Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation. - Archive ouverte HAL Access content directly
Journal Articles Cell Year : 2009

Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation.

Abstract

Polyglycylation is a posttranslational modification that generates glycine side chains on proteins. Here we identify a family of evolutionarily conserved glycine ligases that modify tubulin using different enzymatic mechanisms. In mammals, two distinct enzyme types catalyze the initiation and elongation steps of polyglycylation, whereas Drosophila glycylases are bifunctional. We further show that the human elongating glycylase has lost enzymatic activity due to two amino acid changes, suggesting that the functions of protein glycylation could be sufficiently fulfilled by monoglycylation. Depletion of a glycylase in Drosophila using RNA interference results in adult flies with strongly decreased total glycylation levels and male sterility associated with defects in sperm individualization and axonemal maintenance. A more severe RNAi depletion is lethal at early developmental stages, indicating that protein glycylation is essential. Together with the observation that multiple proteins are glycylated, our functional data point towards a general role of glycylation in protein functions.
Fichier principal
Vignette du fichier
Rogowski_2009.pdf (3.44 Mo) Télécharger le fichier
Origin : Files produced by the author(s)
Loading...

Dates and versions

hal-00400172 , version 1 (11-01-2010)

Identifiers

Cite

Krzysztof Rogowski, François Juge, Juliette van Dijk, Dorota Wloga, Jean-Marc Strub, et al.. Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation.. Cell, 2009, 137 (6), pp.1076-87. ⟨10.1016/j.cell.2009.05.020⟩. ⟨hal-00400172⟩
470 View
276 Download

Altmetric

Share

Gmail Facebook X LinkedIn More