在同一个肌动蛋白单体上存在两个相同的疏水簇：一个肌球蛋白亚片段-1与两个肌动蛋白单体之间的相互作用。

Two identical hydrophobic clusters are present on the same actin monomer: interaction between one myosin subfragment-1 and two actin monomers.

作者信息

Labbé J P, Boyer M, Benyamin Y

机构信息

UPR 9008 Centre de Recherches de Biochimie Macrmoléculaire (CNRS), U249 (INSERM), Montpellier, France.

出版信息

FEBS Lett. 1995 Oct 16;373(3):221-4. doi: 10.1016/0014-5793(95)01044-f.

DOI:10.1016/0014-5793(95)01044-f

PMID:7589470

Abstract

Two-dimensional hydrophobic clusters analysis (HCA) was used to compare the distribution of hydrophobic clusters along various actin sequence. HCA-deduced patterns were not altered by amino-acid variations throughout the evolution of actin and we observed similar hydrophobic motifs comprising myosin subfragment-1 ATP-independent binding sites. HCA suggested the presence of two groups of identical hydrophobic motifs (A1 and A2) which bound on each side of the S1 (63 kDa-31 kDa) connecting segment in relation with two actin monomers. This connection is important in communications between actin- and nucleotide-binding sites. We postulate that some relation and message between the two motifs A1 and A2 take place through myosin subfragment-1 (63 kDa-31 kDa) connecting segment.

摘要

二维疏水簇分析（HCA）用于比较疏水簇沿各种肌动蛋白序列的分布。在肌动蛋白的整个进化过程中，HCA推导的模式不会因氨基酸变异而改变，并且我们观察到包含肌球蛋白亚片段-1非ATP依赖性结合位点的类似疏水基序。HCA表明存在两组相同的疏水基序（A1和A2），它们与两个肌动蛋白单体相关，结合在S1（63 kDa - 31 kDa）连接段的两侧。这种连接在肌动蛋白和核苷酸结合位点之间的通讯中很重要。我们推测，两个基序A1和A2之间的某些关系和信息是通过肌球蛋白亚片段-1（63 kDa - 31 kDa）连接段传递的。