Genomes and Genes
Gene Symbol: atpE
Description: F0 sector of membrane-bound ATP synthase, subunit c
Alias: ECK3730, JW3715, papH, uncE
Species: Escherichia coli str. K-12 substr. MG1655
- Monticello R, Angov E, Brusilow W. Effects of inducing expression of cloned genes for the F0 proton channel of the Escherichia coli F1F0 ATPase. J Bacteriol. 1992;174:3370-6 pubmed..Such induction did result in growth inhibition, but there was no correlation between growth inhibition and either increased membrane proton permeability or the presence of functional, reconstitutable F0. ..
- Groth G, Walker J. Model of the c-subunit oligomer in the membrane domain of F-ATPases. FEBS Lett. 1997;410:117-23 pubmed..The validity of the proposed arrangement of protomers in the dodecameric complex was tested by amino acid substitution analysis and chemical, biochemical and genetic data on subunit c. ..
- Grabar T, Cain B. Genetic complementation between mutant b subunits in F1F0 ATP synthase. J Biol Chem. 2004;279:31205-11 pubmed
- Greie J, Heitkamp T, Altendorf K. The transmembrane domain of subunit b of the Escherichia coli F1F(O) ATP synthase is sufficient for H(+)-translocating activity together with subunits a and c. Eur J Biochem. 2004;271:3036-42 pubmed..Furthermore, the data obtained functionally support the monomeric NMR structure of the synthetic b(1-34). ..
- Maeda M. ATP synthases: bioinformatic based insights into how their electrochemically driven motor comprised of subunits a and c might serve as a drug target. J Bioenerg Biomembr. 2008;40:117-21 pubmed publisher..Since there may be structural divergence even in well-conserved ATP synthases, the c subunit-ring as well as the a subunit in F0 could be targets for drugs for specific bacterial species. ..
- Borloo J, De Smet L, Vergauwen B, Van Beeumen J, Devreese B. A beta-galactosidase-based bacterial two-hybrid system to assess protein-protein interactions in the correct cellular environment. J Proteome Res. 2007;6:2587-95 pubmed..These benefits demonstrate the relevance of the method as a powerful new tool in the broad spectrum of interaction assessment methods. ..
- van Bloois E, Jan Haan G, de Gier J, Oudega B, Luirink J. F(1)F(0) ATP synthase subunit c is targeted by the SRP to YidC in the E. coli inner membrane. FEBS Lett. 2004;576:97-100 pubmed..The data suggest that F0c is targeted by the SRP to the membrane, where it inserts at YidC in a Sec-independent mechanism. F0c appears to be the first natural substrate of this novel pathway. ..
- Girvin M, Fillingame R. Determination of local protein structure by spin label difference 2D NMR: the region neighboring Asp61 of subunit c of the F1F0 ATP synthase. Biochemistry. 1995;34:1635-45 pubmed..The proximity of these residues had been predicted from mutant analyses, where H+ translocation was retained on moving the Asp from position 61 to 24. ..
- Wiedenmann A, Dimroth P, von Ballmoos C. Deltapsi and DeltapH are equivalent driving forces for proton transport through isolated F(0) complexes of ATP synthases. Biochim Biophys Acta. 2008;1777:1301-10 pubmed publisher..The new method is an ideal tool for detailed kinetic investigations of the ion transport mechanism of ATP synthases from various organisms. ..
- Dmitriev O, Fillingame R. The rigid connecting loop stabilizes hairpin folding of the two helices of the ATP synthase subunit c. Protein Sci. 2007;16:2118-22 pubmed..This experimental system may be useful for NMR studies of interactions between subunit c and subunits gamma and epsilon, which together form the rotor of the ATP synthase. ..
- Galkin M, Ishmukhametov R, Vik S. A functionally inactive, cold-stabilized form of the Escherichia coli F1Fo ATP synthase. Biochim Biophys Acta. 2006;1757:206-14 pubmed..The results suggest that thermohysteresis is a consequence of an inactive form of the enzyme that is stabilized by the binding of inhibitory Mg-ADP. ..
