Regulation of the F<sub>1sub>F<sub>0sub>-ATP Synthase Rotary Nanomotor in its Monomeric-Bacterial and Dimeric-Mitochondrial Forms
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- 作者：Jos茅 J. Garc铆a-Trejo and Edgar Morales-R铆os
- 关键词：F1F0 ATPase ; F1F0 ATP synthase ; IF1 ; Inhibitor protein ; Epsilon ; Dimeric ; Rotation ; Interface ; Cristae ; Regulation ; F1 ATPase
- 刊名：Journal of Biological Physics
- 出版时间：April, 2008
- 出版年：2008
- 期刊代码：14_00920606
- 类别：en
- 卷：34
- 期：1-2
- 页码：197-212
- 数据来源：sp
摘要
The F<sub>1sub>F<sub>0sub>-adenosine triphosphate (ATP) synthase rotational motor synthesizes most of the ATP required for living from adenosine diphosphate, Pi, and a proton electrochemical gradient across energy-transducing membranes of bacteria, chloroplasts, and mitochondria. However, as a reversible nanomotor, it also hydrolyzes ATP during de-energized conditions in all energy-transducing systems. Thus, different subunits and mechanisms have emerged in nature to control the intrinsic rotation of the enzyme to favor the ATP synthase activity over its opposite and commonly wasteful ATPase turnover. Recent advances in the structural analysis of the bacterial and mitochondrial ATP synthases are summarized to review the distribution and mechanism of the subunits that are part of the central rotor and regulate its gyration. In eubacteria, the ε subunit works as a ratchet to favor the rotation of the central stalk in the ATP synthase direction by extending and contracting two α-helixes of its C-terminal side and also by binding ATP with low affinity in thermophilic bacteria. On the other hand, in bovine heart mitochondria, the so-called inhibitor protein (IF<sub>1sub>) interferes with the intrinsic rotational mechanism of the central γ subunit and with the opening and closing of the catalytic β-subunits to inhibit its ATPase activity. Besides its inhibitory role, the IF<sub>1sub> protein also promotes the dimerization of the bovine and rat mitochondrial enzymes, albeit it is not essential for dimerization of the yeast F<sub>1sub>F<sub>0sub> mitochondrial complex. High-resolution electron microscopy of the dimeric enzyme in its bovine and yeast forms shows a conical shape that is compatible with the role of the ATP synthase dimer in the formation of tubular the cristae membrane of mitochondria after further oligomerization. Dimerization of the mitochondrial ATP synthase diminishes the rotational drag of the central rotor that would decrease the coupling efficiency between rotation of the central stalk and ATP synthesis taking place at the F<sub>1sub> portion. In addition, F<sub>1sub>F<sub>0sub> dimerization and its further oligomerization also increase the stability of the enzyme to natural or experimentally induced destabilizing conditions.