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 是酿酒酵母中减数分裂特异性 Ime2 蛋白激酶的共有磷酸受体序列。

• 影响指数: 3.321
• 发表时间: Jan 2007 9
• 来源期刊: Biochemistry
• DOI: 10.1021/bi061858p
• PMID: 17198398
• 文章类型: Journal Article
• 中科院分区: Q2
• 方向: 生物
• 作者列表: Moore M,Shin ME,Bruning A,Schindler K,Vershon A,Winter E

Mesh: Amino Acid Motifs; Carrier Proteins / genetics metabolism; Cell Cycle Proteins / genetics metabolism; Intracellular Signaling Peptides and Proteins; Meiosis; Nuclear Proteins / chemistry genetics metabolism; Phosphorylation; Protein Kinases / genetics metabolism; Protein Phosphatase 1; Protein Serine-Threonine Kinases; RecQ Helicases / genetics metabolism; Repressor Proteins; Saccharomyces cerevisiae / enzymology genetics metabolism; Saccharomyces cerevisiae Proteins / chemistry genetics metabolism; Threonine / analysis metabolism; Transcription, Genetic

Abstract

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.

摘要

Ime2是酿酒酵母中减数分裂特异性蛋白激酶，在功能上与细胞周期蛋白依赖性激酶相关。尽管Ime2调节减数分裂的多个步骤，只有少数底物被鉴定出来。在这里，我们显示Ime2磷酸化Sum1，减数分裂基因转录的阻遏物，在Thr-306上。使用Sum1突变体和合成肽的Ime2蛋白激酶测定定义了Ime2有效磷酸化所需的共有Arg-Pro-X-Ser/Thr基序。邻近磷酸受体(+1位置)的羧基残基也影响Ime2磷酸化的效率,丙氨酸是优选的残基。该信息在识别新的潜在Ime2靶标方面具有预测价值，如Ime2在体外磷酸化Sgs1和Gip1的能力所示，并且在分化有丝分裂和减数分裂调节途径中可能很重要。