- Suzuki T, Ozaki Y, Sone N, Feniouk B, Yoshida M. The product of uncI gene in F1Fo-ATP synthase operon plays a chaperone-like role to assist c-ring assembly. Proc Natl Acad Sci U S A. 2007;104:20776-81 pubmed..Na(+) induced dissociation of His-tagged UncI protein from c(11)-ring but not from c-monomers. These results show that UncI is a chaperone-like protein that assists c(11)-ring assembly from c-monomers in the membrane. ..
- Wachter E, Schmid R, Deckers G, Altendorf K. Amino acid replacement in dicyclohexylcarbodiimide-reactive proteins from mutant strains of Escherichia coli defective in the energy-transducing ATPase complex. FEBS Lett. 1980;113:265-70 pubmed
- Schulenberg B, Aggeler R, Murray J, Capaldi R. The gammaepsilon-c subunit interface in the ATP synthase of Escherichia coli. cross-linking of the epsilon subunit to the c subunit ring does not impair enzyme function, that of gamma to c subunits leads to uncoupling. J Biol Chem. 1999;274:34233-7 pubmed..Blocking these structural changes by cross-linking leads to a proton leak within the F(0). ..
- Pedersen P, Ko Y, Hong S. ATP synthases in the year 2000: defining the different levels of mechanism and getting a grip on each. J Bioenerg Biomembr. 2000;32:423-32 pubmed..Nevertheless, in order to get a better grip in this new century on how ATP synthases make ATP and then release it, we must take on the difficult challenge of elucidating each of the three levels of mechanism. ..
- Gay N, Walker J. The atp operon: nucleotide sequence of the promoter and the genes for the membrane proteins, and the delta subunit of Escherichia coli ATP-synthase. Nucleic Acids Res. 1981;9:3919-26 pubmed..The three genes that follow are structural genes for proteins comprising the proton channel of the enzyme. The fifth gene codes for the delta-subunit of F(1)-ATPase. ..
- McCarthy J, Schairer H, Sebald W. Translational initiation frequency of atp genes from Escherichia coli: identification of an intercistronic sequence that enhances translation. EMBO J. 1985;4:519-26 pubmed
- Borsch M, Graber P. Subunit movement in individual H+-ATP synthases during ATP synthesis and hydrolysis revealed by fluorescence resonance energy transfer. Biochem Soc Trans. 2005;33:878-82 pubmed..After reconstitution into a liposome, this enzyme was able to catalyse ATP synthesis when the membrane was energized. ..
- Gogol E, Lücken U, Capaldi R. The stalk connecting the F1 and F0 domains of ATP synthase visualized by electron microscopy of unstained specimens. FEBS Lett. 1987;219:274-8 pubmed..The structures visualized in views normal to the lipid bilayer clearly show the presence of a narrow stalk approx. 45 A long, connecting the F1 to the membrane-embedded F0. ..
- Sengupta D, Rampioni A, Marrink S. Simulations of the c-subunit of ATP-synthase reveal helix rearrangements. Mol Membr Biol. 2009;26:422-34 pubmed publisher..The characterization of the monomer and ring presented in this work sheds light into the structural dynamics of the c-subunit and its functional relevance. ..
- Hellmuth K, Rex G, Surin B, Zinck R, McCarthy J. Translational coupling varying in efficiency between different pairs of genes in the central region of the atp operon of Escherichia coli. Mol Microbiol. 1991;5:813-24 pubmed..Five genes, atpE, atpF, atpH, atpA and atpG, were shown to be translationally coupled to various degrees of tightness...
- Vorburger T, Ebneter J, Wiedenmann A, Morger D, Weber G, Diederichs K, et al. Arginine-induced conformational change in the c-ring/a-subunit interface of ATP synthase. FEBS J. 2008;275:2137-50 pubmed publisher..This mechanism allows efficient interaction between subunit a and the c-ring and simultaneously allows almost frictionless movement against each other. ..
- Krebstakies T, Aldag I, Altendorf K, Greie J, Deckers Hebestreit G. The stoichiometry of subunit c of Escherichia coli ATP synthase is independent of its rate of synthesis. Biochemistry. 2008;47:6907-16 pubmed publisher..coli ATP synthase isolated from atp wildtype and mutant cells, the latter comprising a reduced expression of the atpE gene coding for subunit c due to a point mutation within its Shine-Dalgarno sequence, suggested a variable ..
