Polyglycylation of tubulin: a posttranslational modification in axonemal microtubules.
A posttranslational modification was detected in the carboxyl-terminal region of axonemal tubulin from Paramecium. Tubulin carboxyl-terminal peptides were isolated and analyzed by Edman degradation sequencing, mass spectrometry, and amino acid analysis. All of the peptides, derived from both alpha and beta tubulin subunits, were modified by polyglycylation, containing up to 34 glycyl units covalently bound to the gamma carboxyl group of glutamyl residues. This modification, present in one of the most stable microtubular systems, may influence microtubule stability or axoneme function, or both.
Redeker
V
V
Institut Alfred Fessard, CNRS Unité Propre de Recherche 2212, Gif-sur-Yvette, France.
Levilliers
N
N
Schmitter
J M
JM
Le Caer
J P
JP
Rossier
J
J
Adoutte
A
A
Bré
M H
MH
D000595:Amino Acid Sequence; D000818:Animals; D002923:Cilia / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D018698:Glutamic Acid / Q000378:metabolism; D005998:Glycine / Q000032:analysis / Q000378:metabolism*; D013058:Mass Spectrometry; D008870:Microtubules / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D008969:Molecular Sequence Data; D010247:Paramecium / Q000378:metabolism* / Q000648:ultrastructure; D010455:Peptides / Q000032:analysis / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D014404:Tubulin / Q000032:analysis / Q000737:chemistry / Q000378:metabolism*
D010455:Peptides; D014404:Tubulin; C011080:polyglycine; D018698:Glutamic Acid; D005998:Glycine