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An alternative role of FoF1-ATP synthase in Escherichia coli: synthesis of thiamine triphosphate
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2013 (English)In: Scientific Reports, ISSN 2045-2322, Vol. 3, 1071- p.Article in journal (Refereed) Published
Abstract [en]

In E. coli, thiamine triphosphate (ThTP), a putative signaling molecule, transiently accumulates in response to amino acid starvation. This accumulation requires the presence of an energy substrate yielding pyruvate. Here we show that in intact bacteria ThTP is synthesized from free thiamine diphosphate (ThDP) and P-i, the reaction being energized by the proton-motive force (Delta p) generated by the respiratory chain. ThTP production is suppressed in strains carrying mutations in F-1 or a deletion of the atp operon. Transformation with a plasmid encoding the whole atp operon fully restored ThTP production, highlighting the requirement for FoF1-ATP synthase in ThTP synthesis. Our results show that, under specific conditions of nutritional downshift, FoF1-ATP synthase catalyzes the synthesis of ThTP, rather than ATP, through a highly regulated process requiring pyruvate oxidation. Moreover, this chemiosmotic mechanism for ThTP production is conserved from E. coli to mammalian brain mitochondria.

Place, publisher, year, edition, pages
2013. Vol. 3, 1071- p.
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Biological Sciences
URN: urn:nbn:se:su:diva-88361DOI: 10.1038/srep01071ISI: 000313551000005OAI: diva2:612953


Available from: 2013-03-25 Created: 2013-03-13 Last updated: 2013-03-25Bibliographically approved

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von Ballmoos, Christoph
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Department of Biochemistry and Biophysics
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