The signal anchor sequence of mitochondrial Mas70p contains an oligomerization domain.
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چکیده
منابع مشابه
A signal-anchor sequence selective for the mitochondrial outer membrane
pOMD29 is a hybrid protein containing the NH2-terminal topogenic sequence of a bitopic, integral protein of the outer mitochondrial membrane in yeast, OMM70, fused to dihydrofolate reductase. The topogenic sequence consists of two structural domains: an NH2-terminal basic region (amino acids 1-10) and an apolar region which is the predicted transmembrane segment (amino acids 11-29). The transme...
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Mas70p is an integral membrane protein in Saccharomyces cerevisiae that is targeted and inserted into the mitochondrial outer membrane in an N,,-C, orientation by its --terminal 29-amino acid signal anchor sequence. Recently, we demonstrated that the signal anchor was capable of mediating homo-oligomerization of a fusion protein, pOMD29, in the outer membrane in vitro (Millar, D. G., and Shore,...
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Tail-anchored proteins are a group of membrane proteins oriented with their amino terminus in the cytoplasm and their carboxy terminus embedded in intracellular membranes. This group includes the apoptosis-mediating proteins of the Bcl-2 family as well as the vesicle targeting proteins of the SNARE group, among others. A stretch of hydrophobic amino acids at the extreme carboxy terminus of thes...
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Type I signal-anchor sequences mediate translocation of the N-terminal domain (N-domain) across the endoplasmic reticulum (ER) membrane. To examine the translocation in detail, dihydrofolate reductase (DHFR) was fused to the N-terminus of synaptotagmin II as a long N-domain. Translocation was arrested by the DHFR ligand methotrexate, which stabilizes the folding of the DHFR domain, and resumed ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1993
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)46635-x