Literature DB >> 11768298

Mutagenic analysis of the F0 stator subunits.

B D Cain1.   

Abstract

The a and b subunits constitute the stator elements in the F0 sector of F1F0-ATP synthase. Both subunits have been difficult to study by physical means, so most of the information on structure and function relationships in the a and b subunits has been obtained using mutagenesis in combination with biochemical methods. These approaches were used to demonstrate that the a subunit in association with the ring of c subunits houses the proton channel through F1F0-ATP synthase. The map of the amino acids contributing to the proton channel is probably complete. The two b subunits dimerize, forming an extended flexible unit in the peripheral stalk linking the F1 and F0 sectors. The unique characteristics of specific amino acid substitutions affecting the a and b subunits suggested differential effects on rotation during F1F0-ATPase activity.

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Year:  2000        PMID: 11768298     DOI: 10.1023/a:1005575919638

Source DB:  PubMed          Journal:  J Bioenerg Biomembr        ISSN: 0145-479X            Impact factor:   2.945


  51 in total

1.  Structural changes linked to proton translocation by subunit c of the ATP synthase.

Authors:  V K Rastogi; M E Girvin
Journal:  Nature       Date:  1999-11-18       Impact factor: 49.962

2.  Intragenic and intergenic suppression of the Escherichia coli ATP synthase subunit a mutation of Gly-213 to Asn: functional interactions between residues in the proton transport site.

Authors:  P H Kuo; R K Nakamoto
Journal:  Biochem J       Date:  2000-05-01       Impact factor: 3.857

3.  The a subunit ala-217 --> arg substitution affects catalytic activity of F(1)F(0) ATP synthase.

Authors:  J L Gardner; B D Cain
Journal:  Arch Biochem Biophys       Date:  2000-08-01       Impact factor: 4.013

4.  Role of the carboxyl terminal region of H(+)-ATPase (F0F1) a subunit from Escherichia coli.

Authors:  S Eya; M Maeda; M Futai
Journal:  Arch Biochem Biophys       Date:  1991-01       Impact factor: 4.013

5.  ATP synthase's second stalk comes into focus.

Authors:  S Wilkens; R A Capaldi
Journal:  Nature       Date:  1998-05-07       Impact factor: 49.962

6.  Glutamate residues at positions 219 and 252 in the a-subunit of the Escherichia coli ATP synthase are not functionally equivalent.

Authors:  L P Hatch; G B Cox; S M Howitt
Journal:  Biochim Biophys Acta       Date:  1998-03-25

7.  Proton translocation by the F1F0ATPase of Escherichia coli. Mutagenic analysis of the a subunit.

Authors:  B D Cain; R D Simoni
Journal:  J Biol Chem       Date:  1989-02-25       Impact factor: 5.157

Review 8.  Mitochondrial diseases in man and mouse.

Authors:  D C Wallace
Journal:  Science       Date:  1999-03-05       Impact factor: 47.728

9.  Interaction between Glu-219 and His-245 within the a subunit of F1F0-ATPase in Escherichia coli.

Authors:  B D Cain; R D Simoni
Journal:  J Biol Chem       Date:  1988-05-15       Impact factor: 5.157

Review 10.  Coupling H(+) transport to rotary catalysis in F-type ATP synthases: structure and organization of the transmembrane rotary motor.

Authors:  R H Fillingame; W Jiang; O Y Dmitriev
Journal:  J Exp Biol       Date:  2000-01       Impact factor: 3.312

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  21 in total

1.  Mutagenesis studies of the F1F0 ATP synthase b subunit membrane domain.

Authors:  Andrew W Hardy; Tammy Bohannon Grabar; Deepa Bhatt; Brian D Cain
Journal:  J Bioenerg Biomembr       Date:  2003-10       Impact factor: 2.945

Review 2.  Subunit structure, function, and arrangement in the yeast and coated vesicle V-ATPases.

Authors:  Takao Inoue; Stephan Wilkens; Michael Forgac
Journal:  J Bioenerg Biomembr       Date:  2003-08       Impact factor: 2.945

3.  Aqueous access pathways in subunit a of rotary ATP synthase extend to both sides of the membrane.

Authors:  Christine M Angevine; Kelly A G Herold; Robert H Fillingame
Journal:  Proc Natl Acad Sci U S A       Date:  2003-10-31       Impact factor: 11.205

4.  Structural study on the architecture of the bacterial ATP synthase Fo motor.

Authors:  Jonna K Hakulinen; Adriana L Klyszejko; Jan Hoffmann; Luise Eckhardt-Strelau; Bernd Brutschy; Janet Vonck; Thomas Meier
Journal:  Proc Natl Acad Sci U S A       Date:  2012-06-26       Impact factor: 11.205

5.  Definition of membrane topology and identification of residues important for transport in subunit a of the vacuolar ATPase.

Authors:  Masashi Toei; Satoko Toei; Michael Forgac
Journal:  J Biol Chem       Date:  2011-08-08       Impact factor: 5.157

6.  Manipulating the length of the b subunit F1 binding domain in F1F0 ATP synthase from Escherichia coli.

Authors:  Deepa Bhatt; Stephanie P Cole; Tammy Bohannon Grabar; Shane B Claggett; Brian D Cain
Journal:  J Bioenerg Biomembr       Date:  2005-04       Impact factor: 2.945

Review 7.  ATP synthase: subunit-subunit interactions in the stator stalk.

Authors:  Joachim Weber
Journal:  Biochim Biophys Acta       Date:  2006-04-19

8.  Interaction of transmembrane helices in ATP synthase subunit a in solution as revealed by spin label difference NMR.

Authors:  Oleg Y Dmitriev; Karen H Freedman; Joseph Hermolin; Robert H Fillingame
Journal:  Biochim Biophys Acta       Date:  2007-12-15

9.  Obstruction of transmembrane helical movements in subunit a blocks proton pumping by F1Fo ATP synthase.

Authors:  Kyle J Moore; Robert H Fillingame
Journal:  J Biol Chem       Date:  2013-07-17       Impact factor: 5.157

10.  The b (arg36) contributes to efficient coupling in F(1)F (O) ATP synthase in Escherichia coli.

Authors:  Amanda K Welch; Shane B Claggett; Brian D Cain
Journal:  J Bioenerg Biomembr       Date:  2008-01-19       Impact factor: 2.945

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