Janke Carsten, Rogowski Krzysztof, Wloga Dorota, Regnard Catherine, Kajava Andrey V, Strub Jean-Marc, Temurak Nevzat, van Dijk Juliette, Boucher Dominique, van Dorsselaer Alain, Suryavanshi Swati, Gaertig Jacek, Eddé Bernard
Centre de Recherches de Biochimie Macromoléculaire, CNRS, 34293 Montpellier, France.
Science. 2005 Jun 17;308(5729):1758-62. doi: 10.1126/science.1113010. Epub 2005 May 12.
Polyglutamylation of tubulin has been implicated in several functions of microtubules, but the identification of the responsible enzyme(s) has been challenging. We found that the neuronal tubulin polyglutamylase is a protein complex containing a tubulin tyrosine ligase-like (TTLL) protein, TTLL1. TTLL1 is a member of a large family of proteins with a TTL homology domain, whose members could catalyze ligations of diverse amino acids to tubulins or other substrates. In the model protist Tetrahymena thermophila, two conserved types of polyglutamylases were characterized that differ in substrate preference and subcellular localization.
微管蛋白的多聚谷氨酰胺化与微管的多种功能有关，但确定相关酶一直具有挑战性。我们发现神经元微管蛋白多聚谷氨酰胺酶是一种包含微管蛋白酪氨酸连接酶样（TTLL）蛋白TTLL1的蛋白质复合物。TTLL1是一个具有TTL同源结构域的大家族蛋白质成员，其成员可催化多种氨基酸与微管蛋白或其他底物的连接。在模式原生生物嗜热四膜虫中，鉴定出了两种保守的多聚谷氨酰胺酶类型，它们在底物偏好和亚细胞定位上有所不同。
