High impact information on STF1

• Using mitochondria isolated from null mutants deficient in Inh1, Stf1, and Stf2, we demonstrate that formation of the F(1)F(0)-ATP synthase dimers is not adversely affected by the absence of these proteins [1].
• Inhibition of the yeast F(0)F(1)-ATP synthase by the regulatory peptides IF1 and STF1 was studied using intact mitochondria and submitochondrial particles from wild-type cells or from mutants lacking one or both peptides [2].
• In intact mitochondria, endogenous IF1 only inhibited uncoupled ATP hydrolysis and endogenous STF1 had no effect [2].
• Previous application of a membrane potential favored the release of endogenous IF1 and STF1 [2].
• 0. Our data do not support previously proposed effects of STF1, like the stabilization of the IF1-F(0)F(1) complex or the replacement of IF1 on its binding site in the presence of the proton-motive force or at high pH, and raise the question of the conditions under which STF1 could regulate ATPase activity in vivo [2].

Biological context of STF1

• These observations showed that IF1 and STF1 can fully inhibit ATP hydrolysis at physiological concentrations and are sensitive to the same effectors [2].

Anatomical context of STF1

• The RPL44' gene from Saccharomyces cerevisiae encoding the ribosomal protein YP1 beta(L44') has been found to be linked to the STF1 gene, encoding a stabilizing factor of the F1F0-ATPase inhibitor protein from mitochondria [3].

Analytical, diagnostic and therapeutic context of STF1

• Sequence alignment revealed that this region contains a hydrophobic motif for CaM binding, highly conserved in both yeast IF1 and STF1 sequences [4].

References