| First Author | Ikegami K | Year | 2008 |
| Journal | FEBS Lett | Volume | 582 |
| Issue | 7 | Pages | 1129-34 |
| PubMed ID | 18331838 | Mgi Jnum | J:133337 |
| Mgi Id | MGI:3778306 | Doi | 10.1016/j.febslet.2008.02.079 |
| Citation | Ikegami K, et al. (2008) TTLL10 is a protein polyglycylase that can modify nucleosome assembly protein 1. FEBS Lett 582(7):1129-34 |
| abstractText | Certain proteins can undergo polyglycylation and polyglutamylation. Polyglutamylases (glutamate ligases) have recently been identified in a family of tubulin tyrosine ligase-like (TTLL) proteins. However, no polyglycylase (glycine ligase) has yet been reported. Here we identify a polyglycylase in the TTLL proteins by using an anti-poly-glycine antibody. The antibody reacted with a cytoplasmic 60-kDa protein that accumulated in elongating spermatids. Using tandem mass spectrometry of trypsinized samples, immunoprecipitated by the antibody from the TTLL10-expressing cells, we identified the 60-kDa protein as nucleosome assembly protein 1 (NAP1). Recombinant TTLL10 incorporated glycine into recombinant NAP1 in vitro. Mutational analyses indicated that Glu residues at 359 and 360 in the C-terminal part of NAP1 are putative sites for the modification. Thus, TTLL10 is a polyglycylase for NAP1. |
