Preferential association of apocytochrome c with negatively charged phospholipids in mixed model membranes

Rietveld, Anton; Berkhout, Theo; Roenhorst, A.; Marsh, Derek; Kruijff, Ben de

doi:10.1016/0005-2736(86)90289-0

Cited by 49 publications

(24 citation statements)

References 30 publications

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“…It has been shown before that apocytochrome c and cytochrome c, in agreement with their basic character, bind specifically to negatively charged lipids [5][6][7][8][9]. Apocytochrome c causes a strong perturbation of the lipid packing.…”

Section: Introductionmentioning

confidence: 77%

Interactions of mitochondrial precursor protein apocytochrome c with phosphatidylserine in model membranes. A monolayer study

Pilon¹,

Jordi²,

Kruijff³

et al. 1987

Biochimica et Biophysica Acta (BBA) - Biomembranes

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(1) The interaction of apocytochrome c with different molecular species of phosphatidyiserine was studied using monolayers at constant surface area or constant surface pressure. The protein inserted readily into dioleoylphosphatidylserine monolayers up to a limiting pressure of 50 raN/m, whereas the interaction decreased with increasing molecular packing of the phosphatidyiserine species, indicating the importance of the hydrophobic core of the lipid layer for the interaction. (2) The high affinity of apocytochrome c for dioleoylphosphatidyiserine is indicated by the low K~ of 0.017/zM. There is little or no interaction with phosphatidylcholines. The importance of charge interactions is underlined by its ionic strength and pH dependency. (3) Experiments using ~4C-labelled apocytochrome c indicate that cholesterol can enhance the protein binding. (4) It was demonstrated that apocytochrome c monomers penetrate the monolayer whereas oligomers can be formed in an adsorbed layer and washed off without changing the surface pressure. Preincubation of apocytochrome c in 3 M guanidine, to obtain the monomeric form, was essential to measure the full effect of interracial interaction. (5) The molecular area of apocytochrome c changed from 1200-1300 .AZ/molecule in the absence of lipid to 700-900 ,A2/molecule after penetration of dioleoyiphosphatidylserine monolayers. (6) Apocytochrome c-dioleoylphosphatidyiserine interactions are only possible when the monolayer is approached from the subphase. It is concluded that the charge interactions are required for binding and penetration of the protein.

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Section: Introductionmentioning

confidence: 77%

Interactions of mitochondrial precursor protein apocytochrome c with phosphatidylserine in model membranes. A monolayer study

Pilon¹,

Jordi²,

Kruijff³

et al. 1987

Biochimica et Biophysica Acta (BBA) - Biomembranes

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“…Experiments with myelin basic protein [31] and with apocytochrome c [35] have been performed with mixtures of negatively charged lipids with zwitterionic phosphatidyl~holine. At relatively low concentrations, the effects of phosphatidyIcholine admixture are those that would be predicted from Eqn 2, on the basis of the relative selectivities (Kr) (cf.…”

Section: Surface Effectsmentioning

confidence: 99%

Lipid‐protein interactions in membranes

Marsh

1990

FEBS Letters

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The interactions of lipids with integral and peripheral proteins can be studied in reconstituted and natural membranes using spin label electron spin resonance (ESR) spectroscopy.The ESR spectra reveal a reduction in mobility of the spin-labelled lipid chains on binding of peripheral proteins to negatively-charged lipid bilayers. A selectivity of interaction has been established for different lipid species. and in certain cases evidence is obtained for a partial penetration of the peripheral proteins into the membrane. The latter may be relevant to the import mechanism of apocytochrome c into mitochondria.Integral proteins induce a more direct motional restriction of the spin-labelled lipid chains, allowing the stoichiometry and specificity of the interaction, and the lipid exchange rate at the protein interface to be determined from the ESR spectra. In this way, a population of very slowly exchanging cardiohpin associated with the mitochondrial ADP-ATP carrier has been identified. The residues involved in the specificity for charged lipids of the myelin proteolipid protein have been localized to the deletion in the DM-20 mutant, and the difference in lipid-protein interactions with the .&sheet and x-helical conformations of the M-13 coat protein, has been characterized.

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“…They have demonstrated in a model-membrane system that apocytochrome c, which is relatively positively charged, can interact strongly with negatively-charged phospholipids in an electrostatic manner [3,5]. Fragments of the polypeptide which have the highest net-positive charge, displayed the highest affinity for the negatively-charged membranes [8].…”

Section: Membrane Insertion Properties Of Apocytochrome E Are Essentimentioning

confidence: 99%

“…The electrostatic interaction of the apocytochrome c polypeptide with the phospholipids is thought to induce structural reorganization of the lipids leading to a reduction of the barrier function, thus the anionic phospholipids appear to be sequestered into a microenvironment surrounding the apocytochrome c molecule [4,6,7]. Circular dichroism (CD) studies revealed that the CD pattern of apocytochrome c in an aqueous solution was featureless [5]. During or following the interaction of apocytochrome c with the lipid bilayer, a-helical structure was expressed within the aminoand carboxy-terminal regions of the polypeptide [4].…”

Section: Membrane Insertion Properties Of Apocytochrome E Are Essentimentioning

confidence: 99%

“…No protease-sensitive components exist on the surface of mitochondria to mediate apocytochrome c binding and import [10]. Instead, apocytochrome c partially inserts into the outer mitochondrial membrane [2][3][4][5]7] where it is recognized and binds with high affinity to specific binding sites [11,12,41,42] in a complex which includes cytochrome c heme lyase (CCHL) [10]. CCHL is the enzyme which is responsible for the covalent attachment of heme to apocytochrome c and it displays a dependence on NADH and flavin nucleotides [10].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Apocytochrome c: an exceptional mitochondrial precursor protein using an exceptional import pathway

Stuart

Neupert

1990

Biochimie

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Preferential association of apocytochrome c with negatively charged phospholipids in mixed model membranes

Cited by 49 publications

References 30 publications

Interactions of mitochondrial precursor protein apocytochrome c with phosphatidylserine in model membranes. A monolayer study

Interactions of mitochondrial precursor protein apocytochrome c with phosphatidylserine in model membranes. A monolayer study

Lipid‐protein interactions in membranes

Apocytochrome c: an exceptional mitochondrial precursor protein using an exceptional import pathway

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