Strasser P, Gimona M, Herzog M, Geiger B, Small J V
Institute of Molecular Biology, Austrian Academy of Sciences, Salzburg.
FEBS Lett. 1993 Feb 15;317(3):189-94. doi: 10.1016/0014-5793(93)81274-4.
Metavinculin differs from vinculin in having an additional insert of 68 to 79 amino acids in length in the C-terminal half of the molecule. Cross-species comparison of metavinculin sequences from pig, man, chicken and frog reveals a division of the insert into two parts: the first variable and the second highly conserved. The longest insert, 79 amino acids, was found in Xenopus laevis. Three different C-terminal constructs of vinculin and metavinculin over-expressed in E. coli could be purified by column chromatography. Two-dimensional gel electrophoresis and peptide analysis revealed pI values between 8.35 and 10.25 for the recombinant proteins. Biochemical and structural features of the metavinculin-specific sequence and the conserved vinculin/metavinculin carboxy-terminus are discussed.
间线蛋白与纽蛋白的不同之处在于，在分子的C端一半区域有一段额外的68至79个氨基酸长度的插入序列。对猪、人、鸡和蛙的间线蛋白序列进行跨物种比较发现，该插入序列可分为两部分：第一部分可变，第二部分高度保守。在非洲爪蟾中发现了最长的插入序列，有79个氨基酸。在大肠杆菌中过表达的纽蛋白和间线蛋白的三种不同C端构建体可通过柱色谱法纯化。二维凝胶电泳和肽分析显示，重组蛋白的pI值在8.35至10.25之间。文中讨论了间线蛋白特异性序列以及保守的纽蛋白/间线蛋白羧基末端的生化和结构特征。
