A molecular model for the specific cardiolipin-presequence interactions

Leenhouts, Johanna M.; Török, Zsolt; Chupin, Vladimir; Kruijff, Ben de

doi:10.1042/bst0230968

Cited by 8 publications

(7 citation statements)

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“…The structure of p25 as depicted in Fig. 6B is consistent with many of the observed specific CL p25 interactions (summarized in [42]). Among these observations, results indicated an orientation of the Nterminal part of the helix inserted into the lipid bilayer with its helix axis perpendicular to the membrane surface.…”

Section: Moreover the Medium Range Hu(i)-hfl(i+3) Ha(i)-nh(i + 3)supporting

confidence: 82%

“…Therefore, the consequences of the helix-turn-helix motif for the mitochondrial protein import process could be that the presequence inserts specifically into the CL-containing inner mitochondrial membrane, in such a way that it leads to a correct orientation for processing. Alternative implications of the CL-modulated conformation of p25 for the mitochondrial protein import pathway are suggested elsewhere [42].…”

Section: Moreover the Medium Range Hu(i)-hfl(i+3) Ha(i)-nh(i + 3)mentioning

confidence: 99%

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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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Section: Moreover the Medium Range Hu(i)-hfl(i+3) Ha(i)-nh(i + 3)supporting

confidence: 82%

Section: Moreover the Medium Range Hu(i)-hfl(i+3) Ha(i)-nh(i + 3)mentioning

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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“…We have previously reported that the SS mitochondrial subfraction contains a greater cardiolipin content than the IMF subfraction (19). Interestingly, it is now established that mitochondrial phospholipids, particularly cardiolipin, play an early role in the binding of precursor proteins destined for the mitochondrion (21)(22)(23)(24). If cardiolipin is uniquely important for import into mammalian mitochondria, the SS subfraction should demonstrate a greater rate of protein import than the IMF mitochondria.…”

mentioning

confidence: 99%

Protein Import into Subsarcolemmal and Intermyofibrillar Skeletal Muscle Mitochondria

Takahashi

Hood

1996

Journal of Biological Chemistry

114

104

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To date, no studies have described the import of proteins in mitochondria obtained from skeletal muscle. In this tissue, mitochondria consist of the functionally and biochemically distinct intermyofibrillar (IMF) and subsarcolemmal (SS) subfractions, which are localized in specialized cellular compartments. This mitochondrial heterogeneity in muscle could be due, in part, to differential rates of protein import. To evaluate this possibility, the import of precursor malate dehydrogenase and ornithine carbamyltransferase proteins was investigated in isolated IMF and SS mitochondria in vitro. Import of these was 3-4-fold greater in IMF compared with SS mitochondria as a function of time. This could account for the higher malate dehydrogenase enzyme activity in IMF mitochondria. Divergent import rates in IMF and SS mitochondria likely result from a differential reliance on various components of the import pathway. SS mitochondria possess a greater content of the molecular chaperones hsp60 and Grp75, yet import is lower than in IMF mitochondria. On the other hand, adriamycin inhibition studies illustrated a greater reliance on acidic phospholipids (i.e. cardiolipin) for the import process in SS mitochondria. Matrix ATP levels were 3-fold higher in IMF mitochondria, but experiments in which ATP depletion was performed with atractyloside and oligomycin illustrated a dissociation between import rates and levels of ATP. In contrast, a close relationship was found between the rate of ATP production (i.e. mitochondrial respiration) and protein import. When respiratory rates in IMF and SS mitochondria were equalized, import rates in both subfractions were similar. These data indicate that 1) import rates are more closely related to the rate of ATP production than the steady state ATP level, 2) import into IMF and SS mitochondrial subfractions is regulated differently, and 3) mitochondrial heterogeneity within a cell type can be due to differences in the rates of protein import, suggesting that this step is a potentially regulatable event in determining the final mitochondrial phenotype.

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“…A molecular model of the topology taining membranes, compared to PG-containing membranes, of peptide in the two different systems has been described by This was concluded from a number of experiments. Firstly, Leenhouts et al [30]. the monolayer experiments demonstrate that only in the case…”

Section: Discussionmentioning

confidence: 99%

“…p25 and salts. Next, the monolayer with the protected peptide Z was collected, lyophilized and dissolved in a small volume of E,E ~ water, and the sample was analyzed by N-terminal peptide UJ 30 sequence analysis. The result of the HPLC analysis of the first tr cycle is shown in Fig.…”

mentioning

confidence: 99%

The N‐terminal half of a mitochondrial presequence peptide inserts into cardiolipin‐containing membranes Consequences for the action of a transmembrane potential

et al. 1996

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branes with the help of mitochondrial import machineries (for Abstract The orientation of a mitochondrial presequence peptide, associated with anionic lipid-containing model memreviews, see [1,2]). Translocation of the presequence across the branes, was investigated. The peptide inserts with its N-terminal inner mitochondrial membrane requires a membrane potential a-helical part into cardiolipin (CL) monolayers so that the N-(A~) across that membrane [3,4]. terminal 14 residues are protected from proteinase K. In Although the amount of information about the import prophosphatidylglycerol (PG) monolayers the inserted peptide was cess and components involved is still growing, the molecular fully accessible to the protease. A consequence of the different mechanism of the protein translocation process is largely unorientations of the peptide was that membrane potentialknown. This applies in particular to the molecular interactions dependent protection from trypsin was much faster for the the presequence is involved in. The presequence is assumed to peptide bound to PG-eontaining vesicles compared to CLinteract with different proteinaceous components of the imcontaining membranes, suggesting that in the mitochondrial protein import process other components of the import apparatus port apparatus, as well as with membrane lipids (cf. [5,6]). Of are involved in the efficient potential-driven translocation of special interest is cardiolipin (CL), a phospholipid with a unpresequences across the inner mitochondrial membrane, ique chemical structure, which in the eukaryotic cell is only synthesized [7] and found in mitochondria [8,9]. Several ob-

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A molecular model for the specific cardiolipin-presequence interactions

Cited by 8 publications

References 10 publications

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

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

Protein Import into Subsarcolemmal and Intermyofibrillar Skeletal Muscle Mitochondria

The N‐terminal half of a mitochondrial presequence peptide inserts into cardiolipin‐containing membranes Consequences for the action of a transmembrane potential

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A molecular model for the specific cardiolipin-presequence interactions

Cited by 8 publications

References 10 publications

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

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

Protein Import into Subsarcolemmal and Intermyofibrillar Skeletal Muscle Mitochondria

The N‐terminal half of a mitochondrial presequence peptide inserts into cardiolipin‐containing membranes Consequences for the action of a transmembrane potential

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

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