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Protein translocation across mitochondrial membranes

Article Abstract:

The mitochondrion has an indispensable role in protein secretion and translocation across biological membranes. Research has identified the presence of mitrochondrial components involved in these processes. These include cytosolic heat shock proteins that stabilize protein precursors, mitochondrial outer membrane proteins 19 and 72 that recognize and bind protein to their carriers, processing enhancing proteins and mitochondrial processing peptidases that cleave precursor amino terminal sequences, inner membrane protease 1 and cytochrome c heme lyase.

Author: Neupert, Walter, Wienhues, Ulla
Publisher: John Wiley & Sons, Inc.
Publication Name: BioEssays
Subject: Biological sciences
ISSN: 0265-9247
Year: 1992

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Mitochondrial protein import: reversible binding of the presequence at the trans side of the outer membrane drives partial translocation and unfolding

Article Abstract:

Analysis of the translocation of matrix-targeted, cleavable preproteins across the mitochondrial outer membrane using purified outer membrane vesicles reveals that the protein import machinery generates a translocation channel that inhibits lateral protein aggregation and allows reversible preprotein sliding in the membrane. Reversible binding of the protein to the trans site accelerates partial unfolding and translocation of the protein. The energetic system of the inner membrane is essential for the completion of the protein translocation.

Author: Neupert, Walter, Mayer, Andreas, Lill, Roland
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
Analysis, Protein binding

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Sec18p(NSF)-driven release of Sec17p(alpha-SNAP) can precede docking and fusion of yeast vacuoles

Article Abstract:

Studies into the cell division of Saccharomyces cerevisiae have shown that membrane trafficking process which manage organelle distribution in dividing cells rely on the action of the N-ethylmaleimide(NEM)-sensitive fusion (NSF) protein and soluble NSF attachment proteins (SNAP). In vacuole fusion, the alpha-SNAP homolog Sec17p and the NSF homolog Sec18p interact to support vesicular transport. Subsequent dissociation of Sec17p from the vesicle bound complex drives the fusion of the lipid bilayer.

Author: Mayer, Andreas, Wickner, William, Haas, Albert
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
Saccharomyces, Cell division, Developmental cytology, Cell organelles, Organelles

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Subjects list: Research, Biological transport, Mitochondria, Proteins
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