Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation.
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Rogowski K, Juge F, van Dijk J, Wloga D, Strub JM, Levilliers N, Thomas D, Bre MH, Van Dorsselaer A, Gaertig J, Janke C
Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation.
Cell. 2009 Jun 12;137(6):1076-87. doi: 10.1016/j.cell.2009.05.020.
- PubMed ID
- 19524510 [ View in PubMed]
- 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.
DrugBank Data that Cites this Article
- Polypeptides
Name UniProt ID Tubulin beta-1 chain Q9H4B7 Details Tubulin beta chain P07437 Details Tubulin alpha-1B chain P68363 Details Tubulin alpha-1A chain Q71U36 Details Tubulin alpha-8 chain Q9NY65 Details Tubulin beta-4B chain P68371 Details Tubulin alpha-1C chain Q9BQE3 Details Tubulin alpha-4A chain P68366 Details Tubulin beta-4A chain P04350 Details Tubulin beta-3 chain Q13509 Details Tubulin alpha-3C/D chain Q13748 Details Tubulin alpha-3E chain Q6PEY2 Details Tubulin beta-2A chain Q13885 Details Tubulin beta-2B chain Q9BVA1 Details Tubulin beta-6 chain Q9BUF5 Details Tubulin monoglycylase TTLL3 Q9Y4R7 Details