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N-myristoylation determines dual targeting of mammalian NADH-cytochrome b(5) reductase to ER and mitochondrial outer membranes by a mechanism of kinetic partitioning.
- Source :
-
Journal of Cell Biology . 2/28/2005, Vol. 168 Issue 5, p735-745. 11p. - Publication Year :
- 2005
-
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. [ABSTRACT FROM AUTHOR]
- Subjects :
- *CYTOCHROMES
*CYTOCHROME b
*HEMOPROTEINS
*AMINO acids
*FATTY acids
*MITOCHONDRIA
Subjects
Details
- Language :
- English
- ISSN :
- 00219525
- Volume :
- 168
- Issue :
- 5
- Database :
- Academic Search Index
- Journal :
- Journal of Cell Biology
- Publication Type :
- Academic Journal
- Accession number :
- 16375484
- Full Text :
- https://doi.org/10.1083/jcb.200407082