae that is functionally related to cyclin-dependent kinase. Although Ime2 regulates multiple steps in meiosis, only a few of its substrates have been identified. Here we show that Ime2 phosphorylates Sum1, a repressor of meiotic gene transcription, on Thr-306. Ime2 protein kinase assays with Sum1 mutants and synthetic peptides define a consensus Arg-Pro-X-Ser/Thr motif that is required for efficient phosphorylation by Ime2. The carboxyl residue adjacent to the phosphoacceptor (+1 position) also influences the efficiency of Ime2 phosphorylation with alanine being a preferred residue. This information has predictive value in identifying new potential Ime2 targets as shown by the ability of Ime2 to phosphorylate Sgs1 and Gip1 in vitro and could be important in differentiating mitotic and meiotic regulatory pathways.