caa a22 4500 397494580 CHVBK 20180308164518.0 cr unu---uuuuu 161202e199503 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a124757 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a124757 Cleavage of Bovine Mitochondrial ATPase Inhibitor with Endopeptidases, and Binding of the Resulting Peptides to the Interface between the α- and β-Subunits of F1 ATPase [Elektronische Daten] [Tadao Hashimoto, Yuji Yamamoto, Yukuo Yoshida, Yukuo Yoshida] Mitochondrial ATPase inhibitor binds to F1 ATPase, forming an equimolar complex with the enzyme, and the binding site has been reported to be located in the β-subunit [Klein, G. et al. (1980) Biochemistry 19,2919-2925] or at the interface between the α- and β-subunits of the enzyme [Mimura, H. et al. (1993) J. Biochem. 113, 350-354]. In the present study, bovine ATPase inhibitor as well as three peptide fragments of the inhibitor, Glyl-Asn51, Glu52-Asp84, and Lys46-Asp84, were used to examine the features of the binding of the inhibitor and F1ATPase. Only the amino terminal fragment, Glyl-Asn51, exhibited a similar level of inhibitory activity to that of the native ATPase inhibitor. Although the other two carboxyl terminal side fragments did not exhibit any inhibitory activity, they interfered with the action of the intact ATPase inhibitor when they were pre-loaded to F1 ATPase. Since the two carboxyl fragments did not interfere with the inhibitory action of the amino fragment, it is inferred that the inhibitor interacts with F1 ATPase at its carboxyl terminal region prior to binding at the amino terminal region of the enzyme. Cross-linking experiments revealed that ATPase inhibitor bound to the α- and β-subunits of F1 ATPase, and that the amino terminal peptide preferentially bound to the α-subunit and the carboxyl terminal peptides to the β-subunit. © 1995 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence ATPase inhibitor nationallicence mitochondria nationallicence F1 ATPase nationallicence regulatory protein nationallicence subunit of F1ATPase nationallicence Hashimoto Tadao Department of Applied Chemistry, Muroran Institute of Technology, Muroran, Hokkaido 050 aut Yamamoto Yuji Department of Applied Chemistry, Muroran Institute of Technology, Muroran, Hokkaido 050 aut Yoshida Yukuo Department of Physiological Chemistry, Medical School, Osaka University, Suita, Osaka 565 aut Yoshida Yukuo Department of Applied Chemistry, Muroran Institute of Technology, Muroran, Hokkaido 050 aut The Journal of Biochemistry Oxford University Press 117/3(1995-03), 641-647 0021-924X 117:3<641 1995 117 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a124757 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a124757 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Hashimoto Tadao Department of Applied Chemistry, Muroran Institute of Technology, Muroran, Hokkaido 050 aut NATIONALLICENCE 700 1- Yamamoto Yuji Department of Applied Chemistry, Muroran Institute of Technology, Muroran, Hokkaido 050 aut NATIONALLICENCE 700 1- Yoshida Yukuo Department of Physiological Chemistry, Medical School, Osaka University, Suita, Osaka 565 aut NATIONALLICENCE 700 1- Yoshida Yukuo Department of Applied Chemistry, Muroran Institute of Technology, Muroran, Hokkaido 050 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 117/3(1995-03), 641-647 0021-924X 117:3<641 1995 117 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford