The F<sub>0</sub> Complex of the <i>Escherichia Coli</i> ATP Synthase
European Journal of BiochemistryPublished 1 May 1995Open access
Ralf Birkenhäger, Michael Hoppert, Gabriele Deckers‐Hebestreit, Frank Mayer, Karlheinz Altendorf
Citations131
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TL;DR
Simulations with models of the F0 and the ac complex revealed that the projections observed can be obtained by tilting and rotating a model in which subunit a and the two copies of subunit b are located outside the subunit c oligomer.
Abstract
Cholate‐solubilized F 0 complexes of the ATP synthase (F 0 F 1 ) from Escherichia coli were studied by application of conventional transmission electron microscopy and electron spectroscopic imaging (ESI) of negatively stained samples. Using the ESI mode, the structural organization of the F 0 complex (diameter of 7.5±0.5 nm) could be observed in more detail and defined projections could be distinguished. Projection A appears as a deltoid‐like structure with bilateral symmetry. Projection B has an overall trapezoidal shape with some similarity in shape to the letter W. Applying the ESI mode to the ac complex dissolved in cholate‐containing buffer, an elongated structure consisting of two intensity maxima could be observed. Simulations with models of the F 0 and the ac complex revealed that the projections observed can be obtained by tilting and rotating a model in which subunit α and the two copies of subunit b are located outside the subunit c oligomer. This view of structural organization was supported by results obtained with F 0 complexes decorated with monoclonal antibodies against subunits a, b or c.
Keywords
Biochemistry, Genetics and Molecular Biology
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Journal of Biological ChemistryFo portion of Escherichia coli H+-ATPase. Carboxyl-terminal region of the b subunit is essential for assembly of functional Fo.
49 Citations1988Michiyasu Takeyama, Takato Noumi +2 more
It is suggested that about 30 carboxyl-terminal amino acid residues of the b subunit are essential for formation of the F1-binding site and H+ pathway, and loss of two or more residues abolished both activities completely.
BiochemistryFluoroaluminum and fluoroberyllium nucleoside diphosphate complexes as probes of the enzymic mechanism of the mitochondrial F1-ATPase
48 Citations1991Jean Paul Issartel, Alain Dupuis +2 more
The mechanism by which fluoride and aluminum or beryllium in combination with ADP inhibit beef heart mitochondrial F1-ATPase was investigated and results are discussed in terms of a stochastic model in which the three cooperative catalytic sites of F1 function in interactive pairs.
Biochimica et Biophysica Acta (BBA) - BioenergeticsH+/ATP coupling ratio at the unmodulated CF0CF1-ATP synthase determined by proton flux measurements
48 Citations1996Stephan Berry, B. Rumberg
The investigations give evidence of a H + /ATP coupling ratio of four for the oxidized or unmodulated state of the ATP synthase being at par with the coupling ratio for the reduced or modulatedstate of the enzyme.
BiochemistryOrganization of the F0 sector of Escherichia coli proton-ATPase: the polar loop region of subunit c extends from the cytoplasmic face of the membrane
47 Citations1989Mark E. Girvin, Joe Hermolin +2 more
It is shown here that the "polar loop" lies on the F1 binding side of the membrane of the Escherichia coli H+-transporting ATP synthase sector, and the reversal of inhibition was specific to the antisubunit c serum.
Archives of Biochemistry and BiophysicsFunctional effects and cross-reactivity of antibody to purified subunit b (uncF protein) of Escherichia coli proton-ATPase
47 Citations1985David S. Perlin, Alan E. Senior
The results indicated that trypsin proteolysis of F1-depleted membranes resulted in the transient appearance of three fragments of subunit b that remained tightly bound to the membrane.
Journal of Biological ChemistryMutations in the conserved proline 43 residue of the uncE protein (subunit c) of Escherichia coli F1F0-ATPase alter the coupling of F1 to F0
46 Citations1989Michael J. Miller, Dean Fraga +2 more
The results indicate that the mutant F1F0-ATPases are defective in coupling ATP hydrolysis to H+ translocation and support the idea that Pro43, and neighboring conserved polar residues play an important role in the binding and functional coupling of F1 to F0.
Journal of Biological ChemistryTransmembrane helix-helix interactions in F0 suggested by suppressor mutations to Ala24–>Asp/Asp61–>Gly mutant of ATP synthase subunit.
45 Citations1994Dean Fraga, J Hermolin +1 more
The H+ transporting ATP synthase function of the Ala24-->Asp/Asp61-->Gly mutant is not optimal, and cells grow more slowly than wild type, and three third-site suppressor mutants with optimized function were isolated in this study.
Biochimica et Biophysica Acta (BBA) - BioenergeticsZero-length crosslinking between subunits σ and I of the H+-translocating ATPase of chloroplasts
44 Citations1992G. Beckers, Richard J. Berzborn +1 more
Treatment of thylakoids with EDC/Sulfo-NHS resulted in inhibition of photophosphorylation and CF 0 CF 1 -catalyzed ATP hydrolysis without affecting formation of a proton gradient related to phenazine methosulfate mediated cyclic electron transport.
European Journal of BiochemistryAccessibility of F<sub>0</sub> subunits from <i>Escherichia coli</i> ATP synthase
44 Citations1986Gabriele Deckers‐Hebestreit, Karlheinz Altendorf
In inside-out oriented membrane vesicles the binding avidities of both sets of antisera, against denatured and non-denatured subunits of F0, were similar in the presence as well as in the absence of the F1 part, and a higher membrane protein concentration was necessary for the same antibody binding as in F1-stripped vesicle.
