Modulation of coupling in the Escherichia coli ATP synthase by ADP and P_i: Role of the ε subunit C-terminal domain

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• 作者：M. D'Alessandro^a ; ¹ ; P. Turina^a ; ^{paola.turina@unibo.it} ; ; B.A. Melandri^a ; S.D. Dunn^b
• 关键词：EFOF1 ; ATP synthase of E. coli ; EF1 ; hydrophylic subcomplex of the ATP synthase of E. coli ; εCTD ; C-terminal domain of the ε-subunit ; εNTD ; N-terminal domain of the ε-subunit ; Tris ; (hydroxymethyl)aminomethane ; PMSF ; phenylmethylsulfonyl fluoride ; MOPS ; 3-(N-morpholino)propanesulfonic acid ; Tricine ; N-[2-hydroxy-1 ; 1-bis(hydroxymethyl)ethyl] glycine ; SDS-PAGE ; sodium dodecyl sulfate polyacrylamide gel electrophoresis ; PVDF ; polyvinylidene difluoride ; EDTA ; ethylenediaminetetraacetic acid ; LDAO ; l
• 刊名：Biochimica et Biophysica Acta (BBA) - Bioenergetics
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：1858
• 期：1
• 页码：34-44
• 全文大小：1122 K
• 卷排序：1858

文摘

ATP-Dependent H+-pumping by E. coli ATP synthase depends on bound ADP and Pi. ε Subunit C-terminal domain truncation (εCTD ➔ εtr) reduced H+-pumping. ATP synthase-εtr maintained ATP hydrolytic activity; coupling was defective. Addition of ADP + Pi to ATP synthase-εtr stimulated ATP-dependent H+-pumping. It is proposed that εCTD modulates the binding of ADP and Pi to regulate coupling.