ATP synthase is a multi-subunit enzyme responsible for synthesizing ATP during oxidative phosphorylation. The alpha subunit (atpA) forms part of the F1 catalytic core, interacting with the beta subunit to drive ATP production . Key features include:
Structure: Contains nucleotide-binding domains critical for ATP synthesis/hydrolysis .
Conservation: Highly conserved across eukaryotes and prokaryotes .
Anti-atpA antibodies are widely used to study ATP synthase structure, function, and dysfunction. Key antibody types include:
Membrane-bound vs. Isolated Subunits: Anti-atpA monoclonal antibodies bind more effectively to isolated alpha subunits than to intact ATP synthase, suggesting epitopes are partially buried in the holoenzyme .
Conformational Sensitivity: Antibody binding is enhanced when ATP synthase is denatured (e.g., urea treatment), indicating epitope shielding in native states .
Anti-atpA antibodies exhibit broad cross-reactivity due to sequence conservation. For example, antibodies raised against Arabidopsis thaliana ATP synthase react with algal, mammalian, and bacterial homologs .
Dysregulation of ATP synthase is linked to mitochondrial disorders and cancers. Anti-atpA antibodies enable detection of ATP5A expression changes in diseased tissues .
Mitochondrial Disease Diagnostics: Anti-atpA antibodies identify ATP synthase deficiencies in muscle biopsies .
Cancer Research: ATP5A overexpression in tumors correlates with chemoresistance; antibodies aid in profiling ATP synthase in cancer cells .
Bacterial Studies: Prokaryotic ATP synthase alpha subunits are targeted to study antibiotic mechanisms .
KEGG: ath:ArthCp007
STRING: 3702.ATCG00120.1