THE MITOCHONDRIAL ATP SYNTHASE INHIBITOR PROTEIN BINDS NEAR THE C-TERMINUS OF THE F1 BETA-SUBUNIT

作     者：JACKSON, PJ HARRIS, DA 

作者机构：UNIV OXFORDDEPT BIOCHEMS PARKS RDOXFORD OX1 3QUENGLAND 

出 版 物：《FEBS LETTERS》 (欧洲生化学会联合会快报)

年 卷 期：1988年第229卷第1期

页      面：224-228页

核心收录：

学科分类：0710[理学-生物学] 071010[理学-生物化学与分子生物学] 07[理学] 

主　　题：Mitochondria ATP synthase F 1 -ATPase ATPase inhibitor protein (Bovine heart) EEDQ N -ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline HPLC high-performance liquid chromatography IF 1 mitochondrial ATP synthase inhibitor protein PTH phenylthiohydantoin SDS-PAGE SDS-polyacrylamide gel electrophoresis 

摘      要：The specific, mitochondrial ATP synthase protein (IF1) was covalently cross-linked to its binding site on the catalytic sector of the enzyme (F1-ATPase). The cross-linked complex was selectively cleaved, leaving IF1 intact to facilitate the subsequent purification of the F1 fragment to which IF1 was cross-linked. This fragment was identified by sequence analysis as comprising residues 394-459 on the F1 beta-subunit, near the C-terminus. This finding is discussed in the light of secondary structure predictions for both IF1 and the F1 beta-subunit, and sequence homologies between mitochondrial and other ATP synthases.