Two ATPases

Overview

Journal J Biol Chem

Specialty Biochemistry

Date 2012 Jul 24

PMID 22822068

Citations 16

Authors

Alan E Senior

Affiliations

Soon will be listed here.

Abstract

In this article, I reflect on research on two ATPases. The first is F(1)F(0)-ATPase, also known as ATP synthase. It is the terminal enzyme in oxidative phosphorylation and famous as a nanomotor. Early work on mitochondrial enzyme involved purification in large amount, followed by deduction of subunit composition and stoichiometry and determination of molecular sizes of holoenzyme and individual subunits. Later work on Escherichia coli enzyme utilized mutagenesis and optical probes to reveal the molecular mechanism of ATP hydrolysis and detailed facets of catalysis. The second ATPase is P-glycoprotein, which confers multidrug resistance, notably to anticancer drugs, in mammalian cells. Purification of the protein in large quantity allowed detailed characterization of catalysis, formulation of an alternating sites mechanism, and recently, advances in structural characterization.

Citing Articles

Advances of medical nanorobots for future cancer treatments.

Kong X, Gao P, Wang J, Fang Y, Hwang K J Hematol Oncol. 2023; 16(1):74.

PMID: 37452423 PMC: 10347767. DOI: 10.1186/s13045-023-01463-z.

Frankenbacteriosis targeting interactions between pathogen and symbiont to control infection in the tick vector.

Mazuecos L, Alberdi P, Hernandez-Jarguin A, Contreras M, Villar M, Cabezas-Cruz A iScience. 2023; 26(5):106697.

PMID: 37168564 PMC: 10165458. DOI: 10.1016/j.isci.2023.106697.

Functional importance of αAsp-350 in the catalytic sites of Escherichia coli ATP synthase.

Raheem S, Steiner A, Ahmad Z Arch Biochem Biophys. 2019; 672:108050.

PMID: 31330132 PMC: 6718308. DOI: 10.1016/j.abb.2019.07.015.

Control of rotation of the FF-ATP synthase nanomotor by an inhibitory α-helix from unfolded ε or intrinsically disordered ζ and IF proteins.

Mendoza-Hoffmann F, Zarco-Zavala M, Ortega R, Garcia-Trejo J J Bioenerg Biomembr. 2018; 50(5):403-424.

PMID: 30267331 DOI: 10.1007/s10863-018-9773-9.

Understanding the link between antimicrobial properties of dietary olive phenolics and bacterial ATP synthase.

Amini A, Liu M, Ahmad Z Int J Biol Macromol. 2017; 101:153-164.

PMID: 28322962 PMC: 5884633. DOI: 10.1016/j.ijbiomac.2017.03.087.

References

Senior A . The structure of mitochondrial ATPase. Biochim Biophys Acta. 1973; 301(3):249-77. DOI: 10.1016/0304-4173(73)90006-2. View

Duncan T, Senior A . The defective proton-ATPase of uncD mutants of Escherichia coli. Two mutations which affect the catalytic mechanism. J Biol Chem. 1985; 260(8):4901-7. View

Urbatsch I, Gimi K, Senior A . Investigation of the role of glutamine-471 and glutamine-1114 in the two catalytic sites of P-glycoprotein. Biochemistry. 2000; 39(39):11921-7. DOI: 10.1021/bi001220s. View

Senior A, Muharemagic A, Wilke-Mounts S . Assembly of the stator in Escherichia coli ATP synthase. Complexation of alpha subunit with other F1 subunits is prerequisite for delta subunit binding to the N-terminal region of alpha. Biochemistry. 2006; 45(51):15893-902. PMC: 2548287. DOI: 10.1021/bi0619730. View

Hazard A, Senior A . Defective energy coupling in delta-subunit mutants of Escherichia coli F1F0-ATP synthase. J Biol Chem. 1994; 269(1):427-32. View

Lee J, Urbatsch I, Senior A, Wilkens S . Nucleotide-induced structural changes in P-glycoprotein observed by electron microscopy. J Biol Chem. 2007; 283(9):5769-79. DOI: 10.1074/jbc.M707028200. View

Senior A, Brooks J . Studies on the mitochondrial oligomycin-insensitivt ATPase. I. An improved method of purification and the behavior of the enzyme in solutions of various depolymerizing agents. Arch Biochem Biophys. 1970; 140(1):257-66. DOI: 10.1016/0003-9861(70)90030-5. View

Weber J, Grell E, Senior A . Tryptophan-free Escherichia coli F1-ATPase. Arch Biochem Biophys. 1994; 309(2):363-8. DOI: 10.1006/abbi.1994.1125. View

Weber J, Senior A . Bi-site catalysis in F1-ATPase: does it exist?. J Biol Chem. 2001; 276(38):35422-8. DOI: 10.1074/jbc.M104946200. View

10.

Urbatsch I, Sankaran B, Weber J, Senior A . P-glycoprotein is stably inhibited by vanadate-induced trapping of nucleotide at a single catalytic site. J Biol Chem. 1995; 270(33):19383-90. DOI: 10.1074/jbc.270.33.19383. View

11.

Ahmad Z, Senior A . Mutagenesis of residue betaArg-246 in the phosphate-binding subdomain of catalytic sites of Escherichia coli F1-ATPase. J Biol Chem. 2004; 279(30):31505-13. DOI: 10.1074/jbc.M404621200. View

12.

Weber J, Wilke-Mounts S, Nadanaciva S, Senior A . Quantitative determination of direct binding of b subunit to F1 in Escherichia coli F1F0-ATP synthase. J Biol Chem. 2004; 279(12):11253-8. DOI: 10.1074/jbc.M312576200. View

13.

Rao R, Senior A . The properties of hybrid F1-ATPase enzymes suggest that a cyclical catalytic mechanism involving three catalytic sites occurs. J Biol Chem. 1987; 262(36):17450-4. View

14.

Senior A . Characterization of the adenosine triphosphatase activity of Chinese hamster P-glycoprotein. J Biol Chem. 1993; 268(6):4197-206. View

15.

Weber J, Hammond S, Senior A . Tryptophan substitutions surrounding the nucleotide in catalytic sites of F1-ATPase. Biochemistry. 1998; 37(35):12042-50. DOI: 10.1021/bi981089c. View

16.

Weber J, Grell E, Senior A . Tryptophan fluorescence provides a direct probe of nucleotide binding in the noncatalytic sites of Escherichia coli F1-ATPase. J Biol Chem. 1994; 269(15):11261-8. View

17.

Weber J, Senior A . Catalytic mechanism of F1-ATPase. Biochim Biophys Acta. 1997; 1319(1):19-58. DOI: 10.1016/s0005-2728(96)00121-1. View

18.

Weber J, Senior A . Cooperativity and stoichiometry of substrate binding to the catalytic sites of Escherichia coli F1-ATPase. Effects of magnesium, inhibitors, and mutation. J Biol Chem. 1994; 269(32):20462-7. View

19.

Ahmad Z, Senior A . Involvement of ATP synthase residues alphaArg-376, betaArg-182, and betaLys-155 in Pi binding. FEBS Lett. 2005; 579(2):523-8. DOI: 10.1016/j.febslet.2004.12.022. View

20.

Shapiro A, Vinuela E, Maizel Jr J . Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels. Biochem Biophys Res Commun. 1967; 28(5):815-20. DOI: 10.1016/0006-291x(67)90391-9. View