Structure of the polyglutamyl chain of tubulin: occurrence of alpha and gamma linkages between glutamyl units revealed by monoreactive polyclonal antibodies.
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 alpha- and gamma-linkages between glutamyl units. It is shown that, beside alpha-linkages previously characterized, gamma-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.
Wolff
A
A
Laboratoire de Biochimie Cellulaire, CNRS-URA 1115, Collège de France, Paris.
Houdayer
M
M
Chillet
D
D
de Néchaud
B
B
Denoulet
P
P
D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies; D001923:Brain Chemistry; D004797:Enzyme-Linked Immunosorbent Assay; D018698:Glutamic Acid / Q000737:chemistry*; D015151:Immunoblotting; D051379:Mice; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010455:Peptides / Q000138:chemical synthesis* / Q000276:immunology; D011487:Protein Conformation; D014404:Tubulin / Q000737:chemistry* / Q000276:immunology
D000906:Antibodies; D010455:Peptides; D014404:Tubulin; D018698:Glutamic Acid