The importance of the amino terminus of the mitochondrial precursor protein apocytochrome c for translocation across model membranes

Jordi, W.; Zhou, Li-Gen; Pilon, Marinus; Demel, R.A.; Kruijff, Ben de

doi:10.1016/s0021-9258(18)94175-x

Cited by 63 publications

(69 citation statements)

References 55 publications

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“…Indeed, an additional simulation performed with CW, under the same thermodynamic conditions and the same protocol (described in section IIA), with another CHARMM force field 38 represented in Figure 5 by a green curve, where the H18 and M80 atoms are explicitly bonded to the Fe atom, is more stable than CW (and even CW-M1). This finding is in agreement the fact that these two bonds play a crucial role in the protein secondary structure stability as suggested by [68][69][70] and also with the fact that this force field better reproduces the heme moiety than the CHARMM default force field. We have also computed the structural alignment of the protein in CW-M1 and CW-M2 with the PyMOL alignment utility 71 .…”

Section: B Structure and Stability Of Proteins In Aot Reverse Micellesupporting

confidence: 91%

Molecular dynamics simulations of cytochrome c unfolding in AOT reverse micelles: The first steps

2010

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2This paper explores the reduced form of horse cytochrome c confined in reverse micelles (RM) of sodium bis-(2-ethylhexyl) sulfosuccinate (AOT) in isooctane by molecular dynamics simulation. RMs of two sizes were constructed at a water content of W o = [H 2 O]/[AOT] = 5.5 and 9.1. Our results show that the protein secondary structure and the heme conformation both depend on micellar hydration. At low hydration, the protein structure and the heme moiety remain stable, whereas at high water content the protein becomes unstable and starts to unfold. At W o = 9.1, according to the X-ray structure, conformational changes are mainly localized on protein loops and around the heme moiety, where we observe a partial opening of the heme crevice. These findings suggest that within our time window (10 ns), the structural changes observed at the heme level are the first steps of the protein denaturation process, previously described experimentally in micellar solutions. In addition, a specific binding of AOT molecules to a few lysine residues of the protein was found only in the small-sized RM.3

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Section: B Structure and Stability Of Proteins In Aot Reverse Micellesupporting

confidence: 91%

Molecular dynamics simulations of cytochrome c unfolding in AOT reverse micelles: The first steps

2010

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“…Hovius et al (1990)]. Apocytochrome c is found to be positioned deep in the lipid bilayers when these contain only phosphatidylglycerols, hence illustrating the membrane-insertion propensity of the Nterminus of apocytochrome c, as was reported previously (Jordi et al, 1989a(Jordi et al, ,b, 1990. Additionally, a considerable perturbation of the lipid packing and of the lipid mobility occurs upon binding of apocytochrome c to negatively charged lipid bilayers (Gorrissen et al, 1986;Muga et al, 1991a).…”

Section: Discussionsupporting

confidence: 67%

“…Biochemical and biophysical studies on the interactions of apocytochrome c with model membranes have revealed that the basic precursor protein binds strongly to negatively charged phospholipids (Rietveld et al, 1983), upon which a considerable perturbation of the lipid packing and lipid mobility takes place (Gorrissen et al, 1986;Jordi et al, 1990;Muga et al, 1991a). Furthermore, it has been shown that apocytochrome c, but not cytochrome c, can translocate at least partially across anionic phospholipid bilayers (Dumont & Richards, 1984;Rietveld et al, 1986;Jordi et al, 1989a). Taken together, these studies provide strong indications that lipid-protein interactions can play an important role in the import of apocytochrome c into mitochondria.Recently, attempts have been made to elucidate at least part of the molecular import mechanism.…”

mentioning

confidence: 99%

“…In parallel, native yeast cytochrome c, which is thought not to penetrate the membrane as deeply as does apocytochrome c (Gorrissen et al, 1986;Jordi et al, 1989a), was also investigated. For these studies, yeast cytochrome c was spinlabeled at the single free cysteine residue at position 102 in its C-terminal part, a modification that has been shown not to change the properties of native yeast cytochrome c (Drott etal., 1970;Zuniga &Nall, 1983).…”

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confidence: 99%

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Membrane Location of Spin-labeled Apocytochrome c and Cytochrome c Determined by Paramagnetic Relaxation Agents

