Inactivation of the mitochondrial ATPase inhibitor protein by chemical modification with diethylpyrocarbonate

Guerrieri, Ferruccio; Zanotti, Franco; Wu, Yan; Scarfò, Rosanna; Papa, Sergio

doi:10.1016/0005-2728(87)90232-5

Cited by 21 publications

(4 citation statements)

References 37 publications

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“…In ox heart IF1, residues 1-9 can be removed proteolytically without affecting inhibitory activity, but further removal is deleterious [114]. Also in the ox heart protein, two pairs of histidine residues are potentially interesting, especially since IF1 binds to F. much less strongly after treatment with diethylpyrocarbonate [115].…”

Section: Regulator Proteinsmentioning

confidence: 99%

Control of mitochondrial ATP synthesis in the heart

Harris

1991

Biochemical Journal

323

199

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The maintenance of a constant ATP level ('set-point') is a vital homeostatic function shared by eukaryotic cells. In particular, mammalian myocardium exquisitely safeguards its ATP set-point despite 10-fold fluctuations in cardiac workload. However, the exact mechanisms underlying this regulation of ATP homeostasis remain elusive. Here we show mitochondrial flashes (mitoflashes), recently discovered dynamic activity of mitochondria, play an essential role for the auto-regulation of ATP set-point in the heart. Specifically, mitoflashes negatively regulate ATP production in isolated respiring mitochondria and, their activity waxes and wanes to counteract the ATP supply-demand imbalance caused by superfluous substrate and altered workload in cardiomyocytes. Moreover, manipulating mitoflash activity is sufficient to inversely shift the otherwise stable ATP set-point. Mechanistically, the Bcl-xL-regulated proton leakage through F 1 F o-ATP synthase appears to mediate the coupling between mitoflash production and ATP set-point regulation. These findings indicate mitoflashes appear to constitute a digital auto-regulator for ATP homeostasis in the heart.

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Section: Regulator Proteinsmentioning

confidence: 99%

Control of mitochondrial ATP synthesis in the heart

Harris

1991

Biochemical Journal

323

199

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“…The vpH component of PMF, in particular the matrix pH, on which side IF 1 is associated with the complex, is the critical factor for its binding and inhibitory activity [2,5,6]. In our laboratory it has been found that IF 1 also inhibits passive proton conduction by the F 1 F 0 complex [6].…”

Section: Introductionmentioning

confidence: 84%

“…IF 1 associates reversibly in a 1:1 stoichiometry with F 1 F 0 , from which it is displaced by the PMF, thus IF 1 has no significant effect on ATP synthesis [2]. The ΔpH component of PMF, in particular the matrix pH, on which side IF 1 is associated with the complex, is the critical factor for its binding and inhibitory activity [2,5,6]. In our laboratory it has been found that IF 1 also inhibits passive proton conduction by the F 1 F 0 complex [6].…”

Section: Introductionmentioning

confidence: 98%

“…The 42–58 segment has at positions 48, 49, 55 and 56 four histidines. Histidine chemical modification [5,6], site directed mutagenesis of His49 [16] and chemical substitution of His48, 49, 55, 56 or of Lys46, 47, 58 in the synthetic 42–58 peptide [13] have shown that these residues are directly responsible for the activity and pH dependence of IF 1 .…”

Section: Introductionmentioning

confidence: 99%

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