Arginine 107 of yeast ATP synthase subunit g mediates sensitivity of the mitochondrial permeability transition to phenylglyoxal

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Guo , L , Carraro , M , Sartori , G , Minervini , G , Eriksson , O , Petronilli , V & Bernardi , P 2018 , ' Arginine 107 of yeast ATP synthase subunit g mediates sensitivity of the mitochondrial permeability transition to phenylglyoxal ' , Journal of Biological Chemistry , vol. 293 , no. 38 , pp. 14632-14645 . https://doi.org/10.1074/jbc.RA118.004495

Title: Arginine 107 of yeast ATP synthase subunit g mediates sensitivity of the mitochondrial permeability transition to phenylglyoxal
Author: Guo, Lishu; Carraro, Michela; Sartori, Geppo; Minervini, Giovanni; Eriksson, Ove; Petronilli, Valeria; Bernardi, Paolo
Contributor: University of Helsinki, Ove Eriksson-Rosenberg / Principal Investigator
Date: 2018-09-21
Language: eng
Number of pages: 14
Belongs to series: Journal of Biological Chemistry
ISSN: 0021-9258
URI: http://hdl.handle.net/10138/252431
Abstract: Modification with arginine-specific glyoxals modulates the permeability transition (PT) of rat liver mitochondria, with inhibitory or inducing effects that depend on the net charge of the adduct(s). Here, we show that phenylglyoxal (PGO) affects the PT in a species-specific manner (inhibition in mouse and yeast, induction in human and Drosophila mitochondria). Following the hypotheses (i) that the effects are mediated by conserved arginine(s) and (ii) that the PT is mediated by the F-ATP synthase, we have narrowed the search to 60 arginines. Most of these residues are located in subunits alpha, beta, gamma, epsilon, a, and c and were excluded because PGO modification did not significantly affect enzyme catalysis. On the other hand, yeast mitochondria lacking subunit g or bearing a subunit g R107A mutation were totally resistant to PT inhibition by PGO. Thus, the effect of PGO on the PT is specifically mediated by Arg-107, the only subunit g arginine that has been conserved across species. These findings are evidence that the PT is mediated by F-ATP synthase.
Subject: ATP synthase
mitochondria
mitochondrial permeability transition (MPT)
calcium
bioenergetics
METHYLGLYOXAL METABOLISM
SACCHAROMYCES-CEREVISIAE
DROSOPHILA-MELANOGASTER
CRISTAE MORPHOLOGY
PROTEIN GLYCATION
CHANNEL FORMATION
CA2+ RELEASE
CELL-DEATH
C-SUBUNIT
IN-SITU
3111 Biomedicine
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