Molecular evolution of the modulator of chloroplast ATP synthase: origin of the conformational change dependent regulation.
Chloroplast ATP synthase synthesizes ATP by utilizing a proton gradient as an energy supply, which is generated by photosynthetic electron transport. The activity of the chloroplast ATP synthase is regulated in several specific ways to avoid futile hydrolysis of ATP under various physiological conditions. Several regulatory signals such as Delta mu H(+), tight binding of ADP and its release, thiol modulation, and inhibition by the intrinsic inhibitory subunit epsilon are sensed by this complex. In this review, we describe the function of two regulatory subunits, gamma and epsilon, of ATP synthase based on their possible conformational changes and discuss the evolutionary origin of these regulation systems.
Hisabori
Toru
T
Chemical Resources Laboratory, Tokyo Institute of Technology, and ATP System Project, Exploratory Research for Advanced Technology, Japan Science and Technology Corporation, Yokohama, Japan. thisabor@res.titech.ac.jp
Ueoka-Nakanishi
Hanayo
H
Konno
Hiroki
H
Koyama
Fumie
F
D025222:Chloroplast Proton-Translocating ATPases / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000378:metabolism; D019143:Evolution, Molecular; D008958:Models, Molecular; D010084:Oxidation-Reduction; D011487:Protein Conformation; D021122:Protein Subunits
D021122:Protein Subunits; D025222:Chloroplast Proton-Translocating ATPases