- Kanazawa H, Mabuchi K, Kayano T, Tamura F, Futai M. Nucleotide sequence of genes coding for dicyclohexylcarbodiimide-binding protein and the alpha subunit of proton-translocating ATPase of Escherichia coli. Biochem Biophys Res Commun. 1981;100:219-25 pubmed
- Deckers Hebestreit G, Altendorf K. The Fo complex of the proton-translocating F-type ATPase of Escherichia coli. J Exp Biol. 1992;172:451-9 pubmed..Binding studies with a monoclonal antibody against this epitope are now under investigation to determine the orientation of subunit a.(ABSTRACT TRUNCATED AT 250 WORDS) ..
- Kobayashi M, Matsuki Y, Yumen I, Fujiwara T, Akutsu H. Signal assignment and secondary structure analysis of a uniformly [13C, 15N]-labeled membrane protein, H +-ATP synthase subunit c, by magic-angle spinning solid-state NMR. J Biomol NMR. 2006;36:279-93 pubmed
- Zhang Q, Atreya H, Kamen D, Girvin M, Szyperski T. GFT projection NMR based resonance assignment of membrane proteins: application to subunit C of E. coli F(1)F (0) ATP synthase in LPPG micelles. J Biomol NMR. 2008;40:157-63 pubmed publisher..It is shown that the 4D and 5D spectral information obtained rapidly from GFT and G(2)FT NMR experiments enables one to efficiently obtain (nearly) complete resonance assignments of membrane proteins. ..
- Fimmel A, Jans D, Langman L, James L, Ash G, Downie J, et al. The F1F0-ATPase of Escherichia coli. Substitution of proline by leucine at position 64 in the c-subunit causes loss of oxidative phosphorylation. Biochem J. 1983;213:451-8 pubmedThe uncE410 allele differs from the normal uncE gene in that C leads to T base changes occur at nucleotides 190 and 191, resulting in proline at position 64 in the c-subunit of the F1F0-ATPase being replaced by leucine...
- Dmitriev O, Altendorf K, Fillingame R. Subunit A of the E. coli ATP synthase: reconstitution and high resolution NMR with protein purified in a mixed polarity solvent. FEBS Lett. 2004;556:35-8 pubmed
- Gunsalus R, Brusilow W, Simoni R. Gene order and gene-polypeptide relationships of the proton-translocating ATPase operon (unc) of Escherichia coli. Proc Natl Acad Sci U S A. 1982;79:320-4 pubmed..This approach should be of use for study of other multigene bacterial operons, especially those with genes coding for polypeptides with unknown or unmeasurable catalytic activity. ..
- Walker J, Gay N, Saraste M, Eberle A. DNA sequence around the Escherichia coli unc operon. Completion of the sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and phoS. Biochem J. 1984;224:799-815 pubmed..The glmS gene encoding the amidotransferase, glucosamine synthetase, has been identified by homology with glutamine 5-phosphoribosylpyrophosphate amidotransferase. ..
- Schemidt R, Hsu D, Deckers Hebestreit G, Altendorf K, Brusilow W. The effects of an atpE ribosome-binding site mutation on the stoichiometry of the c subunit in the F1F0 ATPase of Escherichia coli. Arch Biochem Biophys. 1995;323:423-8 pubmed..stoichiometry of the c subunit in the F0 sector of the Escherichia coli F1F0 ATPase is dependent upon the level of atpE gene expression...
- Ballhausen B, Altendorf K, Deckers Hebestreit G. Constant c10 ring stoichiometry in the Escherichia coli ATP synthase analyzed by cross-linking. J Bacteriol. 2009;191:2400-4 pubmed publisher..Independent of the carbon source used for growth and independent of the presence of other FoF1 subunits, an equal pattern of cross-link formation stopping at the formation of decamers was obtained. ..
- Nielsen J, Jørgensen B, van Meyenburg K, Hansen F. The promoters of the atp operon of Escherichia coli K12. Mol Gen Genet. 1984;193:64-71 pubmed..The atp operon transcription terminates at a site approximately 50 bp downstream from the atpC gene. ..
