Phosphorylation of the N-terminal region of Caenorhabditis elegans paramyosin.
Phosphorylation of the N-terminal region of Caenorhabditis elegans paramyosin.
复制标题
秀丽隐杆线虫副肌球蛋白 N 末端区域的磷酸化。
DOI：
10.1016/0022-2836(89)90267-2
复制
发表时间：
1989
影响因子：
5.6
通讯作者：
Waterson,RH
中科院分区：
文献类型：
--
作者：
Schriefer,LA;Waterson,RH
对秀丽线虫的副肌球蛋白进行了翻译后的磷酸化修饰。从混合年龄动物群体中提纯的副肌球蛋白每摩尔副肌球蛋白含有0.7至2.0摩尔的磷酸盐。在体外，副肌球蛋白也被颗粒组分中的一种内源性激酶磷酸化。副肌球蛋白蛋白体外磷酸化的分析与unc-15副肌球蛋白基因OFC的DNA序列比较。α表明，非ELEX-螺旋N-末端区域的丝氨酸残基是该激酶的靶标。副肌球蛋白的N-末端区域与两个体壁肌球蛋白重链OFC的非螺旋C-末端区域有显著的相似性。优雅女装。这三个区域都包含三个拷贝的Ser-∗-Ser-∗-Ala基序，这是副肌球蛋白最有可能的磷酸化目标，这表明这些区域可能被相同的激酶修饰。
Paramyosin fromCaenorhabditis eleganswas examined for post-translational modification by phosphorylation. Paramyosin purified from populations of mixed-age animals contained 0.7 to 2.0 moles of phosphate per mole of paramyosin. Paramyosin was also phosphorylatedin vitroby an endogenous kinase in the particulate fraction. Analysis of thein vitrophosphorylated paramyosin in comparison with the DNA sequence of theunc-15 paramyosin gene ofC. elegansshows that serine residues in the non-α-helical N-terminal region are the targets of the kinase. The N-terminal region of paramyosin has significant similarity to the non-helical C-terminal region of the two body wall myosin heavy chains ofC. elegans. All three regions contain three copies of a Ser-∗-Ser-∗-Ala motif, the most likely target for phosphorylation in paramyosin, suggesting that these regions may be modified by the same kinase.