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Synthetic peptides identify the minimal substrate requirements of tubulin polyglutamylase in side chain elongation
Author(s) -
Westermann Stefan,
Plessmann Uwe,
Weber Klaus
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01227-2
Subject(s) - tubulin , residue (chemistry) , side chain , chemistry , glutamic acid , stereochemistry , substrate (aquarium) , elongation , biochemistry , amino acid , microtubule , microbiology and biotechnology , biology , organic chemistry , materials science , polymer , ecology , ultimate tensile strength , metallurgy
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.