caa a22 4500 397555873 CHVBK 20180308164801.0 cr unu---uuuuu 161202e199601 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021208 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021208 An Intrinsic ATPase Inhibitor Binds near the Active Site of Yeast Mitgchondrial F1-ATPase [Elektronische Daten] [Naoki Ichikawa, Yukuo Yoshida, Tadao Hashimoto, Kunio Tagawa] An ATPase inhibitor and its stabilizing factor, the 9K protein, are regulatory factors of F1Fo-ATPase. The binding sites for these factors on F1 were examined using the zero length cross-linkers, N-ethoxycarbonyl-2-ethoxy-l,2-dihydroquinoline, and l-ethyl-3-[3-di-methylamino)propyl]carbodiimide. The cross-linked products were analyzed by immuno-blotting after SDS-polyacrylamide gel electrophoresis. The inhibitor and the 9K protein cross-linked to the α andβsubunits of F1, indicating that they interacted with both subunits. Peptide mapping and amino acid sequence analysis of the cross-linked products after weak acid hydrolysis showed that the inhibitor cross-linked to the Pro334-Asp363 region of the βsubunit. Amino acid sequence analysis of the cross-linked peptide showed that the inhibitor binds to Asp363 of the βsubunit. As this region contains the amino acid residues, including Tyr359, that are modified by nucleotide analogs and form the active site, the inhibitor probably binds to the catalytic site of F1 © by the Journal of Biochemistry Regular Papers nationallicence ATPase inhibitor nationallicence cross-linking nationallicence F1ATPase nationallicence regulatory protein nationallicence subunit of F1ATPase nationallicence Ichikawa Naoki Department of Food and Nutrition, Faculty of Human Life Science, Osaka City University Sugimotochou, Osaka 558 aut Yoshida Yukuo Department of Physiological Chemistry, Medical School, Osaka University 2-2 Yamadaoka, Suita, Osaka 565 aut Hashimoto Tadao Department of Food and Nutrition, Faculty of Human Life Science, Osaka City University Sugimotochou, Osaka 558 aut Tagawa Kunio Department of Food and Nutrition, Faculty of Human Life Science, Osaka City University Sugimotochou, Osaka 558 aut The Journal of Biochemistry Oxford University Press 119/1(1996-01), 193-199 0021-924X 119:1<193 1996 119 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021208 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021208 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Ichikawa Naoki Department of Food and Nutrition, Faculty of Human Life Science, Osaka City University Sugimotochou, Osaka 558 aut NATIONALLICENCE 700 1- Yoshida Yukuo Department of Physiological Chemistry, Medical School, Osaka University 2-2 Yamadaoka, Suita, Osaka 565 aut NATIONALLICENCE 700 1- Hashimoto Tadao Department of Food and Nutrition, Faculty of Human Life Science, Osaka City University Sugimotochou, Osaka 558 aut NATIONALLICENCE 700 1- Tagawa Kunio Department of Food and Nutrition, Faculty of Human Life Science, Osaka City University Sugimotochou, Osaka 558 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 119/1(1996-01), 193-199 0021-924X 119:1<193 1996 119 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