NAGIOS: RODERIC FUNCIONANDO

Different conformations of nascent polypeptides during translocation across the ER membrane

Repositori DSpace/Manakin

IMPORTANT: Aquest repositori està en una versió antiga des del 3/12/2023. La nova instal.lació está en https://roderic.uv.es/

Different conformations of nascent polypeptides during translocation across the ER membrane

dc.contributor.author	Mingarro Muñoz, Ismael
dc.contributor.author	Nilsson, IngMarie
dc.contributor.author	Whitley, Paul
dc.contributor.author	Heijne, Gunnar von
dc.date.accessioned	2016-09-06T18:00:02Z
dc.date.available	2016-09-06T18:00:02Z
dc.date.issued	2000
dc.identifier.citation	Mingarro Muñoz, Ismael Nilsson, IngMarie Whitley, Paul Heijne, Gunnar von 2000 Different conformations of nascent polypeptides during translocation across the ER membrane Bmc Cell Biology 1 3 1 8
dc.identifier.uri	http://hdl.handle.net/10550/54928
dc.description.abstract	BACKGROUND: In eukaryotic cells, proteins are translocated across the ER membrane through a continuous ribosome-translocon channel. It is unclear to what extent proteins can fold already within the ribosome-translocon channel, and previous studies suggest that only a limited degree of folding (such as the formation of isolated alpha-helices) may be possible within the ribosome. RESULTS: We have previously shown that the conformation of nascent polypeptide chains in transit through the ribosome-translocon complex can be probed by measuring the number of residues required to span the distance between the ribosomal P-site and the lumenally disposed active site of the oligosaccharyl transferase enzyme (J. Biol. Chem 271: 6241-6244). Using this approach, we now show that model segments composed of residues with strong helix-forming properties in water (Ala, Leu) have a more compact conformation in the ribosome-translocon channel than model segments composed of residues with weak helix-forming potential (Val, Pro). CONCLUSIONS: The main conclusions from the work reported here are (i) that the propensity to form an extended or more compact (possibly alpha-helical) conformation in the ribosome-translocon channel does not depend on whether or not the model segment has stop-transfer function, but rather seems to reflect the helical propensities of the amino acids as measured in an aqueous environment, and (ii) that stop-transfer sequences may adopt a helical structure and integrate into the ER membrane at different times relative to the time of glycan addition to nearby upstream glycosylation acceptor sites.
dc.language.iso	eng
dc.relation.ispartof	Bmc Cell Biology, 2000, vol. 1, num. 3, p. 1-8
dc.subject	Aminoàcids
dc.subject	Pèptids
dc.subject	Cèl·lules eucariotes
dc.title	Different conformations of nascent polypeptides during translocation across the ER membrane
dc.type	journal article	es_ES
dc.date.updated	2016-09-06T18:00:02Z
dc.identifier.doi	10.1186/1471-2121-1-3
dc.identifier.idgrec	003979
dc.rights.accessRights	open access	es_ES