期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 286, 期 15, 页码 13423-13429出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M110.155986
关键词
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资金
- Ministry of Education, Culture, Sports, Science, and Technology, Japan [18074002]
- Grants-in-Aid for Scientific Research [18074002] Funding Source: KAKEN
The ATPase activity of chloroplast and bacterial F-1-ATPase is strongly inhibited by both the endogenous inhibitor epsilon and tightly bound ADP. Although the physiological significance of these inhibitory mechanisms is not very well known for the membrane-bound F0F1, these are very likely to be important in avoiding the futile ATP hydrolysis reaction and ensuring efficient ATP synthesis in vivo. In a previous study using the alpha(3)beta(3)gamma complex of F-1 obtained from the thermophilic cyanobacteria, Thermosynechococcus elongatus BP-1, we succeeded in determining the discrete stop position, similar to 80 degrees forward from the pause position for ATP binding, caused by epsilon-induced inhibition (epsilon-inhibition) during gamma rotation (Konno, H., Murakami-Fuse, T., RIM, F., Koyama, F., Ueoka-Nakanishi, H., Pack, C. G., Kinjo, M., and Hisabori, T. (2006) EMBO J. 25, 4596 4604). Because gamma in ADP-inhibited F-1 also pauses at the same position, ADP-induced inhibition (ADP-inhibition) was assumed to be linked to epsilon-inhibition. However, ADP-inhibition and epsilon-inhibition should be independent phenomena from each other because the ATPase core complex, alpha(3)beta(3)gamma, also lapses into the ADP-inhibition state. By way of thorough biophysical and biochemical analyses, we determined that the E subunit inhibition mechanism does not directly correlate with ADP-inhibition. We suggest here that the cyanobacterial ATP synthase epsilon subunit carries out an important regulatory role in acting as an independent braking system for the physiologically unfavorable ATP hydrolysis reaction.
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