| Literature DB >> 8764999 |
Abstract
Mitochondrial ATP synthase is responsive to changes in cytosolic calcium concentration, but the regulatory mechanisms are unclear. Here we identified a major 52 kDa calcium-binding protein in rat enamel cells as the mitochondrial ATP synthase F1-beta-subunit. The F1-beta-subunit behaved as a low affinity and moderate capacity calcium-binding protein during comparative 45Ca overlay analyses. Equivalent behavior was shown by the F1-beta-subunit from rat liver mitochondria, but not by the homologous F1-alpha-subunit, supporting the specificity of calcium binding. Evidence that the catalytic F1-beta-subunit binds calcium specifically introduces new mechanistic possibilities for regulating ATP synthase, and thereby coordinating ATP production with demand for ATP-fuelled calcium pump activity.Entities:
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Year: 1996 PMID: 8764999 DOI: 10.1016/0014-5793(96)00767-3
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124