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Researchers from Max-Planck-Institute of Biophysics Detail Findings in Escherichia coli

February 25, 2014

By a News Reporter-Staff News Editor at Life Science Weekly -- Researchers detail new data in Proteobacteria. According to news reporting out of Frankfurt, Germany, by NewsRx editors, research stated, "F1FO ATP synthases catalyze the synthesis of ATP from ADP and inorganic phosphate driven by ion motive forces across the membrane. A number of ATP synthases have been characterized to date."

Our news journalists obtained a quote from the research from the Max-Planck-Institute of Biophysics, "The one from the hyperthermophilic bacterium Aquifex aeolicus presents unique features, i.e. a putative heterodimeric stalk. To complement previous work on the native form of this enzyme, we produced it heterologously in Escherichia coli. We designed an artificial operon combining the nine genes of A. aeolicus ATP synthase, which are split into four clusters in the A. aeolicus genome. We expressed the genes and purified the enzyme complex by affinity and size-exclusion chromatography. We characterized the complex by native gel electrophoresis, Western blot, and mass spectrometry. We studied its activity by enzymatic assays and we visualized its structure by single-particle electron microscopy. We show that the heterologously produced complex has the same enzymatic activity and the same structure as the native ATP synthase complex extracted from A. aeolicus cells. We used our expression system to confirm that A. aeolicus ATP synthase possesses a heterodimeric peripheral stalk unique among non-photosynthetic bacterial F1FO ATP synthases. Our system now allows performing previously impossible structural and functional studies on A. aeolicus F1FO ATP synthase."

According to the news editors, the research concluded: "More broadly, our work provides a valuable platform to characterize many other membrane protein complexes with complicated stoichiometry, i.e. other respiratory complexes, the nuclear pore complex, or transporter systems."

For more information on this research see: Production of fully assembled and active Aquifex aeolicus F1FO ATP synthase in Escherichia coli. Biochimica Et Biophysica Acta, 2014;1840(1):34-40 (see also Proteobacteria).

Our news journalists report that additional information may be obtained by contacting C. Zhang, Max Planck Institute of Biophysics, Dept. of Molecular Membrane Biology, Max-von-Laue-Str 3, D-60438 Frankfurt am Main, Germany. Additional authors for this research include M. Allegretti, J. Vonck, J.D. Langer, M. Marcia, G. Peng and H. Michel.

Keywords for this news article include: Europe, Germany, Synthase, Frankfurt, Proteobacteria, Escherichia coli, Enterobacteriaceae, Enzymes and Coenzymes, Gram Negative Bacteria.

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Source: Life Science Weekly

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