Work

TTLL10 is a protein polyglycylase that can modify nucleosome assembly protein 1

Year: 2008

Type: article

Abstract: 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.

Source: FEBS Letters

DOI: 10.1016/j.febslet.2008.02.079

Authors: Koji Ikegami, Daisuke Horigome, Masahiro Mukai, Itamar Livnat, Grant R. MacGregor, Mitsutoshi Setou

Institutions: University of California, Irvine, Hamamatsu University, Hamamatsu University School of Medicine

Language: English

Topic: Genomics and Chromatin Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Institutes of Health, Eunice Kennedy Shriver National Institute of Child Health and Human Development

Award: A Novel Gene Required for Sertoli-Spermatids Adhesion