Mitochondrial protein import: Specific recognition and membrane translocation of preproteins

Kiebler, Michael; Becker, Kurt; Pfanner, Nikolaus; Neupert, Walter

doi:10.1007/bf00211091

Cited by 86 publications

(57 citation statements)

References 154 publications

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“…Antibodies-The existence of a common import pathway for mitochondrial and nonmitochondrial peptides active on the PSC justified more investment in order to determine the precise relationship between PSC and GIP, of which ISP 42 is the main component (19). For this purpose, we tested the ability of anti-ISP 42 antibodies to deplete the PSC activity.…”

Section: Mitochondria Can Be Depleted Of Psc Activity By Immunoprecipmentioning

confidence: 99%

“…Protease-sensitive receptors specifically bind mitochondrial presequences prior to their translocation into the mitochondria through a protease-resistant site that includes TOM40/ISP 42 (19). The binding and recognition of mitochondrial proteins appeared to require several different receptors with complex recognition patterns (5,29).…”

Section: Mitochondria Can Be Depleted Of Psc Activity By Immunoprecipmentioning

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: Mitochondria Can Be Depleted Of Psc Activity By Immunoprecipmentioning

confidence: 99%

Section: Mitochondria Can Be Depleted Of Psc Activity By Immunoprecipmentioning

confidence: 99%

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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“…Nuclearly encoded proteins which are destined for the mitohondria, are synthesized in the cytosol as precursors carrying ~n amino terminal extension, the presequence (for a review on mitochondrial protein import, see [1]). These presequences contain the information to target the precursors into the mitochondria and are proteolytically removed once they have reached he mitochondrial matrix.…”

Section: Introductionmentioning

confidence: 99%

Cardiolipin modulates the secondary structure of the presequence peptide of cytochrome oxidase subunit IV: a 2D ¹H‐NMR study

Chupin¹,

Leenhouts²,

Kroon³

et al. 1995

FEBS Letters

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The secondary structure of the presequence of cytochrome oxidase subunit IV (p25) was studied by circular dichroism and 2D nuclear magnetic resonance in micelles of dodecylphosphoeholine (DPC) and mixed micelles of DPC and mitocbondrial cardiolipin (CL). In both systems, a-helix formation ~as observed. The a-helix stretches from the N-to the C-terminus with a break at the proline residue at position 13. Upon introduction of CL in the DPC mieellar system, an increased stability of the helix was observed around proline ~3 and in the (i-terminal hall This observation, together with reported results on specific interactions between CL and p25, led to the proposal of a two-state equilibrium of the a-helical conformation of p25, modulated by CL.

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“…Increasing experimental evidence on the nature of these signals has been obtained [ l , 21. They can be present as a cleavable N-terminal signal sequence or within the mature parts of precursor proteins (reviewed in [3]). The most abundant and best studied are the N-terminal presequences.…”

mentioning

confidence: 99%

Computational Method to Predict Mitochondrially Imported Proteins and their Targeting Sequences

Claros

Vincens

1996

European Journal of Biochemistry

1,533

1,201

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Most of the proteins that are used in mitochondria are imported through the double membrane of the organelle. The information that guides the protein to mitochondria is contained in its sequence and structure, although no direct evidence can be obtained. In this article, discriminant analysis has been performed with 47 parameters and a large set of mitochondrial proteins extracted from the SwissProt database. A computational method that facilitates the analysis and objective prediction of mitochondrially imported proteins has been developed. If only the amino acid sequence is considered, 75-97% of the mitochondrial proteins studied have been predicted to be imported into mitochondria. Moreover, the existence of mitochondrial-targeting sequences is predicted in 76 -94 % of the analyzed mitochondrial precursor proteins. As a practical application, the number of unknown yeast open reading frames that might be mitochondrial proteins has been predicted, which revealed that many of them are clustered.

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Mitochondrial protein import: Specific recognition and membrane translocation of preproteins

Cited by 86 publications

References 154 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

Cardiolipin modulates the secondary structure of the presequence peptide of cytochrome oxidase subunit IV: a 2D ¹H‐NMR study

Computational Method to Predict Mitochondrially Imported Proteins and their Targeting Sequences

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Mitochondrial protein import: Specific recognition and membrane translocation of preproteins

Cited by 86 publications

References 154 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

Cardiolipin modulates the secondary structure of the presequence peptide of cytochrome oxidase subunit IV: a 2D 1H‐NMR study

Computational Method to Predict Mitochondrially Imported Proteins and their Targeting Sequences

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Cardiolipin modulates the secondary structure of the presequence peptide of cytochrome oxidase subunit IV: a 2D ¹H‐NMR study