Incorporation in lipid bilayers of a large conductance cationic channel from mitochondrial membranes.

Thieffry, M; Chich, Jean-François; Goldschmidt, D.; Henry, Jean‐Pierre

doi:10.1002/j.1460-2075.1988.tb02962.x

Cited by 64 publications

(45 citation statements)

References 40 publications

(28 reference statements)

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“…Electrophysiological Recordings-Proteoliposomes were prepared, and bilayers were formed at the tip of microelectrodes by the tip-dip technique as described by Thieffry et al (6). The channel content of a given fraction was quantified by the frequency of the characteristic electrical activity (7) and defined as the total number of channels found divided by the total number of seals (i.e.…”

Section: Methodsmentioning

confidence: 99%

“…The solubilized fraction, which contained most of the radioactivity, was immunoprecipitated overnight at 4°C in the presence of either anti-ISP 42 antiserum or a nonimmune serum, immobilized on protein A-Sepharose 4B. The beads were washed with increasing concentrations of salt (up to 300 mM NaCl) and/or 1% Nonidet P-40 in order to prevent immu- (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13) and ISP 42, a component of the outer membrane import machinery, it was interesting to test the ability of dynorphin B(1-13) to act as a mitochondrial presequence. We thus constructed a chimeric protein (see Table I) containing the sequence of dynorphin B(1-13) fused to the N terminus of cytosolic mouse DHFR using a PCR-directed gene fusion technique (13).…”

Section: Cross-linking Of Dynorphin B(1-13) With Yeast Mitochondrial mentioning

confidence: 99%

“…Trypsin-sensitive Components of the Outer Membrane Discriminate between Dynorphin B (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13) and the Synthetic Mitochondrial Presequence pCytOX IV (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)Y-A possible explanation for the difference observed between the import of natural presequences and that of dynorphin B(1-13) is the presence of receptors on the outer membrane surface (11). These receptors would discriminate between the two types of peptides that would then be transported along the same pathway.…”

Section: Cross-linking Of Dynorphin B(1-13) With Yeast Mitochondrial mentioning

confidence: 99%

“…Following this recognition step, protein translocation appears to occur through an unique pore, the general insertion pore (GIP) 1 (5). The mitochondrial outer membrane contains a voltage-dependent cationic channel of large conductance, the peptide-sensitive channel (PSC) (6,7). The PSC is blocked by small basic peptides derived from mitochondrial presequences (e.g.…”

mentioning

confidence: 99%

“…The PSC is also blocked by basic peptides unrelated to mitochondrial physiology, such as dynorphin B (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13). However, dynorphin B(1-13) failed to inhibit the import of a chimeric protein, cytochrome b 2 -dihydrofolate reductase (DHFR), into the matrix of yeast mitochondria (11).…”

mentioning

confidence: 99%

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Relationship between the Peptide-sensitive Channel and the Mitochondrial Outer Membrane Protein Translocation Machinery

Juin

Thieffry

Henry

et al. 1997

Journal of Biological Chemistry

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The peptide-sensitive channel (PSC), a cationic channel of the mitochondrial outer membrane, is blocked by synthetic mitochondrial presequences and by nonmitochondrial basic peptides such as dynorphin B(1-13). Both types of peptides are imported into mitochondria. However, the import of dynorphin B(1-13) had to be further characterized since its properties differed from those of the general import pathway used by mitochondrial peptides. Cross-linking experiments with iodinated dynorphin B(1-13) led to the labeling of TOM 40/ ISP 42, a component of the protein import machinery of the outer membrane. Accordingly, dynorphin B(1-13) could also be used as a presequence to direct the import of a cytosolic protein into the mitochondria. Pretreatment of intact mitochondria by trypsin removed components capable of discriminating between true mitochondrial presequences and other basic peptides active on the PSC. After proteolysis, both types of peptides appeared to cross the outer membrane through the same pathway. Involvement of the PSC in the translocation complex was shown by immunoprecipitation of the PSC activity by anti-ISP 42 antibodies. Taken together, the present data reinforce the hypothesis that the PSC is the pore responsible for the translocation of protein through the outer membrane.

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Section: Methodsmentioning

confidence: 99%

Section: Cross-linking Of Dynorphin B(1-13) With Yeast Mitochondrial mentioning

confidence: 99%

Section: Cross-linking Of Dynorphin B(1-13) With Yeast Mitochondrial mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Relationship between the Peptide-sensitive Channel and the Mitochondrial Outer Membrane Protein Translocation Machinery

Juin

Thieffry

Henry

et al. 1997

Journal of Biological Chemistry

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Mitochondrial Outer Membrane Channels: Emerging Diversity in Transport Processes

Becker

Wagner

2018

BioEssays

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Mitochondrial function and biogenesis depend on the transport of a large variety of proteins, ions, and metabolites across the two surrounding membranes. While several specific transporters are present in the inner membrane, transport processes across the outer membrane are less understood. Recent studies reveal that the number of outer membrane channels and their transport mechanisms are more diverse than originally thought. Four protein-conducting channels promote transport of distinct sets of precursor proteins across and into the outer membrane. The voltage-dependent anion channel (VDAC) forms the major channel for small hydrophilic molecules. In addition, three channels with yet unknown substrate specificity exist in the outer membrane. In this review, we outline the emerging functional diversity, selectivity, and regulation of mitochondrial outer membrane channels. The presence of several channel-forming proteins challenges the traditional view that the outer membrane forms an unspecific size-exclusion filter for the flux of small hydrophilic molecules.

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The control of mitochondrial respiration in yeast: A possible role of the outer mitochondrial membrane

Ahmadzadeh

Horng

Colombini

1996

Cell Biochemistry & Function

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Mitochondrial respiration in yeast (S. cerevisiae) is regulated by the level of glucose in the medium. Glucose is known to inhibit respiration by repressing key enzymes in the respiratory chain. We present evidence that the early events in this inhibition include the closure of VDAC channels, the primary pathway for metabolite flow across the outer membrane. Aluminum hydroxide is known to inhibit the closure of VDAC. Addition of aluminum acetylacetonate to yeast cells, which should elevate the aluminum hydroxide concentrations in the cytoplasm, caused the inhibition of cell respiration by glucose to be delayed for up to 100 min. No significant effect of aluminum was observed in cells grown on glycerol. Yeast cells lacking the VDAC gene were also unresponsive to the addition of aluminum salt in the presence of glucose. Therefore, the closure of VDAC channels may be an early step in the inhibition of the respiration of yeast by glucose.

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Incorporation in lipid bilayers of a large conductance cationic channel from mitochondrial membranes.

Cited by 64 publications

References 40 publications

Relationship between the Peptide-sensitive Channel and the Mitochondrial Outer Membrane Protein Translocation Machinery

Relationship between the Peptide-sensitive Channel and the Mitochondrial Outer Membrane Protein Translocation Machinery

Mitochondrial Outer Membrane Channels: Emerging Diversity in Transport Processes

The control of mitochondrial respiration in yeast: A possible role of the outer mitochondrial membrane

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