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

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) (Johans et al.， (2005) 280， 12130-12136). Here we show that phenylglyoxal (PGO) affects the PT in a species-specific manner (inhibition in mouse and yeast， induction in human and 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 α， β， γ， ε， a， 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 R107， the only subunit g arginine that has been conserved across species. These findings are evidence that the PT is mediated by F-ATP synthase.