Schröder S, Morris S A, Knorr R, Plessmann U, Weber K, Nguyen G V, Ungewickell E
Max-Planck-Institute for Biochemistry, Martinsried, Germany.
Eur J Biochem. 1995 Mar 1;228(2):297-304.
The protein auxilin is a coat component of brain clathrin-coated vesicles. It interacts directly with the heavy chain of clathrin and supports its assembly into regular cages [Ahle, S. & Ungewickell, E. (1990) J. Cell Biol. 111, 19-29]. The combined open reading frames of three cow brain cDNA clones with a total of 4531 nucleotides predict a molecular mass of 99,504 Da for auxilin. The coding region is followed by a very long untranslated region of at least 1670 nucleotides. By Northern analysis, auxilin transcripts are found only in brain tissue. Auxilin is not related to any of the previously sequenced clathrin-binding proteins, but the region of positions 50-350 is 29% identical (similarity 56%) to the corresponding region of the actin-binding protein tensin from chicken fibroblasts. Recombinant auxilin expressed in and purified from bacteria by affinity chromatography is functional with respect to clathrin binding.
辅助蛋白是脑网格蛋白包被小泡的包被成分。它直接与网格蛋白重链相互作用，并支持其组装成规则的笼状结构[阿勒，S. & 翁格维克勒，E.（1990年）《细胞生物学杂志》111卷，第19 - 29页]。三个牛脑cDNA克隆的联合开放阅读框总共4531个核苷酸，预测辅助蛋白的分子量为99,504道尔顿。编码区后面是至少1670个核苷酸的非常长的非翻译区。通过Northern分析，仅在脑组织中发现辅助蛋白转录本。辅助蛋白与任何先前测序的网格蛋白结合蛋白均无关联，但50 - 350位区域与来自鸡成纤维细胞的肌动蛋白结合蛋白张力蛋白的相应区域有29%的同一性（相似性为56%）。通过亲和层析在细菌中表达并纯化的重组辅助蛋白在网格蛋白结合方面具有功能。
