Proteomics Reveals N-Linked Glycoprotein Diversity in Caenorhabditis elegans and Suggests an Atypical Translocation Mechanism for Integral Membrane Proteins.

Proteomics Reveals N-Linked Glycoprotein Diversity in Caenorhabditis elegans and Suggests an Atypical Translocation Mechanism for Integral Membrane Proteins. Research Abstract Details 

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Proteomics Reveals N-Linked Glycoprotein Diversity in Caenorhabditis elegans and Suggests an Atypical Translocation Mechanism for Integral Membrane Proteins. Abstract Text:

Hiroyuki Kaji,Jun-Ichi Kamiie,Hirotaka Kawakami,Kazuki Kido,Yoshio Yamauchi,Takashi Shinkawa,Masato Taoka,Nobuhiro Takahashi,Toshiaki Isobe,Hiroyuki Kaji,Jun-Ichi Kamiie,Hirotaka Kawakami,Kazuki Kido,Yoshio Yamauchi,Takashi Shinkawa,Masato Taoka,Nobuhiro Takahashi,Toshiaki Isobe,

Protein glycosylation is one of the most common post-translational modifications in eukaryotes and affects various aspects of protein structure and function. To facilitate studies of protein glycosylation, we paired glycosylation site-specific stable isotope tagging of lectin affinity-captured N-linked glycopeptides with mass spectrometry and determined 1,465 N-glycosylated sites on 829 proteins expressed in Caenorhabditis elegans. The analysis shows the diversity of protein glycosylation in eukaryotes in terms of glycosylation sites and oligosaccharide structures attached to polypeptide chains and suggests the substrate specificity of oligosaccharyltransferase, a single multienzyme complex in C. elegans that incorporates an oligosaccharide moiety en bloc to newly synthesized polypeptides. In addition, topological analysis of 257 N-glycosylated proteins containing a putative single transmembrane segment that were identified based on the relative positions of glycosylation sites and transmembrane segments suggests that an atypical non-cotranslational mechanism translocates large N-terminal segments from the cytosol to the endoplasmic reticulum lumen in the absence of signal sequence function.

Proteomics Reveals N-Linked Glycoprotein Diversity in Caenorhabditis elegans and Suggests an Atypical Translocation Mechanism for Integral Membrane Proteins. Publishing Authors By Initials

H Kaji,J Kamiie,H Kawakami,K Kido,Y Yamauchi,T Shinkawa,M Taoka,N Takahashi,T Isobe,H Kaji,J Kamiie,H Kawakami,K Kido,Y Yamauchi,T Shinkawa,M Taoka,N Takahashi,T Isobe,

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Proteomics Reveals N-Linked Glycoprotein Diversity in Caenorhabditis elegans and Suggests an Atypical Translocation Mechanism for Integral Membrane Proteins. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Molecular & cellular proteomics : MCP

VOLUME: 6

Page Numbers: 2100-9

Journal Abbreviation: Mol. Cell Proteomics

ISSN: 1535-9476

DAY: 30

MONTH: 08

YEAR: 2007

Proteomics Reveals N-Linked Glycoprotein Diversity in Caenorhabditis elegans and Suggests an Atypical Translocation Mechanism for Integral Membrane Proteins. Information

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LANGUAGE: eng

NlmUniqueID: 101125647

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Grant and Affiliation Information for Proteomics Reveals N-Linked Glycoprotein Diversity in Caenorhabditis elegans and Suggests an Atypical Translocation Mechanism for Integral Membrane Proteins.

AFFILIATION: Department of Chemistry, Graduate School of Science and Engineering, Tokyo Metropolitan University, Minamiosawa 1-1, Hachioji, Tokyo 192-0397, Japan.

Country: United States

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MEDLINETA: Mol Cell Proteomics

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