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N-glycosylation efficiency is determined by the distance to the C-terminus and the amino acid preceding an Asn-Ser-Thr sequon

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N-glycosylation efficiency is determined by the distance to the C-terminus and the amino acid preceding an Asn-Ser-Thr sequon

dc.contributor.author	Bañó Polo, Manuel
dc.contributor.author	Baldin, Francesca
dc.contributor.author	Tamborero Capilla, Silvia
dc.contributor.author	Martí Renom, Marc A.
dc.contributor.author	Mingarro Muñoz, Ismael
dc.date.accessioned	2016-09-21T13:46:44Z
dc.date.available	2016-09-21T13:46:44Z
dc.date.issued	2011
dc.identifier.citation	Bañó Polo, Manuel Baldin, Francesca Tamborero Capilla, Silvia Martí Renom, Marc A. Mingarro Muñoz, Ismael 2011 N-glycosylation efficiency is determined by the distance to the C-terminus and the amino acid preceding an Asn-Ser-Thr sequon Protein Science 20 1 179 186
dc.identifier.uri	http://hdl.handle.net/10550/55075
dc.description.abstract	N-glycosylation is the most common and versatile protein modification. In eukaryotic cells, this modification is catalyzed cotranslationally by the enzyme oligosaccharyltransferase, which targets the β-amide of the asparagine in an Asn-Xaa-Ser/Thr consensus sequon (where Xaa is any amino acid but proline) in nascent proteins as they enter the endoplasmic reticulum. Because modification of the glycosylation acceptor site on membrane proteins occurs in a compartment-specific manner, the presence of glycosylation is used to indicate membrane protein topology. Moreover, glycosylation sites can be added to gain topological information. In this study, we explored the determinants of N-glycosylation with the in vitro transcription/translation of a truncated model protein in the presence of microsomes and surveyed 25,488 glycoproteins, of which 2,533 glycosylation sites had been experimentally validated. We found that glycosylation efficiency was dependent on both the distance to the C-terminus and the nature of the amino acid that preceded the consensus sequon. These findings establish a broadly applicable method for membrane protein tagging in topological studies.
dc.language.iso	eng
dc.relation.ispartof	Protein Science, 2011, vol. 20, num. 1, p. 179-186
dc.subject	Proteïnes de membrana
dc.subject	Reaccions químiques
dc.subject	Bioquímica
dc.title	N-glycosylation efficiency is determined by the distance to the C-terminus and the amino acid preceding an Asn-Ser-Thr sequon
dc.type	journal article	es_ES
dc.date.updated	2016-09-21T13:46:44Z
dc.identifier.doi	10.1002/pro.551
dc.identifier.idgrec	061079
dc.rights.accessRights	open access	es_ES