HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Bakhtiari, N. Articles by Mueller, D. M. Search for Related Content PubMed PubMed Citation Articles by Bakhtiari, N. Articles by Mueller, D. M. Social Bookmarking                      What's this?

J Biol Chem, Vol. 274, Issue 23, 16363-16369, June 4, 1999

Structure/Function of the -Barrel Domain of F₁-ATPase in the Yeast Saccharomyces cerevisiae

From the Department of Biochemistry and Molecular Biology, Chicago Medical School, North Chicago, Illinois 60064

The first 90 amino acids of the - and -subunits of mitochondrial F₁-ATPase are folded into -barrel domains and were postulated to be important for stabilizing the enzyme (Abrahams, J. P., Leslie, A. G., Lutter, R., and Walker, J. E. (1994) Nature 370, 621-628). The role of the domains was studied by making chimeric enzymes, replacing the domains from the yeast Saccharomyces cerevisiae enzyme with the corresponding domains from the enzyme of the thermophilic bacterium Bacillus PS3. The enzymes containing the chimeric -, -, or - and -subunits were not functional. However, gain-of-function mutations were obtained from the strain containing the enzyme with the chimeric PS3/yeast -subunit. The gain-of-function mutations were all in codons encoding the -barrel domain of the -subunit, and the residues appear to map out a region of subunit-subunit interactions. Gain-of-function mutations were also obtained that provided functional expression of the chimeric PS3/yeast - and -subunits together. Biochemical analysis of this active chimeric enzyme indicated that it was not significantly more thermostable or labile than the wild type. The results of this study indicate that the -barrel domains form critical contacts (distinct from those between the - and -subunits) that are important for the assembly of the ATP synthase.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				L. M. Iyer, K. S. Makarova, E. V. Koonin, and L. Aravind Comparative genomics of the FtsK-HerA superfamily of pumping ATPases: implications for the origins of chromosome segregation, cell division and viral capsid packaging Nucleic Acids Res., October 5, 2004; 32(17): 5260 - 5279. [Abstract] [Full Text] [PDF]

				G. Gruber, D. I. Svergun, J. Godovac-Zimmermann, W. R. Harvey, H. Wieczorek, and M. H. J. Koch Evidence for Major Structural Changes in the Manduca sexta Midgut V1 ATPase Due to Redox Modulation. A SMALL ANGLE X-RAY SCATTERING STUDY J. Biol. Chem., September 22, 2000; 275(39): 30082 - 30087. [Abstract] [Full Text] [PDF]

				Y. H. Ko, J. Hullihen, S. Hong, and P. L. Pedersen Mitochondrial F0F1 ATP Synthase. SUBUNIT REGIONS ON THE F1 MOTOR SHIELDED BY F0, FUNCTIONAL SIGNIFICANCE, AND EVIDENCE FOR AN INVOLVEMENT OF THE UNIQUE F0 SUBUNIT F6 J. Biol. Chem., October 13, 2000; 275(42): 32931 - 32939. [Abstract] [Full Text] [PDF]