Premium
Structure of the C‐Terminal Tail of α‐Tubulin: Increase of Heterogeneity from Newborn to Adult
Author(s) -
Redeker Virginie,
Rusconi Filippo,
Mary Jean,
Promé Danielle,
Rossier Jean
Publication year - 1996
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1996.67052104.x
Subject(s) - tubulin , residue (chemistry) , peptide , biology , biochemistry , terminal (telecommunication) , amino acid , chemistry , microtubule , microbiology and biotechnology , telecommunications , computer science
A combination of posttranslational modifications contributes to the high heterogeneity of brain tubulin in mammals. In this report, the structures of the detyrosinated carboxy‐terminal peptides of α‐tubulin from newborn and adult mouse brain were compared. The heterogeneity of these carboxy‐terminal peptides was observed to increase from newborn to adult brain tubulin. The major part of this increased heterogeneity is due to the posttranslational excision of Glu 450 , which makes α‐tubulin nontyrosinatable (Δ‐2 tubulin). The structures of the polyglutamyl side chain of the bi‐ and triglutamylated peptides were analyzed in this work. In polyglutamylation of α‐tubulin, the first glutamyl residue can only be amide‐linked to the γ‐carboxyl group of Glu 445 , but the additional residues may be linked either to the γ‐ or to the α‐carboxyl groups of the preceding one. By optimized reverse‐phase separations and comparison with synthetic peptides corresponding to all possible linkages for the biglutamylated (γ1α2, γ1γ2) and triglutamylated (γ1α2α3, γ1γ2γ3, γ1α2γ3, γ1γ2α3, γ1γ2α2) tubulin peptides, it was possible to conclude that the mode of linkage connecting the second and third additional glutamyl residues corresponds mostly to α‐bond structures, for both newborn and adult mice.