Literature DB >> 2656299

Alpha 3 beta 3 complex of thermophilic ATP synthase. Catalysis without the gamma-subunit.

Y Kagawa1, S Ohta, Y Otawara-Hamamoto.   

Abstract

A complex of the alpha- and beta-subunits of thermophilic ATP synthase showed about 25% of the ATPase activity of the alpha beta gamma complex. The alpha 3 beta 3 hexamer structure was analyzed by sedimentation (11.2 S) and gel filtration (310 kDa). Dilution of the alpha beta complex caused dissociation of the complex and rapid loss of ATPase activity which was restored by addition of the gamma-subunit. A previous method using urea for isolating the subunits resulted in an alpha beta complex with lower activity than that prepared by over-expression of the genes. The alpha beta-ATP complex was formed from the alpha beta complex, ADP and Pi in the presence of dimethyl sulfoxide.

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Year:  1989        PMID： 2656299     DOI： 10.1016/0014-5793(89)80017-1

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  15 in total

1.  The gamma-subunit rotation and torque generation in F1-ATPase from wild-type or uncoupled mutant Escherichia coli.

Authors:  H Omote; N Sambonmatsu; K Saito; Y Sambongi; A Iwamoto-Kihara; T Yanagida; Y Wada; M Futai
Journal:  Proc Natl Acad Sci U S A       Date:  1999-07-06       Impact factor: 11.205

Review 2.  The alpha beta complexes of ATP synthase: the alpha 3 beta 3 oligomer and alpha 1 beta 1 protomer.

Authors:  Y Kagawa; S Ohta; M Harada; H Kihara; Y Ito; M Sato
Journal:  J Bioenerg Biomembr       Date:  1992-10       Impact factor: 2.945

Review 3.  Kinetic studies of ATP synthase: the case for the positional change mechanism.

Authors:  K F LaNoue; J Duszynski
Journal:  J Bioenerg Biomembr       Date:  1992-10       Impact factor: 2.945

Review 4.  Identification of subunits required for the catalytic activity of the F1-ATPase.

Authors:  Z Gromet-Elhanan
Journal:  J Bioenerg Biomembr       Date:  1992-10       Impact factor: 2.945

5.  Dynamic inter-subunit interactions in thermophilic F(1)-ATPase subcomplexes studied by cross-correlated relaxation-enhanced polarization transfer NMR.

Authors:  Masumi Kobayashi; Hiromasa Yagi; Toshio Yamazaki; Masasuke Yoshida; Hideo Akutsu
Journal:  J Biomol NMR       Date:  2008-01-05       Impact factor: 2.835

6.  The photosynthetic F1-α 3β 3 and α 1β 1 catalytic core complexes.

Authors:  Z Gromet-Elhanan; M Sokolov
Journal:  Photosynth Res       Date:  1995-11       Impact factor: 3.573

7.  Ligand-dependent structural variations in Escherichia coli F1 ATPase revealed by cryoelectron microscopy.

Authors:  E P Gogol; E Johnston; R Aggeler; R A Capaldi
Journal:  Proc Natl Acad Sci U S A       Date:  1990-12       Impact factor: 11.205

8.  Increasing acidification of nonreplicating Lactococcus lactis deltathyA mutants by incorporating ATPase activity.

Authors:  Martin B Pedersen; Brian J Koebmann; Peter R Jensen; Dan Nilsson
Journal:  Appl Environ Microbiol       Date:  2002-11       Impact factor: 4.792

9.  Mutations on the N-terminal edge of the DELSEED loop in either the α or β subunit of the mitochondrial F1-ATPase enhance ATP hydrolysis in the absence of the central γ rotor.

Authors:  Thuy La; George Desmond Clark-Walker; Xiaowen Wang; Stephan Wilkens; Xin Jie Chen
Journal:  Eukaryot Cell       Date:  2013-09-06

10.  The TF1-ATPase and ATPase activities of assembled alpha 3 beta 3 gamma, alpha 3 beta 3 gamma delta, and alpha 3 beta 3 gamma epsilon complexes are stimulated by low and inhibited by high concentrations of rhodamine 6G whereas the dye only inhibits the alpha 3 beta 3, and alpha 3 beta 3 delta complexes.

Authors:  S R Paik; K Yokoyama; M Yoshida; T Ohta; Y Kagawa; W S Allison
Journal:  J Bioenerg Biomembr       Date:  1993-12       Impact factor: 2.945
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