http://www.cnr.it/ontology/cnr/individuo/prodotto/ID169612
Translocation of the C-terminus of a tail-anchored protein across the endoplasmic reticulum membrane in yeast mutants defective in signal peptide-driven translocation (Articolo in rivista)
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- Label
- Translocation of the C-terminus of a tail-anchored protein across the endoplasmic reticulum membrane in yeast mutants defective in signal peptide-driven translocation (Articolo in rivista) (literal)
- Anno
- 2003-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1074/jbc.M210253200 (literal)
- Alternative label
Yabal M., Brambillasca S., Soffientini P., Pedrazzini E., Borgese N., Makarow M. (2003)
Translocation of the C-terminus of a tail-anchored protein across the endoplasmic reticulum membrane in yeast mutants defective in signal peptide-driven translocation
in Journal of biological chemistry (Online)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Yabal M., Brambillasca S., Soffientini P., Pedrazzini E., Borgese N., Makarow M. (literal)
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- http://www.jbc.org/content/278/5/3489.full (literal)
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- Rivista
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- IF 6,7 - Citazioni: 4 (literal)
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- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- YM, MM: Program of Cellular Biotechnology, Institute of Biotechnology, University of Helsinki, Helsinki, Finland
BS, PS, PE, BN: Consiglio Nazionale delle Ricerche Institute of Neuroscience, Milano, Italy
BN: Faculty of Pharmacy, University of Catanzaro \"Magna Graecia,\" (CZ), Italy (literal)
- Titolo
- Translocation of the C-terminus of a tail-anchored protein across the endoplasmic reticulum membrane in yeast mutants defective in signal peptide-driven translocation (literal)
- Abstract
- C-tail-anchored proteins are defined by an N-terminal cytosolic domain followed by a transmembrane anchor close to the C terminus. Their extreme C-terminal polar residues are translocated across membranes by poorly understood post-translational mechanism(s). Here we have used the yeast system to study translocation of the C terminus of a tagged form of mammalian cytochrome b(5), carrying an N-glycosylation site in its C-terminal domain (b(5)-Nglyc). Utilization of this site was adopted as a rigorous criterion for translocation across the ER membrane of yeast wild-type and mutant cells. The C terminus of b(5)-Nglyc was rapidly glycosylated in mutants where Sec61p was defective and incapable of translocating carboxypeptidase Y, a well known substrate for post-translational translocation. Likewise, inactivation of several other components of the translocon machinery had no effect on b(5)-Nglyc translocation. The kinetics of translocation were faster for b(5)-Nglyc than for a signal peptide-containing reporter. Depletion of the cellular ATP pool to a level that retarded Sec61p-dependent post-translational translocation still allowed translocation of b(5)-Nglyc. Similarly, only low ATP concentrations (below 1 microm), in addition to cytosolic protein(s), were required for in vitro translocation of b(5)-Nglyc into mammalian microsomes. Thus, translocation of tail-anchored b(5)-Nglyc proceeds by a mechanism different from that of signal peptide-driven post-translational translocation. (literal)
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