JBC Origene Your Gene Company

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Sorgen, P. L.
Right arrow Articles by Cain, B. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sorgen, P. L.
Right arrow Articles by Cain, B. D.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J Biol Chem, Vol. 273, Issue 43, 27873-27878, October 23, 1998

Deletions in the Second Stalk of F1F0-ATP Synthase in Escherichia coli

Paul L. Sorgen, Tamara L. Caviston, Regina C. Perry, and Brian D. Cain

From the Department of Biochemistry and Molecular Biology, University of Florida, Gainesville, Florida 32610

In Escherichia coli F1F0-ATP synthase, the two b subunits form the second stalk spanning the distance between the membrane F0 sector and the bulk of F1. Current models predict that the stator should be relatively rigid and engaged in contact with F1 at fixed points. To test this hypothesis, we constructed a series of deletion mutations in the uncF(b) gene to remove segments from the middle of the second stalk of the subunit. Mutants with deletions of 7 amino acids were essentially normal, and those with deletions of up to 11 amino acids retained considerable activity. Membranes prepared from these strains had readily detectable levels of F1-ATPase activity and proton pumping activity. Removal of 12 or more amino acids resulted in loss of oxidative phosphorylation. Levels of membrane-associated F1-ATPase dropped precipitously for the longer deletions, and immunoblot analysis indicated that reductions in activity correlated with reduced levels of b subunit in the membranes. Assuming the likely alpha -helical conformation for this area of the b subunit, the 11-amino acid deletion would result in shortening the subunit by approximately 16 Å. Since these deletions did not prevent the b subunit from participating in productive interactions with F1, we suggest that the b subunit is not a rigid rodlike structure, but has an inherent flexibility compatible with a dynamic role in coupling.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Proc. Natl. Acad. Sci. USAHome page
H. Sielaff, H. Rennekamp, A. Wachter, H. Xie, F. Hilbers, K. Feldbauer, S. D. Dunn, S. Engelbrecht, and W. Junge
Domain compliance and elastic power transmission in rotary FOF1-ATPase
PNAS, November 18, 2008; 105(46): 17760 - 17765.
[Abstract] [Full Text] [PDF]

Home page
 Appl. Environ. Microbiol.Home page
Y. Zhu, M. A. Eiteman, R. Altman, and E. Altman
High Glycolytic Flux Improves Pyruvate Production by a Metabolically Engineered Escherichia coli Strain
Appl. Envir. Microbiol., November 1, 2008; 74(21): 6649 - 6655.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
T. Hornung, O. A. Volkov, T. M. A. Zaida, S. Delannoy, J. G. Wise, and P. D. Vogel
Structure of the Cytosolic Part of the Subunit b-Dimer of Escherichia coli F0F1-ATP Synthase
Biophys. J., June 15, 2008; 94(12): 5053 - 5064.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
J. R. Gledhill, M. G. Montgomery, A. G. W. Leslie, and J. E. Walker
Mechanism of inhibition of bovine F1-ATPase by resveratrol and related polyphenols
PNAS, August 21, 2007; 104(34): 13632 - 13637.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
S. B. Claggett, T. B. Grabar, S. D. Dunn, and B. D. Cain
Functional Incorporation of Chimeric b Subunits into F1Fo ATP Synthase
J. Bacteriol., August 1, 2007; 189(15): 5463 - 5471.
[Abstract] [Full Text] [PDF]

