High impact information on ATPAF2

• Work in Saccharomyces cerevisiae has shown that Atp12p binds to unassembled alpha subunits of F(1) and in so doing prevents the alpha subunit from associating with itself in non-productive complexes during assembly of the F(1) moiety of the mitochondrial ATP synthase [1].
• Atp11p and Atp12p are assembly factors for the F(1)-ATPase in human mitochondria [2].
• The ATP concentration was not affected during exposure to fresh or acidified broth, while 4- to 12-h exposures of nonculturable cells to lysed human erythrocytes increased cellular ATP 12- to 150-fold [3].

Biological context of ATPAF2

• The mechanism of the F1 assembly is preserved in all eukaryotic lineages that are capable of ATP synthesis via oxidative phosphorylation and requires Atp11p and Atp12p [4].
• Atp11p and Atp12p are chaperones for F(1)-ATPase biogenesis in mitochondria [5].

Other interactions of ATPAF2

• Differential expression of ATPAF1 and ATPAF2 genes encoding F(1)-ATPase assembly proteins in mouse tissues [6].

Analytical, diagnostic and therapeutic context of ATPAF2

• Our phylogenetic data served as a source for comparative sequence analysis, which identified evolutionarily conserved residues, putative functional domains and their basic structural features for Atp10p, Atp11p, and Atp12p orthologs [4].

References