Genomes and Genes
Gene Symbol: atpB
Description: F0 sector of membrane-bound ATP synthase, subunit a
Alias: ECK3731, JW3716, papD, uncB
Species: Escherichia coli str. K-12 substr. MG1655
- 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. ..
- Valiyaveetil F, Fillingame R. Transmembrane topography of subunit a in the Escherichia coli F1F0 ATP synthase. J Biol Chem. 1998;273:16241-7 pubmed..The positions of second site suppressors, including several isolated here to the nonfunctional E219C and H245C substitutions, provide support for the topographical model proposed. ..
- Moore K, Angevine C, Vincent O, Schwem B, Fillingame R. The cytoplasmic loops of subunit a of Escherichia coli ATP synthase may participate in the proton translocating mechanism. J Biol Chem. 2008;283:13044-52 pubmed publisher..We suggest that the Ag(+)-sensitive domain may be involved in gating H(+) release at the cytoplasmic side of the aqueous access channel extending through F(0). ..
- 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) ..
- Franklin M, Brusilow W, Woodbury D. Determination of proton flux and conductance at pH 6.8 through single FO sectors from Escherichia coli. Biophys J. 2004;87:3594-9 pubmed..We find that wild-type FO has a proton flux of 3100 +/- 500 H+/s/FO at a transmembrane potential of 106 mV (25 degrees C and pH 6.8). This corresponds to a proton conductance of 4.4 fS. ..
- Moore K, Fillingame R. Structural interactions between transmembrane helices 4 and 5 of subunit a and the subunit c ring of Escherichia coli ATP synthase. J Biol Chem. 2008;283:31726-35 pubmed publisher..We suggest that the pH-dependent conformational change may be related to the proposed role of aTMH5 in gating H+ access from the periplasm to the cAsp-61 residue in cTMH2. ..
- Angevine C, Herold K, Fillingame R. Aqueous access pathways in subunit a of rotary ATP synthase extend to both sides of the membrane. Proc Natl Acad Sci U S A. 2003;100:13179-83 pubmed..The aqueous access pathways at the interior of subunit a may be gated by a swiveling of helices in this bundle, alternately exposing cytoplasmic and periplasmic half channels to cAsp-61 during the H+ transport cycle. ..
- DeLeon Rangel J, Ishmukhametov R, Jiang W, Fillingame R, Vik S. Interactions between subunits a and b in the rotary ATP synthase as determined by cross-linking. FEBS Lett. 2013;587:892-7 pubmed publisher..These experiments help to define the juxtaposition of subunits b and a in the ATP synthase. ..
- 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..F1F0 ATPase is sufficient to cause membrane proton permeability, plasmids carrying different combinations of the uncB, E, and F genes, encoding the a, c, and b subunits of the F0 sector, cloned behind the inducible lac promoter in ..
- Cain B, Simoni R. Impaired proton conductivity resulting from mutations in the a subunit of F1F0 ATPase in Escherichia coli. J Biol Chem. 1986;261:10043-50 pubmedMutations in the uncB gene which encodes the a subunit of F1F0-ATPase in Escherichia coli were isolated and characterized. Eight mutations caused premature polypeptide chain termination...
- von Meyenburg K, Jørgensen B, Nielsen J, Hansen F. Promoters of the atp operon coding for the membrane-bound ATP synthase of Escherichia coli mapped by Tn10 insertion mutations. Mol Gen Genet. 1982;188:240-8 pubmed
- Trchounian A. Escherichia coli proton-translocating F0F1-ATP synthase and its association with solute secondary transporters and/or enzymes of anaerobic oxidation-reduction under fermentation. Biochem Biophys Res Commun. 2004;315:1051-7 pubmed..These associations can result from a protein-protein interaction by dithiol-disulfide interchange. In such associations F0F1 has novel functions in bacterial cell physiology. ..