Home page
 J BiochemHome page
A. Poetsch, R. J. Berzborn, J. Heberle, T. A. Link, N. A. Dencher, and H. Seelert
Biophysics and Bioinformatics Reveal Structural Differences of the Two Peripheral Stalk Subunits in Chloroplast ATP Synthase
J. Biochem., March 1, 2007; 141(3): 411 - 420.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. J. Cipriano, K. S. Wood, Y. Bi, and S. D. Dunn
Mutations in the Dimerization Domain of the b Subunit from the Escherichia coli ATP synthase: DELETIONS DISRUPT FUNCTION BUT NOT ENZYME ASSEMBLY
J. Biol. Chem., May 5, 2006; 281(18): 12408 - 12413.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Liu, M. Tarsio, C. M. H. Charsky, and P. M. Kane
Structural and Functional Separation of the N- and C-terminal Domains of the Yeast V-ATPase Subunit H
J. Biol. Chem., November 4, 2005; 280(44): 36978 - 36985.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. Inoue and M. Forgac
Cysteine-mediated Cross-linking Indicates That Subunit C of the V-ATPase Is in Close Proximity to Subunits E and G of the V1 Domain and Subunit a of the V0 Domain
J. Biol. Chem., July 29, 2005; 280(30): 27896 - 27903.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. Motz, T. Hornung, M. Kersten, D. T. McLachlin, S. D. Dunn, J. G. Wise, and P. D. Vogel
The Subunit b Dimer of the FoF1-ATP Synthase: INTERACTION WITH F1-ATPase AS DEDUCED BY SITE-SPECIFIC SPIN-LABELING
J. Biol. Chem., November 19, 2004; 279(47): 49074 - 49081.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. Fethiere, D. Venzke, M. Diepholz, A. Seybert, A. Geerlof, M. Gentzel, M. Wilm, and B. Bottcher
Building the Stator of the Yeast Vacuolar-ATPase: SPECIFIC INTERACTION BETWEEN SUBUNITS E AND G
J. Biol. Chem., September 24, 2004; 279(39): 40670 - 40676.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. B. Grabar and B. D. Cain
Genetic Complementation between Mutant b Subunits in F1F0 ATP Synthase
J. Biol. Chem., July 23, 2004; 279(30): 31205 - 31211.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. B. Grabar and B. D. Cain
Integration of b Subunits of Unequal Lengths into F1F0-ATP Synthase
J. Biol. Chem., September 12, 2003; 278(37): 34751 - 34756.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
T. B. Causey, S. Zhou, K. T. Shanmugam, and L. O. Ingram
Inaugural Article: Engineering the metabolism of Escherichia coli W3110 for the conversion of sugar to redox-neutral and oxidized products: Homoacetate production
PNAS, February 4, 2003; 100(3): 825 - 832.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
M. Revington, S. D. Dunn, and G. S. Shaw
Folding and stability of the b subunit of the F1F0 ATP synthase
Protein Sci., May 1, 2002; 11(5): 1227 - 1238.
[Abstract] [Full Text] [PDF]

Home page
 J. Exp. Biol.Home page
K Altendorf, W Stalz, J Greie, and G Deckers-Hebestreit
Structure and function of the F(o) complex of the ATP synthase from Escherichia coli
J. Exp. Biol., January 1, 2000; 203(1): 19 - 28.
[Abstract]

Home page
 J. Biol. Chem.Home page
P. L. Sorgen, M. R. Bubb, and B. D. Cain
Lengthening the Second Stalk of F1F0 ATP Synthase in Escherichia coli
J. Biol. Chem., December 17, 1999; 274(51): 36261 - 36266.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Revington, D. T. McLachlin, G. S. Shaw, and S. D. Dunn
The Dimerization Domain of the b Subunit of the Escherichia coli F1F0-ATPase
J. Biol. Chem., October 22, 1999; 274(43): 31094 - 31101.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
N. Bakhtiari, J. Lai-Zhang, B. Yao, and D. M. Mueller
Structure/Function of the beta -Barrel Domain of F1-ATPase in the Yeast Saccharomyces cerevisiae
J. Biol. Chem., June 4, 1999; 274(23): 16363 - 16369.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. T. McLachlin, A. M. Coveny, S. M. Clark, and S. D. Dunn
Site-directed Cross-linking of b to the alpha , beta , and a Subunits of the Escherichia coli ATP Synthase
J. Biol. Chem., June 2, 2000; 275(23): 17571 - 17577.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. M. H. Charsky, N. J. Schumann, and P. M. Kane
Mutational Analysis of Subunit G (Vma10p) of the Yeast Vacuolar H+-ATPase
J. Biol. Chem., November 17, 2000; 275(47): 37232 - 37239.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. Suzuki, J. Suzuki, N. Mitome, H. Ueno, and M. Yoshida
Second Stalk of ATP Synthase. CROSS-LINKING OF gamma SUBUNIT IN F1 TO TRUNCATED Fob SUBUNIT PREVENTS ATP HYDROLYSIS
J. Biol. Chem., November 22, 2000; 275(48): 37902 - 37906.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y. Arata, J. D. Baleja, and M. Forgac
Cysteine-directed Cross-linking to Subunit B Suggests That Subunit E Forms Part of the Peripheral Stalk of the Vacuolar H+-ATPase
J. Biol. Chem., January 25, 2002; 277(5): 3357 - 3363.
[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 
Copyright © 1998 by the American Society for Biochemistry and Molecular Biology.