凝溶胶蛋白的第2结构域直接与原肌球蛋白结合。

Domain 2 of gelsolin binds directly to tropomyosin.

作者信息

Maciver S K, Ternent D, McLaughlin P J

机构信息

Genes and Development Group, Department of Biomedical Sciences, University of Edinburgh, Hugh Robson Building, George Square, Edinburgh, UK.

出版信息

FEBS Lett. 2000 May 4;473(1):71-5. doi: 10.1016/s0014-5793(00)01507-6.

DOI:10.1016/s0014-5793(00)01507-6

PMID:10802062

Abstract

Gelsolin is an actin filament severing protein composed of six similar structured domains that differ with respect to actin, calcium and polyphospho-inositide binding. Previous work has established that gelsolin binds tropomyosin [Koepf, E.K. and Burtnick, L.D. (1992) FEBS Lett. 309, 56-58]. We have produced various specific gelsolin domains in Escherichia coli in order to establish which of the six domains binds tropomyosin. Gelsolin domains 1-3 (G1-3), G1-2 and G2 all bind tropomyosin in a pH and calcium insensitive manner whereas binding of G4-6 to tropomyosin was barely detectable under the conditions tested. We conclude that gelsolin binds tropomyosin via domain 2 (G2).

摘要

凝溶胶蛋白是一种肌动蛋白丝切断蛋白，由六个结构相似的结构域组成，这些结构域在肌动蛋白、钙和多磷酸肌醇结合方面存在差异。先前的研究已经证实凝溶胶蛋白能结合原肌球蛋白[科夫，E.K.和伯特尼克，L.D.（1992年）《欧洲生物化学学会联合会快报》309，56 - 58]。我们在大肠杆菌中制备了各种特定的凝溶胶蛋白结构域，以确定六个结构域中哪一个能结合原肌球蛋白。凝溶胶蛋白结构域1 - 3（G1 - 3）、G1 - 2和G2都以对pH和钙不敏感的方式结合原肌球蛋白，而在测试条件下几乎检测不到G4 - 6与原肌球蛋白的结合。我们得出结论，凝溶胶蛋白通过结构域2（G2）结合原肌球蛋白。