Publication Information
Zielinska et al., 2012
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Abstract
Mol Cell. 2012 May 25;46(4):542-8. doi: 10.1016/j.molcel.2012.04.031.
Mapping N-glycosylation sites across seven evolutionarily distant species
reveals a divergent substrate proteome despite a common core machinery.
Zielinska DF(1), Gnad F, Schropp K, Wiśniewski JR, Mann M.
Author information:
(1)Department of Proteomics and Signal Transduction, Max-Planck-Institute of
Biochemistry, Martinsried 82152, Germany.
N-linked glycosylation is an important posttranslational modification in all
eukaryotes, but little is known about the N-glycoproteomes in nonmammalian
systems. Here, we measure N-glycoproteomes of the major model organisms
Arabidopsis thaliana, Schizosaccharomyces pombe, Saccharomyces cerevisiae,
Caenorhabditis elegans, Drosophila melanogaster, and Danio rerio,
representatively spanning the eukaryotic domain of life. The number of detected
N-glycosylation sites varied between 425 in fission yeast, 516 in budding yeast,
1,794 in worm, 2,186 in plant, 2,229 in fly, and 2,254 in zebrafish. We find
that all eukaryotic N-glycoproteomes have invariant characteristics including
sequence recognition patterns, structural constraints, and subcellular
localization. However, a surprisingly large percentage of the N-glycoproteome
evolved after the phylogenetic divergences between plants, fungi, nematodes,
insects, and vertebrates. Many N-glycosylated proteins coevolved with the rise
of extracellular processes that are specific within corresponding phylogenetic
groups and essential for organismal development, body growth, and organ
formation.
Copyright © 2012 Elsevier Inc. All rights reserved.
DOI: 10.1016/j.molcel.2012.04.031
PMID: 22633491 [Indexed for MEDLINE]
