ATP Induces a Conformational Change in Lipid-bound Cytochrome c

Tuominen, Esa K. J.; Zhu, Kun; Wallace, Carmichael J. A.; Clark‐Lewis, Ian; Craig, Douglas B.; Rytömaa, Marjatta; Kinnunen, Paavo K.J.

doi:10.1074/jbc.m100853200

Cited by 54 publications

(65 citation statements)

References 58 publications

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“…40%) complex dissociation in agreement with Tuominen et al [38]. In fact, although the latter experiments were carried out under different conditions, (1-3 mM) concentration of ATP significantly altered the tertiary conformation of phosphatidylglycero-bound horse cyt c. Therefore, although 1-3 mM ATP is not enough to induce dissociation, it is sufficient to destabilize the complex.…”

Section: Effect Of Atp On Complex Formation/dissociationsupporting

confidence: 87%

The effects of ATP and sodium chloride on the cytochrome c–cardiolipin interaction: The contrasting behavior of the horse heart and yeast proteins

Sinibaldi¹,

Droghetti²,

Polticelli³

et al. 2011

Journal of Inorganic Biochemistry

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In cells a portion of cytochrome c (cyt c) (15-20%) is tightly bound to cardiolipin (CL), one of the phospholipids constituting the mitochondrial membrane. The CL-bound protein, which has nonnative tertiary structure, altered heme pocket, and disrupted Fe(III)-M80 axial bond, is thought to play a role in the apoptotic process. This has attracted considerable interest in order to clarify the mechanisms governing the cyt c-CL interaction. Herein we have investigated the binding reaction of CL with the c-type cytochromes from horse heart and yeast. Although the two proteins possess a similar tertiary architecture, yeast cyt c displays lower stability and, contrary to the equine protein, it does not bind ATP and lacks pro-apoptotic activity. The study has been performed in the absence and in the presence of ATP and NaCl, two compounds that influence the (horse cyt c)-CL binding process and, thus, the pro-apoptotic activity of the protein. The two proteins behave differently: while CL interaction with horse cyt c is strongly influenced by the two effectors, no effect is observed for yeast cyt c. It is noteworthy that NaCl induces dissociation of the (horse cyt c)-CL complex but has no influence on that of yeast cyt c. The differences found for the two proteins highlight that specific structural factors, such as the different local structure conformation of the regions involved in the interactions with either CL or ATP, can significantly affect the behavior of cyt c in its reaction with liposomes and the subsequent pro-apoptotic action of the protein.

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Section: Effect Of Atp On Complex Formation/dissociationsupporting

confidence: 87%

The effects of ATP and sodium chloride on the cytochrome c–cardiolipin interaction: The contrasting behavior of the horse heart and yeast proteins

Sinibaldi¹,

Droghetti²,

Polticelli³

et al. 2011

Journal of Inorganic Biochemistry

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show abstract

“…The electrostatic A-site interaction can be reversed by ATP and does not involve pronounced changes in the protein conformation as revealed by circular dichroism measurements on native cyt c and fluorescence spectroscopy studies using a derivative of cyt c, in which the heme iron has been substituted by zinc (11). Studies of the C-site lipid-bound cyt c have demonstrated this type of interaction not to be reversed by ATP (10).…”

Section: Cytochrome C (Cyt C)mentioning

confidence: 99%

Phospholipid-Cytochrome c Interaction

Tuominen¹,

Wallace²,

Kinnunen³

2002

Journal of Biological Chemistry

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290

115

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“…Membrane association of Cyc1 occurs by electrostatic interactions of encounter complexes with bc 1 , CcO, and the lipid bilayer as well as hydrophobic effects with the bilayer (36,42,43). Cardiolipin contributes to the membrane anchoring of Cyc1 (36).…”

Section: Discussionmentioning

confidence: 99%

“…To gain insights into the mechanism by which Cyc1 restores CcO function in coa4⌬ cells, we sought to investigate the membrane association of Cyc1 and stability of CcO in WT versus coa4⌬ cells. Cyc1 is associated with the inner membrane by forming transient encounter complexes with bc 1 and CcO, primarily by electrostatic interactions in addition to hydrophobic contacts with the lipid bilayer that involve cardiolipin (36,42,43). First, mitoplasts isolated from each cell were treated with increasing salt concentrations or proteinase K, and membrane association of Cyc1 was assessed by immunoblotting (Fig.…”

Section: Characterization Of Human Surf1 Missense Mutations In the Yementioning

confidence: 99%

Analysis of Leigh Syndrome Mutations in the Yeast SURF1 Homolog Reveals a New Member of the Cytochrome Oxidase Assembly Factor Family

Bestwick

Jeong

Khalimonchuk

et al. 2010

Molecular and Cellular Biology

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ATP Induces a Conformational Change in Lipid-bound Cytochrome c

Cited by 54 publications

References 58 publications

The effects of ATP and sodium chloride on the cytochrome c–cardiolipin interaction: The contrasting behavior of the horse heart and yeast proteins

The effects of ATP and sodium chloride on the cytochrome c–cardiolipin interaction: The contrasting behavior of the horse heart and yeast proteins

Phospholipid-Cytochrome c Interaction

Analysis of Leigh Syndrome Mutations in the Yeast SURF1 Homolog Reveals a New Member of the Cytochrome Oxidase Assembly Factor Family

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