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TTLL10 is a protein polyglycylase that can modify nucleosome assembly protein 1
Author(s) -
Ikegami Koji,
Horigome Daisuke,
Mukai Masahiro,
Livnat Itamar,
MacGregor Grant R.,
Setou Mitsutoshi
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.02.079
Subject(s) - recombinant dna , immunoprecipitation , dna ligase , biochemistry , microbiology and biotechnology , biology , trypsinization , tyrosine , chemistry , enzyme , gene , trypsin
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.