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Structure of the polyglutamyl chain of tubulin: Occurrence of alpha and gamma linkages between glutamyl units revealed by monoreactive polyclonal antibodies
Author(s) -
Wolff Annie,
Houdayer Monique,
Chillet Denise,
Néchaud Béatrice,
Denoulet Philippe
Publication year - 1994
Publication title -
biology of the cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 85
eISSN - 1768-322X
pISSN - 0248-4900
DOI - 10.1016/0248-4900(94)90049-3
Subject(s) - polyclonal antibodies , biology , alpha (finance) , tubulin , antibody , microbiology and biotechnology , alpha chain , biochemistry , immunology , microtubule , gene , developmental psychology , construct validity , psychology , psychometrics
Summary— Polyglutamylation, a posttranslational modification which consists of the sequential addition of one to six glutamyl units in the carboxy‐terminal domain of both tubulin subunits, is a major event in neurons. Its structure has been investigated by using monoreactive polyclonal antibodies directed against distinct glutamylation motifs, ie α‐ and γ‐linkages between glutamyl units. It is shown that, beside α‐linkages previously characterized, γ‐Linkages also occur in glutamyl chains of brain tubulin. The co‐existence of these two basic motifs leads to a conception of the polyglutamyl chain with a very sophisticated structure which could, through its complexity, help the microtubule to reach its structure and fulfil its functions.