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FEBS Letters
Article . 2008 . Peer-reviewed
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FEBS Letters
Article . 2008
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TTLL10 is a protein polyglycylase that can modify nucleosome assembly protein 1

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

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

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.

Keywords

Male, Spermiogenesis, Molecular Sequence Data, Glutamic Acid, Cell Cycle Proteins, Antibodies, Mice, Animals, Amino Acid Sequence, Peptide Synthases, Glycylation, Glycylase, Nucleosome Assembly Protein 1, Nuclear Proteins, Tubulin tyrosine ligase, Immunohistochemistry, Spermatids, Mice, Inbred C57BL, Histone, Polyglutamic Acid, Nucleosome assembly protein, Carrier Proteins, Protein Processing, Post-Translational

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citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
49
Top 10%
Top 10%
Top 10%
bronze