http://www.cnr.it/ontology/cnr/individuo/prodotto/ID37856

N-myristoylation determines dual targeting of mammalian NADH-cytochrome b5 reductase to ER and mitochondrial outer membranes by a mechanism of kinetic partitioning. (Articolo in rivista)

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N-myristoylation determines dual targeting of mammalian NADH-cytochrome b5 reductase to ER and mitochondrial outer membranes by a mechanism of kinetic partitioning. (Articolo in rivista) (literal)

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Alternative label

Colombo S; Longhi R; Alcaro S; Ortuso F; Sprocati T; Flora A; Borgese N (2005)
N-myristoylation determines dual targeting of mammalian NADH-cytochrome b5 reductase to ER and mitochondrial outer membranes by a mechanism of kinetic partitioning.
in The Journal of cell biology; Rockefeller University Press, New York (Stati Uniti d'America)
(literal)

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Colombo S; Longhi R; Alcaro S; Ortuso F; Sprocati T; Flora A; Borgese N (literal)

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Colombo S: Istituto di Neuroscienze del CNR e Dipartimento di Farmacologia Medica, Università di Milano; Longhi R: Istituto di Chimica del Riconoscimento Molecolare del CNR, Milano; Alcaro S: Dipartimento di Scienze Farmacobiologiche, Università \"Magna Graecia\" di Catanzaro; Ortuso F: Dipartimento di Scienze Farmacobiologiche, Università \"Magna Graecia\" di Catanzaro; Sprocati T: Istituto di Neuroscienze del CNR e Dipartimento di Farmacologia Medica, Università di Milano; Flora A: Istituto di Neuroscienze del CNR e Dipartimento di Farmacologia Medica, Università di Milano; Borgese N: Istituto di Neuroscienze del CNR e Dipartimento di Farmacologia Medica, Università di Milano;Dipartimento di Scienze Farmacobiologiche, Università \"Magna Graecia\" di Catanzaro (literal)

Titolo

N-myristoylation determines dual targeting of mammalian NADH-cytochrome b5 reductase to ER and mitochondrial outer membranes by a mechanism of kinetic partitioning. (literal)

Abstract

Mammalian NADH-cytochrome b(5) reductase (b5R) is an N-myristoylated protein that is dually targeted to ER and mitochondrial outer membranes. The N-linked myristate is not required for anchorage to membranes because a stretch of hydrophobic amino acids close to the NH2 terminus guarantees a tight interaction of the protein with the phospholipid bilayer. Instead, the fatty acid is required for targeting of b5R to mitochondria because a nonmyristoylated mutant is exclusively localized to the ER. Here, we have investigated the mechanism by which N-linked myristate affects b5R targeting. We find that myristoylation interferes with interaction of the nascent chain with signal recognition particle, so that a portion of the nascent chains escapes from cotranslational integration into the ER and can be post-translationally targeted to the mitochondrial outer membrane. Thus, competition between two cotranslational events, binding of signal recognition particle and modification by N-myristoylation, determines the site of translation and the localization of b5R. (literal)

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