Principal Investigator
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P14 Volker Müller
Professor
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Molecular Microbiology & Bioenergetics
Institute of Molecular Biosciences
Biocenter
Goethe-University Frankfurt a.M.
Max-von-Laue-Str. 9
60438 Frankfurt am Main, Germany
Phone +49 (0)69 79 82 95 07
Fax +49 (0)69 79 82 93 06
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P14 ATP synthases: structure and functon of unique enzymes from bacteria and archaea
ATP synthases are key elements in cellular bioenergetics. They developed very early in evolution but still little is known about ATP synthases from ancient life forms, the archaea. Our own preparatory work revealed novel and unique features in these enzymes such as a collar surrounding part of the central stalk, two peripheral stalks and an enormous diversity in size and number of ion-translocating residues in the rotor subunit c. We will focus on the elucidation of their subunit composition and topology, the structure and function of the holoenzymes, subcomplexes and mutant versions isolated from the membranes of archaea or after heterologous production. In addition, we focus on a rather unusual bacterial Na+ F1FO ATP synthase which has a membrane bound rotor composed of different rotor subunits, a bacterial-like FO and a eukaryal-like VO c subunit. The analysis of this intermediate in evolution, the first VO-FO hybrid rotor found in nature, will shed light on the evolution of structure and function of ATP synthases.
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High-resolution AFM topographs (A-C) and electron micrographs (D) of reconstituted c rings from Acebacterium woodii. Each ring is either neighbored by rings either exposing their wide or narrow ends. Reference free correlation averages of the different assemblies revealed 11 masses forming wide and narrow end of the rings. D shows a projection map of 13 merged images at 5 Å resolution. One unit cell of plane group p22,2, with its symmetry elements (two-fold rotation axes and screw axes) is indicated. The unit cell measures 100.3 x 108 Å and contains four c rings.
Structural model of the A1Ao ATP synthase from Pyrococcus furiosus based on single particle analyses. X-ray structures of subunits from F- or A-ATP synthases were fitted into the map. The a subunit is given in yellow, the two peripheral stalks are made by EH-dimers (pink), and the size of the Ao domain is sufficient to harbour the 16-hairpin c-ring from Enterococcus hirae.
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Publications
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Küper, U., Meyer, C., Müller, V., Rachel, R. and Huber, H. (2010) Energized outer membrane and spatial separation of metabolic processes in the hyperthermophilic Archaeon Ignicoccus hospitalis. Proc Natl Acad Sci USA 107, 3152-3156.
Vonck, J., Pisa, K. Y., Morgner, N., Brutschy, B. and Müller, V. (2009) Three-dimensional structure of A1AO ATP synthase from the hyperthermophilic archaeon Pyrococcus furiosus by electron microscopy. J Biol Chem 284, 10110-10119.
Saum, R., Schlegel, K., Meyer, B. and Müller, V. (2009) The F1FO ATP synthase genes in Methanosarcina acetivorans are dispensable for growth and ATP synthesis. FEMS Microbiol Lett 300, 230-236.
Fritz, M., Klyszejko, A.L., Morgner, N., Vonck, J., Brutschy, B., Muller, D.J., Meier. T. and Müller, V. (2008) An intermediate step in the evolution of ATPases: a hybrid FO-VO rotor in a bacterial Na+ F1FO ATP synthase. FEBS Journal 275, 1999-2007.
Deppenmeier U. and Müller, V. (2008) Life close to the thermodynamic limit: How methanogenic archaea conserve energy. Results Probl Cell Differ 45, 123-152.
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Collaborations
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Michel (P3), Kühlbrandt (P1), Meier (P15), Tampé (P16), Dötsch/Bernhard (P2)