tailieunhanh - Báo cáo khoa học: An intermediate step in the evolution of ATPases – a hybrid F0–V0 rotor in a bacterial Na+ F1F0 ATP synthase

The Na + F1F0 ATP synthase operon of the anaerobic, acetogenic bacte-rium Acetobacterium woodiiis unique because it encodes two types of csubunits, two identical 8 kDa bacterial F0-like csubunits (c2 and c3 ), with two transmembrane helices, and a 18 kDa eukaryal V0 -like (c1 ) csubunit, with four transmembrane helices but only one binding site. | ỊFEBS Journal An intermediate step in the evolution of ATPases - a hybrid F0-V0 rotor in a bacterial Na F1F0 ATP synthase Michael Fritz Adriana L. Klyszejko Nina Morgner Janet Vonck Bernd Brutschy Daniel J. Muller2 Thomas Meier4 and Volker Muller1 1 Molecular Microbiology Bioenergetics Institute of Molecular Biosciences Johann Wolfgang Goethe University Frankfurt Main Germany 2 BioTechnologicalCenter University of Technology Dresden Germany 3 Microkinetic Clusterchemistry Mass- and Laserspectroscopy Institute of Physicaland TheoreticalChemistry Johann Wolfgang Goethe University Frankfurt Main Germany 4 Max-Planck-Institute of Biophysics Frankfurt Germany Keywords Acetobacterium acetogen ATP-synthase c ring F0-V0 hybrid rotor Correspondence V. Muller Molecular Microbiology Bioenergetics Institute of Molecular Biosciences Johann Wolfgang Goethe University Max-von-Laue-StraBe 9 D-60438 Frankfurt Germany Fax 49 69 79829306 Tel 49 69 79829507 E-mail vmueller@ These authors contributed equally to this study Received 18 December 2007 revised 15 February 2008 accepted 22 February 2008 doi The Na F1F0 ATP synthase operon of the anaerobic acetogenic bacterium Acetobacterium woodii is unique because it encodes two types of c subunits two identical 8 kDa bacterial F0-like c subunits c2 and c3 with two transmembrane helices and a 18 kDa eukaryal V0-like c1 c subunit with four transmembrane helices but only one binding site. To determine whether both types of rotor subunits are present in the same c ring we have isolated and studied the composition of the c ring. High-resolution atomic force microscopy of 2D crystals revealed 11 domains each corresponding to two transmembrane helices. A projection map derived from electron micrographs calculated to 5 A resolution revealed that each c ring contains two concentric slightly staggered packed rings each composed of 11 densities representing 22 transmembrane helices. The inner and .

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