Interactions involved in grasping and locking of the inhibitory peptide IF1 by mitochondrial ATP synthase
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- 作者：Qian Wua ; 1 ; qian.wu@cea.fr" class="auth_mail ; Tiona Andrianaivomananjaonaa ; 1 ; tiona.andrianaivomananjaona@cea.fr" class="auth_mail ; Emmanuel Tetaudb ; tetaud@ibgc.cnrs.fr" class="auth_mail ; Vincent Corvesta ; 2 ; vcorvest@calixar.com" class="auth_mail ; Francis Harauxa ; francis.haraux@cea.fr" class="auth_mail
- 关键词：F0F1-ATPase ; ATP synthase complex (EC 3.6.3.14) ; F1-ATPase ; isolated extrinsic part of ATP synthase ; IF1 ; endogenous inhibitory peptide of mitochondrial ATP synthase ; yIF1 ; IF1 from yeast ; SMP ; submitochondrial particle ; pmf ; protonmotive force ; Tris ; tris(hydroxymethyl)aminomethane ; MES ; 2-(N-morpholino)ethanesulfonic acid ; FCCP ; carbonyl cyanide-p-trifluoromethoxyphenylhydrazone ; Ni-NTA ; nickel-nitrilotriacetic acid ; PGK ; phosphoglycerate kinase ; KanMX4 ; kanamycin-resistance gene ; G418 ; geneti
- 刊名：Biochimica et Biophysica Acta (BBA)/Bioenergetics
- 出版年：June 2014
- 年：2014
- 卷：1837
- 期：6
- 页码：761-772
- 全文大小：1223 K
文摘
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The two-step binding of IF1 inhibitory peptide to mitochondrial F1-ATPase is studied.
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The effect of F1-ATPase mutations on IF1 binding is investigated for the first time.
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Kinetic experiments reveal residues involved in IF1 initial binding and final locking.
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Some residues of 尾 subunit are involved in IF1 grasping.
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Some 伪 and 尾 motifs contribute to IF1 locking; their interactions with 纬 may help.