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多头绒泡菌的F-肌动蛋白封端蛋白:帽蛋白42(a)即便不完全相同,也与凝溶蛋白非常相似,并且在结构和功能上与凝溶胶蛋白高度同源;帽蛋白42(b)是绒泡菌肌动蛋白。

The F-actin capping proteins of Physarum polycephalum: cap42(a) is very similar, if not identical, to fragmin and is structurally and functionally very homologous to gelsolin; cap42(b) is Physarum actin.

作者信息

Ampe C, Vandekerckhove J

机构信息

Laboratorium voor Genetica, Rijksuniversiteit Gent, Belgium.

出版信息

EMBO J. 1987 Dec 20;6(13):4149-57. doi: 10.1002/j.1460-2075.1987.tb02761.x.

Abstract

We have carried out a primary structure analysis of the F-actin capping proteins of Physarum polycephalum. Cap42(b) was completely sequenced and was found to be identical with Physarum actin. Approximately 88% of the sequence of cap42(a) was determined. Cap42(a) and fragmin were found to be identical by amino acid composition, isoelectric point, mol. wt, elution time on reversed-phase chromatography and amino acid sequence of their tryptic peptides. The available sequence of cap42(a) is greater than 36% homologous with the NH2-terminal 42-kd domain of human gelsolin. A highly homologous region of 16 amino acids is also shared between cap42(a), gelsolin and the Acanthamoeba profilins. Cap42(a) binds two actin molecules in a similar way to gelsolin suggesting a mechanism of F-actin modulation that has been conserved during evolution.

摘要

我们对多头绒泡菌的F-肌动蛋白封端蛋白进行了一级结构分析。Cap42(b)已完全测序,发现它与绒泡菌肌动蛋白相同。确定了Cap42(a)约88%的序列。通过氨基酸组成、等电点、分子量、反相色谱洗脱时间及其胰蛋白酶肽的氨基酸序列,发现Cap42(a)和凝溶蛋白相同。Cap42(a)的现有序列与人类凝溶胶蛋白的NH2末端42-kd结构域的同源性大于36%。Cap42(a)、凝溶胶蛋白和棘阿米巴肌动蛋白单体结合蛋白之间也共享一个16个氨基酸的高度同源区域。Cap42(a)以与凝溶胶蛋白类似的方式结合两个肌动蛋白分子,这表明在进化过程中保守的F-肌动蛋白调节机制。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ced/553898/2b85fac0216b/emboj00253-0271-a.jpg

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