| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 264, Issue 12, 6797-6803, 04, 1989
D Fraga and RH Fillingame
The uncE114 mutation (Gln42----Glu) in subunit c of the Escherichia coli H+
ATP synthetase causes uncoupling of proton translocation from ATP
hydrolysis (Mosher, M. E., White, L. K., Hermolin, J., and Fillingame, R.
H. (1985) J. Biol. Chem. 260, 4807-4814). In the background of strain ER,
the mutation led to dissociation of F1 from the membrane. Ten revertants to
the uncE114 mutation were isolated, and the uncE gene was cloned and
sequenced. Six of the revertants were intragenic and had substitutions of
glycine, alanine, or valine for the mutant glutamate residue at position
42. The intragenic, revertant uncE genes were incorporated into an
otherwise wild type chromosome of strain ER. Membrane vesicles prepared
from each of the revertants showed a restoration of F1 binding to F0. The
Val42 revertant differed from the other two revertants in that the ATPase
activity of F1 was inhibited when membrane bound. This was shown by the
stimulation of ATPase activity when F1 was released from the membrane. The
Gly42 and Ala42 revertants demonstrated membrane ATPase activity that was
resistant to dicyclohexylcarbodiimide treatment. Resistance was shown to be
due to the increased dissociation of F1 from the membrane under ATPase
assay conditions. The Ala42 revertant showed a significant reduction in
ATP-dependent quenching of quinacrine fluorescence that was attributed to
less efficient coupling of ATP hydrolysis to H+ translocation, whereas the
other revertants showed responses very near to that of wild type. Minor
changes in the F1-F0 interaction in all three revertants were indicated by
an increase in H+ leakiness, as judged by reduced NADH-dependent quenching
of quinacrine fluorescence. The minor defects in the revertants support the
idea that residue 42 is involved in the binding and coupling of F1 to F0
but also show that the conserved glutamine (or asparagine) is not
absolutely necessary in this function.
Conserved polar loop region of Escherichia coli subunit c of the F1F0 H+-ATPase. Glutamine 42 is not absolutely essential, but substitutions alter binding and coupling of F1 to F0
Department of Physiological Chemistry, University of Wisconsin Medical School, Madison 53706.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  O. D. Vincent, B. E. Schwem, P. R. Steed, W. Jiang, and R. H. Fillingame Fluidity of Structure and Swiveling of Helices in the Subunit c Ring of Escherichia coli ATP Synthase as Revealed by Cysteine-Cysteine Cross-Linking J. Biol. Chem., November 16, 2007; 282(46): 33788 - 33794. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. M. Angevine and R. H. Fillingame Aqueous Access Channels in Subunit a of Rotary ATP Synthase J. Biol. Chem., February 14, 2003; 278(8): 6066 - 6074. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 P. C. Jones Introduction of a Carboxyl Group in the First Transmembrane Helix of Escherichia coli F1Fo ATPase Subunit c and Cytoplasmic pH Regulation J. Bacteriol., March 1, 2001; 183(5): 1524 - 1530. [Abstract] [Full Text]
|
|
|
|
|
|
P. C. Jones, J. Hermolin, and R. H. Fillingame Mutations in Single Hairpin Units of Genetically Fused Subunit c Provide Support for a Rotary Catalytic Mechanism in F0F1 ATP Synthase J. Biol. Chem., April 6, 2000; 275(15): 11355 - 11360. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. J. Ketchum and R. K. Nakamoto A Mutation in the Escherichia coli F0F1-ATP Synthase Rotor, gamma E208K, Perturbs Conformational Coupling between Transport and Catalysis J. Biol. Chem., August 28, 1998; 273(35): 22292 - 22297. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
P. C. Jones, W. Jiang, and R. H. Fillingame Arrangement of the Multicopy H+-translocating Subunit c in the Membrane Sector of the Escherichia coli F1F0 ATP Synthase J. Biol. Chem., July 3, 1998; 273(27): 17178 - 17185. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
F. I. Valiyaveetil and R. H. Fillingame Transmembrane Topography of Subunit a in the Escherichia coli F1F0 ATP Synthase J. Biol. Chem., June 26, 1998; 273(26): 16241 - 16247. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 W. Jiang and R. H. Fillingame Interacting helical faces of subunits a and c in the F1Fo ATP synthase of Escherichia coli defined by disulfide cross-linking PNAS, June 9, 1998; 95(12): 6607 - 6612. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. D. Dunn and J. Chandler Characterization of a b2delta Complex from Escherichia coli ATP Synthase J. Biol. Chem., April 10, 1998; 273(15): 8646 - 8651. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
F. I. Valiyaveetil and R. H. Fillingame On the Role of Arg-210 and Glu-219 of Subunit a in Proton Translocation by the Escherichia coli F0F1-ATP Synthase J. Biol. Chem., December 19, 1997; 272(51): 32635 - 32641. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. D. Watts and R. A. Capaldi Interactions between the F1 and F0 Parts in the Escherichia coli ATP Synthase. ASSOCIATIONS INVOLVING THE LOOP REGION OF C SUBUNITS J. Biol. Chem., June 13, 1997; 272(24): 15065 - 15068. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. K. Al-Shawi, C. J. Ketchum, and R. K. Nakamoto Energy Coupling, Turnover, and Stability of the F0F1 ATP Synthase Are Dependent on the Energy of Interaction between gamma and beta Subunits J. Biol. Chem., January 24, 1997; 272(4): 2300 - 2306. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
P. C. Jones, J. Hermolin, W. Jiang, and R. H. Fillingame 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., September 29, 2000; 275(40): 31340 - 31346. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
