Biochemical and genetic studies on the assembly and function of the F1-F0 adenosine triphosphatase of Escherichia coli.
نویسنده
چکیده
I am deeply appreciative of the honour of being invited to deliver the 13th Hopkins Memorial Lecture. In doing so, I am conscious that this honour reflects on the many colleagues, both academic and technical, who have worked in the laboratory in Canberra over the years. While it might seem invidious to single out individuals for special mention, and the names of many collaborators are cited in references, I must make one exception. I refer to my colleague, Dr. Graeme Cox, who has been involved in the work I will be describing since its inception, and whose contributions, both practical and conceptual, have been outstanding.
منابع مشابه
The uncA gene codes for the alpha-subunit of the adenosine triphosphatase of Escherichia coli. Electrophoretic analysis of uncA mutant strains.
Four mutant strains of Escherichia coli which lack membrane-bound adenosine triphosphatase activity were shown by genetic-complementation tests to carry mutations in the uncA gene. A soluble inactive F1-ATPase aggregate was released from the membranes of three of the uncA mutant strains by low-ionic-strength washing, and purified by procedures developed for the purification of F1-ATPase from no...
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How the ‘energy currency’ of the cell, adenosine triphosphate (ATP), is produced consequent upon the oxidation of foodstuffs (oxidative phos phorylation) is, despite prolonged research, still a matter of debate and the molecular mechanism of the process is unknown. I t appears that the problem of oxidative phosphorylation can be approached with the aid of the biochemical genetics of the bacter...
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How the 'energy currency' of the cell, adenosine triphosphate (ATP), is produced consequent upon the oxidation of foodstuffs (oxidative phosphorylation) is, despite prolonged research, still a matter of debate and the molecular mechanism of the process is unknown. It appears that the problem of oxidative phosphorylation can be approached with the aid of the biochemical genetics of the bacterium...
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F1-ATPase (F1) is a multisubunit water-soluble domain of FoF1- ATP synthase and is a rotary enzyme by itself. Earlier genetic studies using yeast suggested that two factors, Atp11p and Atp12p, contribute to F1 assembly. Here, we show that their mammalian counterparts, AF1 and AF2, are essential and sufficient for efficient production of recombinant bovine mitochondrial F1 in Escherichia coli ce...
متن کاملInhibition of the membrane-bound adenosine triphosphatase of Escherichia coli by dicyclohexylcarbodi-imide.
The inhibition of the membrane-bound adenosine triphosphatase of Escherichia coli by DCCD (dicyclohexylcarbodi-imide) is studied under conditions of varying KCl concentration. An increase in K+ concentration and in other cations causes an increase in the DCCD sensitivity of the enzyme, as well as significant changes in the kinetic parameters.
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عنوان ژورنال:
- Biochemical Society transactions
دوره 11 3 شماره
صفحات -
تاریخ انتشار 1983