来自大肠杆菌的ATP合酶（F1F0）膜部分（F0）的亚基b对于H+转运以及水溶性F1部分的结合是不可或缺的。
Subunit b of the membrane moiety (F0) of ATP synthase (F1F0) from Escherichia coli is indispensable for H+ translocation and binding of the water-soluble F1 moiety.
作者信息
Schneider E, Altendorf K
出版信息
Proc Natl Acad Sci U S A. 1984 Dec;81(23):7279-83. doi: 10.1073/pnas.81.23.7279.
Abstract
The ATP synthase complex, designated F1F0, of Escherichia coli is composed of a water-soluble portion (F1; membrane-associated ATPase, EC 3.6.1.3) with ATP-hydrolyzing activity and a membrane-integrated part (F0) with H+-translocating activity. F0 is built up from three kinds of subunits (a, b, and c). We have isolated the F0 portion directly from membranes of an E. coli strain (KY 7485) that overproduces the enzyme several fold. Subunit b was extracted from purified F0 by two methods. One method included prolonged incubation of the F0 complex in the presence of trichloroacetate (2.5 M) and the separation of subunit b and an a-c complex by gel filtration. Alternatively, subunit b was extracted by deoxycholate and separated from the a-c complex by hydrophobic-interaction chromatography. Integrated into liposomes, the a-c complex exhibited neither H+ uptake nor binding of F1. However, a functional F0 complex was reconstituted by adding stoichiometric amounts of subunit b to the a-c complex.
摘要
大肠杆菌的ATP合酶复合体，即F1F0，由具有ATP水解活性的水溶性部分（F1；膜结合ATP酶，EC 3.6.1.3）和具有H⁺转运活性的膜整合部分（F0）组成。F0由三种亚基（a、b和c）构成。我们已直接从一株能使该酶过量表达数倍的大肠杆菌菌株（KY 7485）的膜中分离出F0部分。通过两种方法从纯化的F0中提取亚基b。一种方法是在三氯乙酸（2.5 M）存在下将F0复合体长时间温育，然后通过凝胶过滤分离亚基b和a - c复合体。另一种方法是用脱氧胆酸盐提取亚基b，并通过疏水相互作用色谱法将其与a - c复合体分离。整合到脂质体中的a - c复合体既不表现出H⁺摄取，也不表现出与F1的结合。然而，通过向a - c复合体中添加化学计量的亚基b可重建功能性F0复合体。
相似文献
1
Subunit b of the membrane moiety (F0) of ATP synthase (F1F0) from Escherichia coli is indispensable for H+ translocation and binding of the water-soluble F1 moiety.
Proc Natl Acad Sci U S A. 1984 Dec;81(23):7279-83. doi: 10.1073/pnas.81.23.7279.
2
Topological and functional aspects of the proton conductor, F0, of the Escherichia coli ATP-synthase.
Biosci Rep. 1982 Aug;2(8):631-9. doi: 10.1007/BF01314228.
3
Cross-linking and labeling of the Escherichia coli F1F0-ATP synthase reveal a compact hydrophilic portion of F0 close to an F1 catalytic subunit.
J Biol Chem. 1983 Dec 10;258(23):14599-609.
4
ATP synthetase (F1F0) of Escherichia coli K-12. High-yield preparation of functional F0 by hydrophobic affinity chromatography.
Eur J Biochem. 1982 Aug;126(1):149-53. doi: 10.1111/j.1432-1033.1982.tb06759.x.
5
All three subunits are required for the reconstitution of an active proton channel (F0) of Escherichia coli ATP synthase (F1F0).
EMBO J. 1985 Feb;4(2):515-8. doi: 10.1002/j.1460-2075.1985.tb03658.x.
6
Chemical modification of the F0 part of the ATP synthase (F1F0) from Escherichia coli. Effects on proton conduction and F1 binding.
Eur J Biochem. 1984 Feb 1;138(3):617-22. doi: 10.1111/j.1432-1033.1984.tb07959.x.
7
The DCCD-reactive aspartyl-residue of subunit C from the Escherichia coli ATP-synthase is important for the conformation of F0.
Biochem Biophys Res Commun. 1984 Apr 30;120(2):527-33. doi: 10.1016/0006-291x(84)91286-5.
8
Purification and reconstitution into proteoliposomes of the F1F0 ATP synthase from the obligately anaerobic gram-positive bacterium Clostridium thermoautotrophicum.
J Bacteriol. 1997 Mar;179(5):1714-20. doi: 10.1128/jb.179.5.1714-1720.1997.
9
Subunits coupling H+ transport and ATP synthesis in the Escherichia coli ATP synthase. Cys-Cys cross-linking of F1 subunit epsilon to the polar loop of F0 subunit c.
J Biol Chem. 1995 Oct 13;270(41):24609-14.
10
Role of the delta subunit in enhancing proton conduction through the F0 of the Escherichia coli F1F0 ATPase.
