Journal
FEBS LETTERS
Volume 582, Issue 7, Pages 1129-1134Publisher
WILEY
DOI: 10.1016/j.febslet.2008.02.079
Keywords
glycylation; glycylase; nucleosome assembly protein; tubulin tyrosine ligase; histone; spermiogenesis
Funding
- NICHD NIH HHS [U01 HD045913-01, U01 HD045913-02, U01 HD045913-05, U01 HD045913-03, U01 HD045913-04] Funding Source: Medline
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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. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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