TTLL10 can perform tubulin glycylation when co-expressed with TTLL8 |
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Authors: | Koji Ikegami |
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Affiliation: | a Department of Molecular Anatomy, Molecular Imaging Advanced Research Center, Hamamatsu University School of Medicine, 1-20-1 Handayama, Hamamatsu, Shizuoka 431-3192, Japan b Mitsubishi Kagaku Institute of Life Sciences (MITILS), Machida, Tokyo 194-8511, Japan |
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Abstract: | 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 α- and β-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. |
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Keywords: | NAP1, nucleosome assembly protein 1 PTM, post-translational modification TTL, tubulin tyrosine ligase TTLL, TTL-like R-polygly, anti-poly-glycine polyclonal antibody mAb, monoclonal antibody cDNA, complementary DNA PCR, polymerase chain reaction PBS, phosphate-buffered saline |
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