- Takahata M, Tamura T, Abe K, Mihara H, Kurokawa S, Yamamoto Y, et al. Selenite assimilation into formate dehydrogenase H depends on thioredoxin reductase in Escherichia coli. J Biochem. 2008;143:467-73 pubmed publisher..Our present study reports for the first time the physiological involvement of thioredoxin reductase in the reductive assimilation of selenite in E. coli. ..
- Norwood T, Crawford D, Steventon M, Driscoll P, Campbell I. Heteronuclear 1H-15N nuclear magnetic resonance studies of the c subunit of the Escherichia coli F1F0 ATP synthase: assignment and secondary structure. Biochemistry. 1992;31:6285-90 pubmed..This model is consistent with information about the molecular motion of the protein deduced from 15N-1H heteronuclear NOE data and observed pKa values of carboxylic acid groups. ..
- Nielsen J, Hansen F, Hoppe J, Friedl P, von Meyenburg K. The nucleotide sequence of the atp genes coding for the F0 subunits a, b, c and the F1 subunit delta of the membrane bound ATP synthase of Escherichia coli. Mol Gen Genet. 1981;184:33-9 pubmed..The precise start positions of the atpE (c), atpF (b), atpH (delta) and atpA (alpha) genes have been defined by comparison of the potential coding ..
- Düser M, Zarrabi N, Cipriano D, Ernst S, Glick G, Dunn S, et al. 36 degrees step size of proton-driven c-ring rotation in FoF1-ATP synthase. EMBO J. 2009;28:2689-96 pubmed publisher..Using single-molecule fluorescence resonance energy transfer, we provide the first experimental determination of a 36 degrees sequential stepping mode of the c-ring during ATP synthesis. ..
- Jiang W, Hermolin J, Fillingame R. The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10. Proc Natl Acad Sci U S A. 2001;98:4966-71 pubmed
- Jans D, Fimmel A, Langman L, James L, Downie J, Senior A, et al. Mutations in the uncE gene affecting assembly of the c-subunit of the adenosine triphosphatase of Escherichia coli. Biochem J. 1983;211:717-26 pubmed..of the uncE429 allele differed from normal in that a G leads to A base change occurred at nucleotide 68 of the uncE gene, resulting in glycine being replaced by aspartic acid at position 23 in the c-subunit...
- Ishmukhametov R, Pond J, Al Huqail A, Galkin M, Vik S. ATP synthesis without R210 of subunit a in the Escherichia coli ATP synthase. Biochim Biophys Acta. 2008;1777:32-8 pubmed..The results suggest that minimal requirements for proton translocation by the ATP synthase include a positive charge in subunit a and a weak interface between subunit a and oligomeric subunit c. ..
- Etzold C, Deckers Hebestreit G, Altendorf K. Turnover number of Escherichia coli F0F1 ATP synthase for ATP synthesis in membrane vesicles. Eur J Biochem. 1997;243:336-43 pubmed..Therefore, these studies demonstrate that the ATP synthase complex of E. coli has, with respect to maximum rates, the same capacity as the corresponding enzymes of eukaryotic organells. ..
- Kasimoglu E, Park S, Malek J, Tseng C, Gunsalus R. Transcriptional regulation of the proton-translocating ATPase (atpIBEFHAGDC) operon of Escherichia coli: control by cell growth rate. J Bacteriol. 1996;178:5563-7 pubmed..Together, these studies establish that synthesis of the F0F1 ATPase is not greatly varied by modulating atp operon transcription. ..
- Sielaff H, Rennekamp H, Wächter A, Xie H, Hilbers F, Feldbauer K, et al. Domain compliance and elastic power transmission in rotary F(O)F(1)-ATPase. Proc Natl Acad Sci U S A. 2008;105:17760-5 pubmed publisher..This elastic buffer smoothes the cooperation of the 2 stepping motors. It is located were needed, between the 2 sites where the power strokes in F(O) and F(1) are generated and consumed. ..