Journal of BacteriologyEssential residues in the polar loop region of subunit c of Escherichia coli F1F0 ATP synthase defined by random oligonucleotide-primed mutagenesis
43 Citations1991Dean Fraga, Robert Fillingame
It is concluded that Arg-41 is essential in the function of the polar loop and that the ensemble of other conserved residues collectively maintain an optimal environment required for that function.
PubMedTorque generation by the flagellar rotary motor.
41 Citations1995Howard C. Berg
The structure and dynamics of the flagellar rotary motor are reviewed and the motor torque-speed relationship has been measured over a wide dynamic range.
Journal of Biological ChemistryArginine 41 of subunit c of Escherichia coli H(+)-ATP synthase is essential in binding and coupling of F1 to F0.
40 Citations1994Dean Fraga, J Hermolin +3 more
The uncoupled phenotype of the R41K mutant closely resembles that previously reported for the c Q42E mutant and the mutant genes were recombined into the chromosome using a novel method for the unc system.
Biochemical JournalThe first putative transmembrane helix of the 16 kDa proteolipid lines a pore in the Vo sector of the vacuolar H+-ATPase
37 Citations1995Phil Jones, Michael A. Harrison +3 more
Analysis of restored vacuolar H(+)-ATPase function showed that segment 1 residues sensitive to mutation to cysteine were clustered on a single face, but only if the segment was helical, which is consistent with a model in which the fluorescein maleimide-accessible face of helix I lines a pore at the centre of a hexameric complex formed by the proteolipid.
Journal of Biological ChemistryInfluence of subunit-specific antibodies on the activity of the F0 complex of the ATP synthase of Escherichia coli. I. Effects of subunit b-specific polyclonal antibodies.
37 Citations1992Gabriele Deckers‐Hebestreit, R D Simoni +1 more
The immunoblot analysis of truncated b' subunits different in length showed that the antigenic determinants are located in the carboxyl-terminal half of the polypeptide chain.
Proceedings of the National Academy of SciencesSecond-site revertants of an arginine-210 to lysine mutation in the a subunit of the F0F1-ATPase from Escherichia coli: implications for structure.
36 Citations1992Susan M. Howitt, G B Cox
Modifications of a previously proposed model for the transmembrane helices of the F0 portion of theF0F1-ATPase are suggested and the implications of these modifications for the mechanism of proton translocation are discussed.
European Journal of BiochemistryPrecise epitope mapping of monoclonal antibodies to the cytoplasmic side of the acetylcholine receptor α subunit
35 Citations1992Socrates J. Tzartos, Michael S. REMOUNDOS
The epitopes for twelve monoclonal antibodies against the cytoplasmic side of the acetylcholine receptor (AChR) alpha subunit were precisely mapped using over 300 continuously overlapping synthetic peptides attached on poly(ethylene) rods and should prove instructive in searches for VICE-alpha-like epitopes carrying autoantigens with potential involvement in myasthenia gravis.
Journal of Molecular BiologyQuaternary structure of the isolated restriction endonuclease endor · BglI from Bacillus globigii as revealed by electron microscopy
34 Citations1979Walther Johannssen, H. R. Schütte +2 more
A model of the enzyme particle was developed containing 20 identical, biologically active monomers of molecular weight around 61,000, arranged as a pentagonal dodecahedron, established decisively by interconversion of the different appearances of given particles in the expected way.
Journal of Biological ChemistryA mutation of the c subunit of the Escherichia coli proton-translocating ATPase that suppresses the effects of a mutant b subunit.
31 Citations1987Carol A. Kumamoto, R D Simoni
The characterization of a new mutation that partially suppresses the effects of the original b mutation is described, which causes the substitution of serine for alanine at position 62 of the c subunit.
Journal of BacteriologyMacromolecular organization of F1-ATPase isolated from Clostridium thermoaceticum as revealed by electron microscopy
31 Citations1986Frank Mayer, D. M. Ivey +1 more
Membrane vesicles and the F1-ATPase from Clostridium thermoaceticum were examined by electron microscopy and found to have an alpha 3 beta 3 gamma delta structure.
Biochimica et Biophysica Acta (BBA) - BioenergeticsOrientation of subunit c of the ATP synthase of Escherichia coli — a study with peptide-specific antibodies
30 Citations1990Michael Hensel, Gabriele Deckers‐Hebestreit +2 more
It is concluded that the hydrophilic region of subunit c of the ATP synthase from Escherichia coli obtained by cleavage with cyanogen bromide is exposed to the cytoplasmic side of the membrane.
FEBS LettersThe transmembrane topology of the α subunit from the ATPase in <i>Escherichia coli</i> analyzed by PhoA protein fusions
30 Citations1990Christian Bjørbæk, Vibeke Foërsom +1 more
The atpB gene encodes the α subunit of the H+‐ATPase of E. coli that has been analyzed by PhoA fusions and supports an eight transmembrane segment model that is consistent with the hydropathic profile.
Biochimica et Biophysica Acta (BBA) - BioenergeticsPrediction of transmembrane topology of F0 proteins from Escherichia coli F1F0 ATP synthase using variational and hydrophobic moment analyses
29 Citations1992Steven B. Vik, Nguyen N. Dao
Topographical models for the a- and c-subunits and for the F0 complex are proposed on the basis of Fourier analysis of sequence variation in the E. coli F1F0 ATP synthase indicates that the single transmembrane span of the b-subunit and the C-terminalspan of the c subunit each have a face in contact with membrane lipids.
European Journal of BiochemistryChemical modification of the F<sub>0</sub> part of the ATP synthase (F<sub>1</sub>F<sub>0</sub>) from <i>Escherichia coli</i>
28 Citations1984Karl Steffens, Erwin Schneider +3 more
It is concluded that carboxyl-groups, different from the dicyclohexylcarbodiimide-binding site, are involved in H+ translocation through F0 and, in part, in the functional binding of F1.
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