Rotary F1-ATPase. Is the C-terminus of subunit gamma fixed or mobile?

European Journal of Biochemistry
Martin MüllerO Pänke

Abstract

F-ATP synthase synthesizes ATP at the expense of ion motive force by a rotary coupling mechanism. A central shaft, subunit gamma, functionally connects the ion-driven rotary motor, F(O), with the rotary chemical reactor, F(1). Using polarized spectrophotometry we have demonstrated previously the functional rotation of the C-terminal alpha-helical portion of gamma in the supposed 'hydrophobic bearing' formed by the (alpha beta)(3) hexagon. In apparent contradiction with these spectroscopic results, an engineered disulfide bridge between the alpha-helix of gamma and subunit alpha did not impair enzyme activity. Molecular dynamics simulations revealed the possibility of a 'functional unwinding' of the alpha-helix to form a swivel joint. Furthermore, they suggested a firm clamping of that part of gamma even without the engineered cross-link, i.e. in the wild-type enzyme. Here, we rechecked the rotational mobility of the C-terminal portion of gamma relative to (alpha beta)(3). Non-fluorescent, engineered F(1) (alpha P280C/gamma A285C) was oxidized to form a (nonfluorescent) alpha gamma heterodimer. In a second mutant, containing just the point mutation within alpha, all subunits were labelled with a fluorescent dye. Following disass...Continue Reading

References

May 1, 1977·Analytical Biochemistry·J J Sedmak, S E Grossberg
Mar 1, 1978·Analytical Biochemistry·D LeBelA R Beaudoin
Nov 21, 1995·Proceedings of the National Academy of Sciences of the United States of America·T M DuncanR L Cross
Jun 13, 1996·Nature·D SabbertW Junge
Jul 9, 1996·Proceedings of the National Academy of Sciences of the United States of America·M J van RaaijJ E Walker
Sep 3, 1996·Proceedings of the National Academy of Sciences of the United States of America·J P AbrahamsJ E Walker
Mar 20, 1997·Nature·H NojiK Kinosita
Apr 29, 1997·Proceedings of the National Academy of Sciences of the United States of America·D SabbertW Junge
Mar 18, 1997·Proceedings of the National Academy of Sciences of the United States of America·D Sabbert, W Junge
Jan 1, 1997·Annual Review of Biochemistry·P D Boyer
Oct 10, 1997·FEBS Letters·S Engelbrecht, W Junge
Jul 8, 1999·Proceedings of the National Academy of Sciences of the United States of America·H OmoteM Futai
Jul 15, 1999·Biochemical and Biophysical Research Communications·H NojiS Engelbrecht
Nov 27, 1999·Science·D StockJ E Walker
Nov 18, 2000·The Journal of Biological Chemistry·H Noji, M Yoshida
Dec 15, 2000·Current Opinion in Structural Biology·D StockJ E Walker
Sep 5, 2001·FEBS Letters·W JungeS Engelbrecht
Sep 5, 2001·The Journal of Biological Chemistry·K GumbiowskiS Engelbrecht
Mar 15, 2002·Trends in Biochemical Sciences·Roderick A Capaldi, Robert Aggeler
Apr 20, 2002·The Journal of Biological Chemistry·Martin MüllerSiegfried Engelbrecht
May 9, 2002·Biochimica Et Biophysica Acta·Alan E SeniorJoachim Weber

❮ Previous
Next ❯

Citations

May 24, 2011·Nature Structural & Molecular Biology·Gino Cingolani, Thomas M Duncan
Aug 19, 2007·Proceedings of the National Academy of Sciences of the United States of America·Jonathan R GledhillJohn E Walker
Jan 25, 2008·Proceedings of the National Academy of Sciences of the United States of America·Jingzhi Pu, Martin Karplus
Nov 13, 2008·Proceedings of the National Academy of Sciences of the United States of America·Hendrik SielaffWolfgang Junge
Aug 30, 2008·Biophysical Journal·Hendrik SielaffWolfgang Junge
May 22, 2009·Nature·Wolfgang JungeSiegfried Engelbrecht
Apr 21, 2017·Biophysics Reviews·Hiroyuki NojiDuncan G G McMillan
Mar 11, 2008·Journal of Molecular Biology·Elke A DianChristian Motz

❮ Previous
Next ❯

Related Concepts

Related Feeds

ATP Synthases

ATP synthases are enzymes located in the inner mitochondrial membrane that catalyze the synthesis of ATP during cellular respiration. Discover the latest research on ATP synthases here.