- Kobayashi M, Struts A, Fujiwara T, Brown M, Akutsu H. Fluid mechanical matching of H+-ATP synthase subunit c-ring with lipid membranes revealed by 2H solid-state NMR. Biophys J. 2008;94:4339-47 pubmed publisher..These findings may be important for the torque generation in the rotary catalytic mechanism of the F(1)F(o)-ATPse molecular motor. ..
- Kol S, Turrell B, de Keyzer J, van der Laan M, Nouwen N, Driessen A. YidC-mediated membrane insertion of assembly mutants of subunit c of the F1F0 ATPase. J Biol Chem. 2006;281:29762-8 pubmed..These data show that oligomerization is not essential for the stable YidC-dependent membrane insertion of F(0)c consistent with a function of YidC as a membrane protein insertase. ..
- Hoppe J, Schairer H, Sebald W. Identification of amino-acid substitutions in the proteolipid subunit of the ATP synthase from dicyclohexylcarbodiimide-resistant mutants of Escherichia coli. Eur J Biochem. 1980;112:17-24 pubmed..Its polypeptide chain would have to fold back to bring together these two residues separated by a segment of 32 residues. ..
- Rastogi V, Girvin M. Structural changes linked to proton translocation by subunit c of the ATP synthase. Nature. 1999;402:263-8 pubmed..Rotation of these subunits within F1 causes the catalytic conformational changes in the active sites of F1 that result in ATP synthesis. ..
- Fillingame R, Oldenburg M, Fraga D. Mutation of alanine 24 to serine in subunit c of the Escherichia coli F1F0-ATP synthase reduces reactivity of aspartyl 61 with dicyclohexylcarbodiimide. J Biol Chem. 1991;266:20934-9 pubmed..the FO was cloned from four independently isolated DCCD-resistant mutants, and the sequence of the subunit c gene (uncE) was determined. An Ala24 to serine (A24S) substitution was found in the subunit c gene of each mutant...
- Senior A. The proton-translocating ATPase of Escherichia coli. Annu Rev Biophys Biophys Chem. 1990;19:7-41 pubmed..Long-range conformational interaction between the H+ conduction machinery in F0 and the catalytic sites in F1 seems basic to energy coupling; a major future goal is to provide a realistic physical explanation to validate this concept. ..
- McCarthy J, Sebald W, Gross G, Lammers R. Enhancement of translational efficiency by the Escherichia coli atpE translational initiation region: its fusion with two human genes. Gene. 1986;41:201-6 pubmed..The addition of the 30-bp sequence, found immediately upstream of the E. coli atpE gene Shine-Dalgarno (SD) sequence, to the translational initiation regions of IL2 and INF beta increased the ..
- Mottamal M, Shen S, Guembe C, Krilov G. Solvation of transmembrane proteins by isotropic membrane mimetics: a molecular dynamics study. J Phys Chem B. 2007;111:11285-96 pubmed..This was particularly true for the deprotonated form of the protein and found to be linked to solvent stabilization of the charged Asp(61). ..
- Krebstakies T, Zimmermann B, Graber P, Altendorf K, Börsch M, Greie J. Both rotor and stator subunits are necessary for efficient binding of F1 to F0 in functionally assembled Escherichia coli ATP synthase. J Biol Chem. 2005;280:33338-45 pubmed..The subunit c ring plays a crucial role in the binding of F1 to F0, whereas subunit a does not contribute significantly. ..
- Foster D, Fillingame R. Stoichiometry of subunits in the H+-ATPase complex of Escherichia coli. J Biol Chem. 1982;257:2009-15 pubmed..The most surprising conclusion from this study is that there are 10 +/- 1 omega ("proteolipid") subunits in each F1F0 complex. This is considerably more than had been assumed previously. ..
- Aris J, Klionsky D, Simoni R. The Fo subunits of the Escherichia coli F1Fo-ATP synthase are sufficient to form a functional proton pore. J Biol Chem. 1985;260:11207-15 pubmed..J., Brusilow, W.S.A., and Simoni, R.D. (1983) J. Biol. Chem. 258, 10136-10143) and present evidence that the Fo subunits alone are sufficient to assemble a functional proton pore. ..