Snel¹,

Dekruijff²,

Marsh³

1994

Biochemistry

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The mitochondrial precursor protein horse heart apocytochrome c was spin-labeled on the cysteine residue at position 14 or 17 in the N-terminal region, and the mature protein yeast cytochrome c was similarly labeled on the single free cysteine residue at position 102 at the C-terminal. The proteins were bound to negatively charged phospholipid bilayers, and the accessibility of the spin-labeled cysteine residues to lipid-soluble molecular oxygen and to the lipid-impermeant chromium oxalate anion was determined from the saturation properties of the ESR spectra. Binding of the protein was found to have a considerable effect on the local oxygen concentrations within the lipid bilayer. The accessibilities of the spin-labeled proteins relative to those obtained for phospholipids spin-labeled either in the headgroup or at positions in the sn-2 acyl chain, in the presence of unlabeled protein, identify the position of the spin-labeled cysteine residues in the phospholipid bilayer. The spin label on apocytochrome c bound to phosphatidylglycerol bilayers lies between the 5- and 14-C positions of the lipid acyl chain. Admixture of > or = 75 mol % phosphatidylcholine induces an additional surface-associated apocytochrome c population. The spin label on native and heat-denatured cytochrome c is located at the membrane surface. These different extents of membrane penetration correlate also with the reduction in local oxygen concentration experienced by spin-labeled phospholipids on binding of apo- and holocytochrome c. The possible biological implications of the data are discussed.

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“…Because of the positively charged amphiphilic property, signal sequences are well-suited for interaction with mitochondrial membranes. Studies with a variety of signal sequences showed that they are highly surface-active and they can bind to lipid bilayers containing negatively charged lipids (Tamm, 1986;Roise et al, 1986;Skerjac et al, 1987;Jordi et al, 1989;Frey & Tamm, 1990;Hoyt et al, 1991;de Kroon etal., 1991;Roise, 1992;Swansom & Roise, 1992;Zardeneta & Horwitz, 1992).…”

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confidence: 99%

Evaluation of electrostatic and hydrophobic effects on the interaction of mitochondrial signal sequences with phospholipid bilayers

Wang

Weiner²

1994

Biochemistry

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The information that directs a nuclear-coded protein to be imported into mitochondria resides in an N-terminal extension, called a signal sequence. The primary sequences of all known ones differ. The only common feature is their ability to theoretically form an amphiphilic, positively charged, alpha-helix. We previously showed that a short stable helical segment was required for a peptide to be functional in import [Wang, Y., & Weiner, H. (1993) J. Biol. Chem. 268, 4759-4765]. Here we investigate the interaction of three altered signal sequences with phospholipid membranes containing cardiolipin to ascertain the importance of electrostatic and hydrophobic interactions with the membrane. The three already described peptides were derivatives of the signal sequence from aldehyde dehydrogenase, which is composed of three segments, two helices separated by a linker. ANCN had the C-helix replaced by the N-helix of the signal sequence of cytochrome c oxidase subunit IV, ANCC had the C-terminal helix replaced by the C-terminal random coil of cytochrome oxidase subunit IV, and linker deleted had the linker region deleted. ANCC, which functioned poorly as a signal sequence, had a very low affinity for binding to the negatively charged membranes. In contrast, both ANCN and linker deleted showed a relatively high affinity for the membranes and were capable of functioning as a good leader sequence. It appears that linker deleted possessed a stronger hydrophobic effect with membranes while ANCN had a higher electrostatic interaction. On the basic of these studies, a model was proposed to describe the interaction of mitochondrial signal sequences with negatively charged phospholipid membranes involving electrostatic interaction for initial binding and hydrophobic interaction for insertion.(ABSTRACT TRUNCATED AT 250 WORDS)

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The importance of the amino terminus of the mitochondrial precursor protein apocytochrome c for translocation across model membranes

Cited by 63 publications

References 55 publications

Molecular dynamics simulations of cytochrome c unfolding in AOT reverse micelles: The first steps

Molecular dynamics simulations of cytochrome c unfolding in AOT reverse micelles: The first steps

Membrane Location of Spin-labeled Apocytochrome c and Cytochrome c Determined by Paramagnetic Relaxation Agents

Evaluation of electrostatic and hydrophobic effects on the interaction of mitochondrial signal sequences with phospholipid bilayers

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