- Düser M, Bi Y, Zarrabi N, Dunn S, Börsch M. The proton-translocating a subunit of F0F1-ATP synthase is allocated asymmetrically to the peripheral stalk. J Biol Chem. 2008;283:33602-10 pubmed publisher..This relationship provides stability to the membrane interface between a and b2, allowing it to withstand the torque imparted by the rotor during ATP synthesis as well as ATP hydrolysis. ..
- 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. ..
- Del Rizzo P, Bi Y, Dunn S. ATP synthase b subunit dimerization domain: a right-handed coiled coil with offset helices. J Mol Biol. 2006;364:735-46 pubmed..The results indicate a right-handed coiled-coil structure with intrinsic asymmetry, the two helices being offset rather than in register. A function for the right-handed coiled coil in rotational catalysis is proposed. ..
- Yi L, Jiang F, Chen M, Cain B, Bolhuis A, Dalbey R. YidC is strictly required for membrane insertion of subunits a and c of the F(1)F(0)ATP synthase and SecE of the SecYEG translocase. Biochemistry. 2003;42:10537-44 pubmed
- Bae L, Vik S. A more robust version of the Arginine 210-switched mutant in subunit a of the Escherichia coli ATP synthase. Biochim Biophys Acta. 2009;1787:1129-34 pubmed publisher..This same unusual result was observed in the triple mutant background, P204T/R210Q/Q252R, suggesting that the Arginine-switched mutants are using the normal proton pathway from the periplasm. ..
- Angevine C, Fillingame R. Aqueous access channels in subunit a of rotary ATP synthase. J Biol Chem. 2003;278:6066-74 pubmed..Residues 215 and 218 on TMH4, as well as residue 245 on TMH5, are Ag(+)-accessible but N-ethylmaleimide-inaccessible and may form part of an aqueous pocket extending from Asp(61) of subunit c to the periplasmic surface. ..
- Long J, Wang S, Vik S. Membrane topology of subunit a of the F1F0 ATP synthase as determined by labeling of unique cysteine residues. J Biol Chem. 1998;273:16235-40 pubmed..On the basis of these and earlier results, a transmembrane topology for the subunit a is proposed. ..
- Hsu D, Brusilow W. Effects of the uncI gene on expression of uncB, the gene coding for the a subunit of the F1F0 ATPase of Escherichia coli. FEBS Lett. 1995;371:127-31 pubmed..to measure gene expression in vivo, we tested the effects of deleting uncI on the expression of the adjacent gene uncB, which codes for the a subunit of the F0 sector of the ATPase...
- Bann J, Frieden C. Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR. Biochemistry. 2004;43:13775-86 pubmedThe folding of the two-domain bacterial chaperone PapD has been studied to develop an understanding of the relationship between individual domain folding and the formation of domain-domain interactions...
- Vik S, Ishmukhametov R. Structure and function of subunit a of the ATP synthase of Escherichia coli. J Bioenerg Biomembr. 2005;37:445-9 pubmed..Use of a chemical protease reagent, 5-(-bromoacetamido)-1,10-phenanthroline-copper, has indicated that the periplasmic end of transmembrane helix 5 is near that of transmembrane helix 2. ..
- Schwem B, Fillingame R. Cross-linking between helices within subunit a of Escherichia coli ATP synthase defines the transmembrane packing of a four-helix bundle. J Biol Chem. 2006;281:37861-7 pubmed..Other key residues in TMHs 2, 4, and 5, which were concluded previously to compose a possible aqueous access pathway from the periplasm, were found to locate to the inside of the four-helix bundle. ..
- 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). ..
- Kanazawa H, Mabuchi K, Kayano T, Noumi T, Sekiya T, Futai M. Nucleotide sequence of the genes for F0 components of the proton-translocating ATPase from Escherichia coli: prediction of the primary structure of F0 subunits. Biochem Biophys Res Commun. 1981;103:613-20 pubmed
- Grabar T, Cain B. Genetic complementation between mutant b subunits in F1F0 ATP synthase. J Biol Chem. 2004;279:31205-11 pubmed
- Steed P, Fillingame R. Subunit a facilitates aqueous access to a membrane-embedded region of subunit c in Escherichia coli F1F0 ATP synthase. J Biol Chem. 2008;283:12365-72 pubmed publisher..The results described here provide further evidence for an aqueous-accessible region at the interface of subunits a and c extending from the middle of the membrane to the cytoplasm. ..
