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首页> 外文期刊>Acta crystallographica. Section D, Structural biology. >Structural insights into the recognition of phosphorylated Hop1 by Mek1
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Structural insights into the recognition of phosphorylated Hop1 by Mek1

机译：结构识别的见解的磷酸化Hop1 Mek1

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摘要

The FHA domain‐containing protein Mek1 is a meiosis‐specific kinase that is involved in the regulation of interhomolog recombination in meiosis in Saccharomyces cerevisiae . The recruitment and activation of Mek1 require the phosphorylation of the chromosome axis protein Hop1 at Thr318 (pT318), which is necessary for recognition by the Mek1 FHA domain. Here, crystal structures of the Mek1 FHA domain in the apo state and in complex with the Hop1 pT318 peptide are presented, demonstrating that the hydrophobic residues Phe320 and Val321 at the pT+2 and pT+3 positions in the ligand contribute to the preferential recognition. It was further found that in Schizosaccharomyces pombe Mek1 FHA binds both pT15 in its N‐terminal SQ/TQ cluster domain (SCD) and pT270 in the Hop1 SCD. The results revealed the structural basis for the preferential recognition of phosphorylated Hop1 by Mek1 in S. cerevisiae and facilitate the understanding of the interaction between the S. pombe Mek1 FHA domain and its binding targets.
机译：FHA域包含蛋白质Mek1地理减数分裂激酶参与了监管interhomolog重组在酿酒酵母减数分裂。招聘和激活Mek1要求蛋白质磷酸化的染色体轴Hop1 Thr318 (pT318),这是必要的识别由Mek1 FHA域。apo Mek1 FHA的结构域状态和在复杂Hop1 pT318肽疏水性,证明残留Phe320和Val321 pT + 2和pT + 3配体为位置优惠的认可。在粟酒裂殖酵母Mek1 FHA绑定两pT15 N量终端平方/ TQ集群域(SCD)和pT270 Hop1化合物。揭示了结构基础识别磷酸化Hop1优惠Mek1在酿酒酵母和促进的理解之间的交互。非洲酒Mek1 FHA域及其约束力的目标。

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