Disease relevance of ATP5J2

• Studies on Na+ and H+ translocation through the Fo part of the Na(+)-translocating F1Fo ATPase from Propionigenium modestum: discovery of a membrane potential dependent step [1].

High impact information on ATP5J2

• Purified F1Fo ATPase of Propionigenium modestum was rapidly inactivated by dicyclohexylcarbodiimide (DCCD) with k2 = 1.2 x 10(5) M-1 min-1 at pH 5.6 and 0 degree C. Na+ ions provided specific protection from the modification by DCCD while protons stimulated the reaction [2].
• Kinetics of inactivation of the F1Fo ATPase of Propionigenium modestum by dicyclohexylcarbodiimide in relationship to H+ and Na+ concentration: probing the binding site for the coupling ions [2].
• Subunit c of the F1Fo-ATPase from Propionigenium modestum was extracted from the particulate cell fraction with chloroform/methanol [3].
• This is in spite of the fact that Jurkat cells pretreated with carbonyl cyanide m-chlorophenylhydrazone plus oligomycin are otherwise energetically competent, due to a high rate of glycolysis and the inhibition of mitochondrial F1Fo-ATPase by oligomycin [4].
• K+ portasomes, which resemble F1-Fo ATPase particles, stud these K+ transporting apical membranes and are though to be the unit of active K+ transport [5].

Other interactions of ATP5J2

• Mitochondrial ATP synthase (F1Fo-ATPase) is regulated by an intrinsic ATPase inhibitor protein [6].

References