- Yi L, Celebi N, Chen M, Dalbey R. Sec/SRP requirements and energetics of membrane insertion of subunits a, b, and c of the Escherichia coli F1F0 ATP synthase. J Biol Chem. 2004;279:39260-7 pubmed..Taken together, the in vivo data suggest that subunits a and b are inserted by the Sec/SRP pathway with the help of YidC, and subunit c is integrated into the membrane by the novel YidC pathway. ..
- Jones P, Hermolin J, Jiang W, Fillingame R. Insights into the rotary catalytic mechanism of F0F1 ATP synthase from the cross-linking of subunits b and c in the Escherichia coli enzyme. J Biol Chem. 2000;275:31340-6 pubmed..These experiments provide a biochemical verification that the oligomeric c-ring can move with respect to the b-stator and provide further support for a rotary catalytic mechanism in the ATP synthase. ..
- Jones H, Brajkovich C, Gunsalus R. In vivo 5' terminus and length of the mRNA for the proton-translocating ATPase (unc) operon of Escherichia coli. J Bacteriol. 1983;155:1279-87 pubmed..The level of unc operon expression, as assayed with the unc promoter plasmid, did not significantly differ when cells bearing the plasmid were grown either aerobically or anaerobically. ..
- van der Laan M, Bechtluft P, Kol S, Nouwen N, Driessen A. F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesis. J Cell Biol. 2004;165:213-22 pubmed..In conclusion, a novel membrane protein insertion pathway in E. coli is described in which YidC plays an exclusive role. ..
- McCarthy J, Gerstel B, Surin B, Wiedemann U, Ziemke P. Differential gene expression from the Escherichia coli atp operon mediated by segmental differences in mRNA stability. Mol Microbiol. 1991;5:2447-58 pubmed..We discuss the implications of these results in terms of the pathway of mRNA degradation and of the role of mRNA stability in the control of gene expression. ..
- Pierson H, Uhlemann E, Dmitriev O. Interaction with monomeric subunit c drives insertion of ATP synthase subunit a into the membrane and primes a-c complex formation. J Biol Chem. 2011;286:38583-91 pubmed publisher..Correct assembly of the ATP synthase incorporating topologically correct fusion of subunits a and c validates using this model protein for high resolution structural studies of the ATP synthase proton channel. ..
- Saraste M, Gay N, Eberle A, Runswick M, Walker J. The atp operon: nucleotide sequence of the genes for the gamma, beta, and epsilon subunits of Escherichia coli ATP synthase. Nucleic Acids Res. 1981;9:5287-96 pubmed..The genes for the alpha and beta subunits have evolved from a common ancestor. ..
- Zimmermann B, Diez M, Zarrabi N, Graber P, Börsch M. Movements of the epsilon-subunit during catalysis and activation in single membrane-bound H(+)-ATP synthase. EMBO J. 2005;24:2053-63 pubmed..The three states of the inactive enzyme were unequally populated. We conclude that the active-inactive transition was associated with a conformational change of epsilon within the central stalk. ..
- Bulygin V, Duncan T, Cross R. Rotor/Stator interactions of the epsilon subunit in Escherichia coli ATP synthase and implications for enzyme regulation. J Biol Chem. 2004;279:35616-21 pubmed..Furthermore, the rate of beta-epsilon cross-linking is much faster than that indicated by previous studies, allowing for the possibility of a rapid response to regulatory signals. ..
- Dmitriev O, Fillingame R. Structure of Ala(20) --> Pro/Pro(64) --> Ala substituted subunit c of Escherichia coli ATP synthase in which the essential proline is switched between transmembrane helices. J Biol Chem. 2001;276:27449-54 pubmed..The prolinyl residue may introduce structural flexibility in this region of the protein, which may be necessary for the proposed movement of the alpha-helical segments during the course of the H(+) pumping catalytic cycle. ..
- Fillingame R, Angevine C, Dmitriev O. Mechanics of coupling proton movements to c-ring rotation in ATP synthase. FEBS Lett. 2003;555:29-34 pubmed..The concerted rotation of interacting helices in subunit a and subunit c is proposed to be the mechanical force driving rotation of the c-rotor, using a mechanism akin to meshed gears. ..