期刊
FEBS LETTERS
卷 583, 期 12, 页码 1957-1963出版社
WILEY
DOI: 10.1016/j.febslet.2009.05.003
关键词
Glycylase; Monoglycylase; Polyglycylase; Glutamylation; Glutamylase; Tubulin tyrosine ligase
资金
- JST
- JSPS
Tubulin can undergo unusual post-translational modifications, glycylation and glutamylation. We previously failed to find glycylase (glycine ligase) for tubulin while identifying TTLL10 as a polyglycylase for nucleosome assembly protein 1. We here examine whether TTLL10 performs tubulin glycylation. We used a polyclonal antibody (R-polygly) raised against a poly(glycine) chain, which does not recognize monoglycylated protein. R-polygly strongly reacted with mouse tracheal cilia and axonemal tubulins. R-polygly detected many proteins in cell lysates co-expressing TTLL10 with TTLL8. Two-dimensional electrophoresis revealed that the R-polygly-reactive proteins included alpha- and beta-tubulin. R-polygly labeling signals overlapped with microtubules. These results indicate that TTLL10 can strongly glycylate tubulin in a TTLL8-dependent manner. Furthermore, these two TTLL proteins can glycylate unidentified 170-, 110-, 75-, 40-, 35-, and 30-kDa acidic proteins. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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