- Yamada H, Moriyama Y, Maeda M, Futai M. Transmembrane topology of Escherichia coli H(+)-ATPase (ATP synthase) subunit a. FEBS Lett. 1996;390:34-8 pubmed..5%) or by sonication. These results suggest that at least parts of the three peptide segments of subunit a face the cytoplasm. Based on these observations, we propose a novel transmembrane topology of subunit a. ..
- Stalz W, Greie J, Deckers Hebestreit G, Altendorf K. Direct interaction of subunits a and b of the F0 complex of Escherichia coli ATP synthase by forming an ab2 subcomplex. J Biol Chem. 2003;278:27068-71 pubmed..The interaction between subunits a and b, which has been shown to be stoichiometric and functional, is not triggered by any cross-linking reagent and therefore reflects subunit interactions occurring within the F0 complex in vivo. ..
- 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. ..
- 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. ..
- 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. ..
- 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. ..
- DeLeon Rangel J, Zhang D, Vik S. The role of transmembrane span 2 in the structure and function of subunit a of the ATP synthase from Escherichia coli. Arch Biochem Biophys. 2003;418:55-62 pubmed..In summary, the results support a model in which the amino-terminal, cytoplasmic end of the second transmembrane span has close contact with subunit b, while the carboxy-terminal, periplasmic end is important for proton translocation. ..
- Vik S, Lee D, Marshall P. Temperature-sensitive mutations at the carboxy terminus of the alpha subunit of the Escherichia coli F1F0 ATP synthase. J Bacteriol. 1991;173:4544-8 pubmed..Truncated forms of this subunit showed a temperature sensitivity phenotype. We conclude that the carboxy terminus of the a subunit is not involved directly with proton translocation but that it has an important structural role. ..
- Lee Y, DiGiuseppe P, Silhavy T, Hultgren S. P pilus assembly motif necessary for activation of the CpxRA pathway by PapE in Escherichia coli. J Bacteriol. 2004;186:4326-37 pubmed..Thus, the data presented in this study argue that PapE has features inherent in its structure or during its folding that act as specific inducers of Cpx signal transduction. ..
- Ziemke P, McCarthy J. The control of mRNA stability in Escherichia coli: manipulation of the degradation pathway of the polycistronic atp mRNA. Biochim Biophys Acta. 1992;1130:297-306 pubmed..The first two genes, atpI and atpB, are rapidly inactivated and degraded at the mRNA level. The remaining seven genes are more stable...
- 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. ..
- 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. ..
- Cain B, Simoni R. Proton translocation by the F1F0ATPase of Escherichia coli. Mutagenic analysis of the a subunit. J Biol Chem. 1989;264:3292-300 pubmedCassette site-directed mutagenesis was employed to generate mutations in the a subunit (uncB (a) gene) of F1F0ATP synthase...
- 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. ..
- Wada T, Long J, Zhang D, Vik S. A novel labeling approach supports the five-transmembrane model of subunit a of the Escherichia coli ATP synthase. J Biol Chem. 1999;274:17353-7 pubmed..These results provide a more detailed view of the transmembrane spans of subunit a and also provide a simple and reliable technique for detection of periplasmic regions of inner membrane proteins in E. coli. ..
- 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. ..
- Steffen D, Schleif R. In vitro construction of plasmids which result in overproduction of the protein product of the araC gene of Escherichia coli. Mol Gen Genet. 1977;157:341-4 pubmed..coli fused to the araC gene of E. coli. E. coli possessing these plasmids contain about 50 times as much of the araC gene product as do cells with a wild-type araC gene and promotor. ..
- Pedersen P, Amzel L. ATP synthases. Structure, reaction center, mechanism, and regulation of one of nature's most unique machines. J Biol Chem. 1993;268:9937-40 pubmed
- 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. ..
