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首页> 外文期刊>Biochemistry >Influence of Myristoylation, Phosphorylation, and Deamidation on the Structural Behavior of the N-Terminus of the Catalytic Subunit of CAMP-Dependent Protein Kinas
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Influence of Myristoylation, Phosphorylation, and Deamidation on the Structural Behavior of the N-Terminus of the Catalytic Subunit of CAMP-Dependent Protein Kinas

机译：肉豆蔻酰化，磷酸化和脱酰胺对CAMP依赖蛋白激酶的催化亚基的N末端的结构行为的影响。

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摘要

A number of isoenzymes of the catalytic subunit of cAMP-dependent protein kinase arise through post translational modifications of the enzyme outside the catalytic domain; the biological significance of these is not yet fully clear. A clustering of sites for such modification exists at the N-terminus of the protein, where myristoylation (of Glyl), phosphorylation (at SerlO), and dearnidation of Asn2 have been observed. As the first two are known to govern membrane binding and thus subcellular compartmentalization in some proteins, it was of interest to see whether the local structure of the N-terminus was being influenced by one or more of these modifications. A series of synthetic peptides mimicing the 16 N-terminal residues of the catalytic subunit Ca. was produced covering the full range of possible modifications, singly and in combination, and tested for possible effects on local structure by measuring the circular dichroism under varying polarity. It was found that myristoylation and phosphorylation modify the structure in this region in opposite ways and in a manner designed to amplify the action of a potential myristoy1/electrostatic switch. To what extent dearnidation of Asn2 may oppose a potential membrane binding is unknown. Deamidation, however, had no effect on the structure of the peptide either alone or in combination with acylation and/or phosphorylation, suggesting that the change of the nuclear/cytoplasmic disribution in cells caused by dearnidation [Pepperkok et al. (2000) I. Cell BioI. 148,715-726] is due to a more complex signaling mechanism. The structural implications of the data are discussed.
机译：cAMP依赖性蛋白激酶的催化亚基的许多同工酶是通过在催化结构域外对酶进行翻译后修饰而产生的。这些的生物学意义尚未完全清楚。在蛋白质的N-末端存在用于这种修饰的位点的簇，其中已经观察到（Glyl的）肉豆蔻酰化，（Ser10的）磷酸化和Asn2的脱酰胺化。由于已知前两个分子控制膜结合，从而控制某些蛋白质的亚细胞区室化，因此有兴趣观察一下N端的局部结构是否受到一个或多个这些修饰的影响。一系列合成肽，模拟催化亚基Ca的16个N端残基。单独或组合生产了涵盖所有可能修饰范围的产品，并通过测量在不同极性下的圆二色性来测试对局部结构的可能影响。发现肉豆蔻酰化和磷酸化以相反的方式并且以设计用于放大潜在的肉豆蔻酰1 /静电开关的作用的方式来修饰该区域中的结构。尚不清楚Asn2的脱酰胺作用在多大程度上可以对抗潜在的膜结合。然而，脱酰胺作用单独或与酰化和/或磷酸化结合对肽的结构都没有影响，这表明由脱酰胺作用引起的细胞核/细胞质分布的变化[Pepperkok等人，J.Biol.Chem.Soc。，1992，8，5119]。 （2000）I.细胞生物学。 [148,715-726]是由于更复杂的信令机制。讨论了数据的结构含义。

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