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首页> 外文期刊>Genes to cells : >Solution structures of yeast Saccharomyces cerevisiae calmodulin in calcium- and target peptide-bound states reveal similarities and differences to vertebrate calmodulin
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Solution structures of yeast Saccharomyces cerevisiae calmodulin in calcium- and target peptide-bound states reveal similarities and differences to vertebrate calmodulin

机译：酵母酿酒酵母钙调蛋白在钙和目标肽结合状态下的溶液结构揭示了与脊椎动物钙调蛋白的异同

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摘要

We determined the solution structures of the calmodulin (CaM) isoform from yeast Saccharomyces cerevisiae (yCaM) in the calcium-bound form and in complex with a target peptide using NMR spectroscopy and small-angle X-ray scattering (SAXS). yCaM shows a number of unique features distinct from the vertebrate CaM isoforms: (i) it has only approximately 60% sequence identity to vertebrate CaM; (ii) its fourth Ca2+-binding domain is inactivated by amino acid substitution. As NMR analyses of Ca2+-bound full-length yCaM implied that the fourth EF-hand motif region (EF4) presents a disordered conformation, we determined the solution structure of an EF4-deletion mutant of Ca2+-bound yCaM. The deletion mutant showed a compact globular structure, with the target recognition sites of the N-terminal domain and the third EF-hand region bound to each other. Furthermore, we determined the solution structure of Ca2+-bound yCaM complexed with a calcineurin-derived peptide. Interestingly, the structure closely resembled that of the vertebrate CaMcalcineurin complex, with the EF4 region in cooperation with the peptide binding. Moreover, the results of SAXS analyses were consistent with the NMR solution structures and showed the conformational changes of yCaM in three functional stages. These unique structural characteristics of yCaM are closely related to Ca2+-mediated signal transduction in yeast.
机译：我们使用核磁共振波谱法和小角度X射线散射（SAXS）方法，确定了来自啤酒酵母（yCaM）的钙结合形式且与目标肽复合的钙调蛋白（CaM）同工型的溶液结构。 yCaM显示出许多不同于脊椎动物CaM亚型的独特特征：（i）与脊椎动物CaM仅具有约60％的序列同一性; （ii）其第四个Ca 2+结合结构域通过氨基酸取代而失活。由于对Ca2 +结合的全长yCaM的NMR分析表明第四个EF手基序区域（EF4）呈现无序构象，因此我们确定了与Ca2 +结合的yCaM的EF4缺失突变体的溶液结构。缺失突变体显示出紧密的球状结构，其N-末端结构域的靶标识别位点与第三个EF-手区域相互结合。此外，我们确定了与钙调神经磷酸酶衍生的肽复合的Ca2 +结合的yCaM的溶液结构。有趣的是，该结构与脊椎动物CaMcalcineurin复合物的结构非常相似，其中EF4区与肽结合协同作用。此外，SAXS分析的结果与NMR溶液结构一致，并显示了yCaM在三个功能阶段的构象变化。 yCaM的这些独特的结构特征与酵母中Ca2 +介导的信号转导密切相关。

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