Mapping N-Glycosylation Sites across Seven Evolutionarily Distant Species Reveals a Divergent Substrate Proteome Despite a Common Core Machinery
2012; Elsevier BV; Volume: 46; Issue: 4 Linguagem: Inglês
10.1016/j.molcel.2012.04.031
ISSN1097-4164
AutoresDorota Zielińska, Florian Gnad, Katharina Schropp, Jacek R. Wiśniewski, Matthias Mann,
Tópico(s)Studies on Chitinases and Chitosanases
ResumoSummary 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.
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