J Bacteriol. 1994 Mar;176(5):1383-9. doi: 10.1128/jb.176.5.1383-1389.1994.
引用本文的文献
1
ATP Synthase Diseases of Mitochondrial Genetic Origin.
Front Physiol. 2018 Apr 4;9:329. doi: 10.3389/fphys.2018.00329. eCollection 2018.
2
Subunit δ is the key player for assembly of the H(+)-translocating unit of Escherichia coli F(O)F1 ATP synthase.
J Biol Chem. 2013 Sep 6;288(36):25880-25894. doi: 10.1074/jbc.M113.484675. Epub 2013 Jul 17.
3
Genetic characterization of optochin-susceptible viridans group streptococci.
Antimicrob Agents Chemother. 2003 Oct;47(10):3187-94. doi: 10.1128/AAC.47.10.3187-3194.2003.
4
The structural and functional connection between the catalytic and proton translocating sectors of the mitochondrial F1F0-ATP synthase.
J Bioenerg Biomembr. 2000 Aug;32(4):401-11. doi: 10.1023/a:1005584221456.
5
Subunit organization of the stator part of the F0 complex from Escherichia coli ATP synthase.
J Bioenerg Biomembr. 2000 Aug;32(4):357-64. doi: 10.1023/a:1005523902800.
6
Role of the delta subunit in enhancing proton conduction through the F0 of the Escherichia coli F1F0 ATPase.
J Bacteriol. 1994 Mar;176(5):1383-9. doi: 10.1128/jb.176.5.1383-1389.1994.
7
The F0 complex of the ATP synthase of Escherichia coli contains a proton pathway with large proton polarizability caused by collective proton fluctuation.
Biophys J. 1995 Jan;68(1):104-10. doi: 10.1016/S0006-3495(95)80164-5.
8
Bacterial adenosine 5'-triphosphate synthase (F1F0): purification and reconstitution of F0 complexes and biochemical and functional characterization of their subunits.
Microbiol Rev. 1987 Dec;51(4):477-97. doi: 10.1128/mr.51.4.477-497.1987.
9
Proton conduction by subunit a of the membrane-bound ATP synthase of Escherichia coli revealed after induced overproduction.
EMBO J. 1985 Sep;4(9):2357-63. doi: 10.1002/j.1460-2075.1985.tb03939.x.
10
Effects of inducing expression of cloned genes for the F0 proton channel of the Escherichia coli F1F0 ATPase.
J Bacteriol. 1992 May;174(10):3370-6. doi: 10.1128/jb.174.10.3370-3376.1992.
本文引用的文献
1
Membrane integration and function of the three F0 subunits of the ATP synthase of Escherichia coli K12.
EMBO J. 1983;2(1):99-103. doi: 10.1002/j.1460-2075.1983.tb01388.x.
2
The topology of the proton translocating F0 component of the ATP synthase from E. coli K12: studies with proteases.
EMBO J. 1983;2(1):105-10. doi: 10.1002/j.1460-2075.1983.tb01389.x.
3
Delipidation of bacteriorhodopsin and reconstitution with exogenous phospholipid.
Proc Natl Acad Sci U S A. 1980 Jan;77(1):323-7. doi: 10.1073/pnas.77.1.323.
4
Stoichiometry of subunits in the H+-ATPase complex of Escherichia coli.
J Biol Chem. 1982 Feb 25;257(4):2009-15.
5
The proteolipid subunit of the chloroplast adenosine triphosphatase complex. Reconstitution and demonstration of proton-conductive properties.
J Biol Chem. 1980 Nov 25;255(22):10638-43.
6
Reconstitution of the purified proton conductor (F0) of the adenosine triphosphatase complex from Escherichia coli.
FEBS Lett. 1980 Jul 28;116(2):173-6. doi: 10.1016/0014-5793(80)80636-3.
7
Amino acid replacement in dicyclohexylcarbodiimide-reactive proteins from mutant strains of Escherichia coli defective in the energy-transducing ATPase complex.
FEBS Lett. 1980 May 5;113(2):265-70. doi: 10.1016/0014-5793(80)80606-5.
8
Chemical modification of the F0 part of the ATP synthase (F1F0) from Escherichia coli. Effects on proton conduction and F1 binding.
Eur J Biochem. 1984 Feb 1;138(3):617-22. doi: 10.1111/j.1432-1033.1984.tb07959.x.
9
Cross-linking and labeling of the Escherichia coli F1F0-ATP synthase reveal a compact hydrophilic portion of F0 close to an F1 catalytic subunit.
J Biol Chem. 1983 Dec 10;258(23):14599-609.
10
An Asp-Asn substitution in the proteolipid subunit of the ATP-synthase from Escherichia coli leads to a non-functional proton channel.
FEBS Lett. 1982 Aug 16;145(1):21-9. doi: 10.1016/0014-5793(82)81198-8.
Zotero 插件