Literature DB >> 7852354

Assembly of F0 sector of Escherichia coli H+ ATP synthase. Interdependence of subunit insertion into the membrane.

J Hermolin1, R H Fillingame.   

Abstract

The F0 sector of the Escherichia coli H+ transporting ATP synthase is composed of a complex of three subunits, each of which traverses the inner membrane. We have studied the interdependence of subunit insertion into the membrane in a series of chromosomal mutants in which the primary mutation prevented insertion of one of the F0 subunits. Subunit insertion was assessed using Western blots of mutant membrane preparations. Subunit b and subunit c were found to insert into the membrane independently of the other two F0 subunits. On the other hand, subunit a was not inserted into membranes that lacked either subunit b or subunit c. The conclusion that subunit a insertion is dependent upon the co-insertion of subunits b and c differs from the conclusion of several studies, where subunits were expressed from multicopy plasmids.

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Year:  1995        PMID: 7852354     DOI: 10.1074/jbc.270.6.2815

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  18 in total

1.  Energy-driven subunit rotation at the interface between subunit a and the c oligomer in the F(O) sector of Escherichia coli ATP synthase.

Authors:  M L Hutcheon; T M Duncan; H Ngai; R L Cross
Journal:  Proc Natl Acad Sci U S A       Date:  2001-07-03       Impact factor: 11.205

2.  HMW1 is required for stability and localization of HMW2 to the attachment organelle of Mycoplasma pneumoniae.

Authors:  Melisa J Willby; Mitchell F Balish; Stephanie M Ross; Kyungok K Lee; Jarrat L Jordan; Duncan C Krause
Journal:  J Bacteriol       Date:  2004-12       Impact factor: 3.490

3.  ATP synthesis without R210 of subunit a in the Escherichia coli ATP synthase.

Authors:  Robert R Ishmukhametov; J Blake Pond; Asma Al-Huqail; Mikhail A Galkin; Steven B Vik
Journal:  Biochim Biophys Acta       Date:  2007-11-19

4.  Constant c10 ring stoichiometry in the Escherichia coli ATP synthase analyzed by cross-linking.

Authors:  Britta Ballhausen; Karlheinz Altendorf; Gabriele Deckers-Hebestreit
Journal:  J Bacteriol       Date:  2009-01-30       Impact factor: 3.490

5.  Subunit δ is the key player for assembly of the H(+)-translocating unit of Escherichia coli F(O)F1 ATP synthase.

Authors:  Florian Hilbers; Ruth Eggers; Kamila Pradela; Kathleen Friedrich; Brigitte Herkenhoff-Hesselmann; Elisabeth Becker; Gabriele Deckers-Hebestreit
Journal:  J Biol Chem       Date:  2013-07-17       Impact factor: 5.157

Review 6.  Biogenesis of bacterial inner-membrane proteins.

Authors:  Sandra J Facey; Andreas Kuhn
Journal:  Cell Mol Life Sci       Date:  2010-03-05       Impact factor: 9.261

7.  Interaction with monomeric subunit c drives insertion of ATP synthase subunit a into the membrane and primes a-c complex formation.

Authors:  Hannah E Pierson; Eva-Maria E Uhlemann; Oleg Y Dmitriev
Journal:  J Biol Chem       Date:  2011-09-07       Impact factor: 5.157

8.  Analysis of an N-terminal deletion in subunit a of the Escherichia coli ATP synthase.

Authors:  Robert R Ishmukhametov; Jessica DeLeon-Rangel; Shaotong Zhu; Steven B Vik
Journal:  J Bioenerg Biomembr       Date:  2017-01-11       Impact factor: 2.945

9.  Time-delayed in vivo assembly of subunit a into preformed Escherichia coli FoF1 ATP synthase.

Authors:  Britta Brockmann; Kim Danielle Koop Genannt Hoppmann; Henrik Strahl; Gabriele Deckers-Hebestreit
Journal:  J Bacteriol       Date:  2013-07-08       Impact factor: 3.490

10.  Structural interactions between transmembrane helices 4 and 5 of subunit a and the subunit c ring of Escherichia coli ATP synthase.

Authors:  Kyle J Moore; Robert H Fillingame
Journal:  J Biol Chem       Date:  2008-09-11       Impact factor: 5.157

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