- 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..vivo unc mRNA initiates with a guanine residue 73 bases before the start of the proposed gene 1 or 474 bases before uncB. An in vivo unc mRNA species of approximately 7,000 nucleotides in length which initiates in the unc promoter ..
- 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. ..
- 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. ..
- Lewis M, Chang J, Simoni R. A topological analysis of subunit alpha from Escherichia coli F1F0-ATP synthase predicts eight transmembrane segments. J Biol Chem. 1990;265:10541-50 pubmed..amino acid 271, the carboxyl-terminal residue, but not at amino acid 260, was able to complement the strain RH305 (uncB-) for growth on succinate and suggests the last 11 amino acids of the alpha subunit are critical to the function of ..
- 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..designated atpI, which codes for the N-terminal part of a 14 kD polypeptide, is located in front (upstream) of the atpB gene (the first structural gene in the atp operon), the other one codes for the C-terminal part of the gidB gene...
- Long J, DeLeon Rangel J, Vik S. Characterization of the first cytoplasmic loop of subunit a of the Escherichia coli ATP synthase by surface labeling, cross-linking, and mutagenesis. J Biol Chem. 2002;277:27288-93 pubmed
- Bjørbaek C, Foërsom V, Michelsen O. The transmembrane topology of the a [corrected] subunit from the ATPase in Escherichia coli analyzed by PhoA protein fusions. FEBS Lett. 1990;260:31-4 pubmedThe atpB encodes the a [corrected] subunit of the H(+)-ATPase of E. coli. The topology of this membrane protein has been analyzed by PhoA fusions...
- 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. ..
- Angevine C, Herold K, Vincent O, Fillingame R. Aqueous access pathways in ATP synthase subunit a. Reactivity of cysteine substituted into transmembrane helices 1, 3, and 5. J Biol Chem. 2007;282:9001-7 pubmed..Further, aqueous access between cAsp-61 and the cytoplasmic surface is likely to be mediated by residues in TMH4 and TMH5 at the exterior of the four-helix bundle that are in contact with the c-ring. ..
- 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. ..
- 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. ..
- Kumamoto C, Simoni R. Genetic evidence for interaction between the a and b subunits of the F0 portion of the Escherichia coli proton translocating ATPase. J Biol Chem. 1986;261:10037-42 pubmed..The suppressor mutations cause amino acid substitutions at position 240 of the a subunit. Membranes derived from strains carrying a suppressor mutation and the basp9 mutation exhibited ATP-dependent proton translocating activity. ..
- Dmitriev O, Abildgaard F, Markley J, Fillingame R. Backbone 1H, 15N and 13C assignments for the subunit a of the E. coli ATP synthase. J Biomol NMR. 2004;29:439-40 pubmed..The protein was found to consist of multiple elongated alpha-helical segments. This finding is generally consistent with previous predictions of multiple transmembrane alpha-helices in this polytopic protein. ..
- 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. ..
- von Ballmoos C, Brunner J, Dimroth P. The ion channel of F-ATP synthase is the target of toxic organotin compounds. Proc Natl Acad Sci U S A. 2004;101:11239-44 pubmed..Taken together these results indicate that the subunit a ion channel is the target site for ATPase inhibition by toxic organotin compounds. An inhibitor interacting specifically with this site has not been reported previously. ..
- Arechaga I, Miroux B, Runswick M, Walker J. Over-expression of Escherichia coli F1F(o)-ATPase subunit a is inhibited by instability of the uncB gene transcript. FEBS Lett. 2003;547:97-100 pubmed..All of them but uncB (subunit a) were expressed separately at very high levels in the bacterial hosts Escherichia coli C41(DE3) and C43(..
- McLachlin D, Coveny A, Clark S, Dunn S. Site-directed cross-linking of b to the alpha, beta, and a subunits of the Escherichia coli ATP synthase. J Biol Chem. 2000;275:17571-7 pubmed
- 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. ..
- 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 genes are expressed in the counterclockwise direction. Their order (counterclockwise) is: atpB (a), atpE (c), atpF (b), atpH (delta) and atpA(alpha)...