Synthetic peptides identify the minimal substrate requirements of tubulin polyglutamylase in side chain elongation

FEBS Letters

Weber, Klaus¹  Westermann, Stefan¹  Plessmann, Uwe¹ 

[1] Max Planck Institute for Biophysical Chemistry, Department of Biochemistry, Am Fassberg 11, 37077 Goettingen, Germany

关键词: Polyglutamylation;    Trypanosomatid;    Post-translational modification;    Tubulin;    Crithidia fasciculata;   

DOI  :  10.1016/S0014-5793(99)01227-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The minimal sequence requirement of Crithidia tubulin polyglutamylase is already fulfilled by tubulin-related peptides carrying a free α-carboxylate on a glutamic acid residue. Since the product of each glutamylation step fulfills the substrate requirements necessary for the next cycle, very long side chains are generated with brain tubulin as a substrate. Up to 70 mol of glutamic acid was incorporated per αβ-heterodimer. We speculate that the strict choice of a particular glutamate residue for the formation of the isopeptide bond initiating a novel side chain is made by a tubulin monoglutamylase which requires the entire tubulin as substrate.

【 授权许可】

Unknown