Literature DB >> 149108

Energy transduction in Escherichia coli: new mutation affecting the Fo portion of the ATP synthetase complex.

B P Rosen, R N Brey, S M Hasan.   

Abstract

A mutation affecting the intrinsic membrane portion (BFo) of the ATP synthetase complex is described. The phenotype is different from previously reported BFo mutants. This mutation results in the ability of membranes lacking the extrinsic membrane portion (BF1) of the ATP synthetase complex to maintain a transmembrane pH gradient. Unlike other BFo mutants, this strain, NR71, is capable of utilizing ATP hydrolysis for the formation of a transmembrane pH gradient.

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Year:  1978        PMID： 149108      PMCID： PMC222352          DOI： 10.1128/jb.134.3.1030-1038.1978

Source DB:  PubMed          Journal:  J Bacteriol        ISSN： 0021-9193            Impact factor:   3.490


  22 in total

1.  Physiological suppression of a transport defect in Escherichia coli mutants deficient in Ca2+, Mg2+-stimulated adenosine triphosphatase.

Authors:  J Boonstra; D L Gutnick; H R Kaback
Journal:  J Bacteriol       Date:  1975-12       Impact factor: 3.490

2.  The maintenance of the energized membrane state and its relation to active transport in Escherichia coli.

Authors:  B P Rosen; L W Adler
Journal:  Biochim Biophys Acta       Date:  1975-04-14

3.  Energy transduction in Escherichia coli. The role of the Mg2+ATPase.

Authors:  T Tsuchiya; B P Rosen
Journal:  J Biol Chem       Date:  1975-11-10       Impact factor: 5.157

4.  A mutation affecting a second component of the F0 portion of the magnesium ion-stimulated adenosine triphosphatase of Escherichia coli K12. The uncC424 allele.

Authors:  F Gibson; G B Cox; J A Downie; J Radik
Journal:  Biochem J       Date:  1977-04-15       Impact factor: 3.857

5.  Removal of protein interference in the Fiske-Subbarow method by sodium dodecyl sulfate.

Authors:  Y Tashima
Journal:  Anal Biochem       Date:  1975-12       Impact factor: 3.365

6.  Properties of Escherichia coli mutants with alterations in Mg2+-adenosine triphosphatase.

Authors:  L W Adler; B P Rosen
Journal:  J Bacteriol       Date:  1976-10       Impact factor: 3.490

7.  A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.

Authors:  M M Bradford
Journal:  Anal Biochem       Date:  1976-05-07       Impact factor: 3.365

8.  Different effects of inhibitors on two mutants of Escherichia coli K12 affected in the Fo portion of the adenosine triphosphatase complex.

Authors:  G B Cox; F L Crane; J A Downie; J Radik
Journal:  Biochim Biophys Acta       Date:  1977-10-12

9.  The use of several energy-coupling reactions in characterizing mutants of Escherichia coli K12 defective in oxidative phosphorylation.

Authors:  H U Schairer; P Friedl; B I Schmid; G Vogel
Journal:  Eur J Biochem       Date:  1976-07-01

10.  Energy transduction in Escherichia coli. The effect of chaotropic agents on energy coupling in everted membrane vesicles from aerobic and anaerobic cultures.

Authors:  S M Hasan; B P Rosen
Journal:  Biochim Biophys Acta       Date:  1977-02-07
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  5 in total

1.  The uncA gene codes for the alpha-subunit of the adenosine triphosphatase of Escherichia coli. Electrophoretic analysis of uncA mutant strains.

Authors:  A E Senior; J A Downie; G B Cox; F Gibson; L Langman; D R Fayle
Journal:  Biochem J       Date:  1979-04-15       Impact factor: 3.857

Review 2.  Transport of H+, K+, Na+ and Ca++ in Streptococcus.

Authors:  D L Heefner
Journal:  Mol Cell Biochem       Date:  1982-04-30       Impact factor: 3.396

Review 3.  Structure and function of proton-translocating adenosine triphosphatase (F0F1): biochemical and molecular biological approaches.

Authors:  M Futai; H Kanazawa
Journal:  Microbiol Rev       Date:  1983-09

4.  Properties and function of the proton-translocating adenosine triphosphatase of Clostridium perfringens.

Authors:  S M Hasan; B P Rosen
Journal:  J Bacteriol       Date:  1979-11       Impact factor: 3.490

5.  Method for isolation of Escherichia coli mutants with defects in the proton-translocating sector of the membrane adenosine triphosphatase complex.

Authors:  R H Fillingame; K Knoebel; A E Wopat
Journal:  J Bacteriol       Date:  1978-11       Impact factor: 3.490
  5 in total

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