Characterization of Escherichia coli ATP synthase .beta.-subunit mutations using a chromosomal delection strain

Biochemistry ◽  
1991 ◽  
Vol 30 (28) ◽  
pp. 6842-6847 ◽  
Author(s):  
Rita S. F. Lee ◽  
Janet Pagan ◽  
Susan Wilke-Mounts ◽  
Alan E. Senior
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Beta Subunit

Site-directed mutagenesis of conserved cysteine residues within the .beta. subunit of Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of the mutated enzymes

Biochemistry ◽  
1993 ◽  
Vol 32 (8) ◽  
pp. 2013-2023 ◽  
Author(s):  
Valerie Augier ◽  
Bruno Guigliarelli ◽  
Marcel Asso ◽  
Patrick Bertrand ◽  
Chantal Frixon ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Nitrate Reductase ◽  
Beta Subunit ◽  
Site Directed Mutagenesis ◽  
Cysteine Residues ◽  
Directed Mutagenesis

Characterization of two nucleotide binding sites on the isolated, reconstitutively active .beta. subunit of the F0.cntdot.F1 ATP synthase

Biochemistry ◽  
1984 ◽  
Vol 23 (5) ◽  
pp. 1022-1028 ◽  
Author(s):  
Zippora Gromet-Elhanan ◽  
Daniel Khananshvili
Keyword(s):  
Atp Synthase ◽  
Binding Sites ◽  
Nucleotide Binding ◽  
Beta Subunit ◽  
Nucleotide Binding Sites

Characterization of an inorganic phosphate binding site on the isolated, reconstitutively active .beta. subunit of F0.cntdot.F1 ATP synthase

Biochemistry ◽  
1985 ◽  
Vol 24 (10) ◽  
pp. 2482-2487 ◽  
Author(s):  
Daniel Khananshvili ◽  
Zippora Gromet-Elhanan
Keyword(s):  
Binding Site ◽  
Atp Synthase ◽  
Inorganic Phosphate ◽  
Beta Subunit ◽  
Phosphate Binding

Assembly of the Escherichia coli FoF1 ATP synthase involves distinct subcomplex formation

2013 ◽  
Vol 41 (5) ◽  
pp. 1288-1293 ◽  
Author(s):  
Gabriele Deckers-Hebestreit
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Cytoplasmic Membrane ◽  
Atp Synthesis ◽  
E Coli ◽  
Assembly Pathway ◽  
Polypeptide Chains ◽  
Fof1 Atp Synthase

The ATP synthase (FoF1) of Escherichia coli couples the translocation of protons across the cytoplasmic membrane by Fo to ATP synthesis or hydrolysis in F1. Whereas good knowledge of the nanostructure and the rotary mechanism of the ATP synthase is at hand, the assembly pathway of the 22 polypeptide chains present in a stoichiometry of ab2c10α3β3γδϵ has so far not received sufficient attention. In our studies, mutants that synthesize different sets of FoF1 subunits allowed the characterization of individually formed stable subcomplexes. Furthermore, the development of a time-delayed in vivo assembly system enabled the subsequent synthesis of particular missing subunits to allow the formation of functional ATP synthase complexes. These observations form the basis for a model that describes the assembly pathway of the E. coli ATP synthase from pre-formed subcomplexes, thereby avoiding membrane proton permeability by a concomitant assembly of the open H+-translocating unit within a coupled FoF1 complex.

scholarly journals Characterization of the mutant-unc D-gene product in a strain of Escherichia coli K12. An altered β-subunit of the magnesium ion-stimulated adenosine triphosphatase

1978 ◽  
Vol 172 (3) ◽  
pp. 523-531 ◽  
Author(s):  
D R H Fayle ◽  
J A Downie ◽  
G B Cox ◽  
F Gibson ◽  
J Radik
Keyword(s):  
Escherichia Coli ◽  
Adenosine Triphosphatase ◽  
Polyacrylamide Gel Electrophoresis ◽  
Beta Subunit ◽  
Beta Subunits ◽  
Normal Strain ◽  
Diploid Strain ◽  
Escherichia Coli K12 ◽  
Low Ionic Strength

Membranes from a mutant strain of Escherichia coli K12 carrying the uncD409 allele were washed in low-ionic-strength buffers in the presence or absence of the proteinase inhibitor p-aminobenzamidine. Unlike membranes from a normal strain, those from strain AN463 (uncD409) did not become proton-permeable, as judged by NADH-induced atebrinfluorescence quenching, when the membranes were washed in the absence of p-aminobenzamide. Furthermore, ATP-dependent atebrin-fluorscence quenching in such washed membranes could not be reconstituted by the addition of solubilized Mg2+-stimulated adenosine triphosphatase preparations. The examination by two-dimensional polyacrylamide-gel electrophoresis of the polypeptide composition of the washed membranes from strain AN463 (uncD409) indicated the presence of a polypeptide of similar molecular weight to the normal beta-subunit of the Mg2+-stimulated adenosine triphosphatase, but with an altered isoelectric point. Both the normal and abnormal beta-subunits were identified in membranes prepared from a partial diploid strain carrying both the unc+ and uncD409 alleles. It is concluded that the uncD gene codes for the beta-subunit of the Mg2+-stimulated adenosine triphosphatase.

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