Coordination of the Research Unit 967
Final Report Abstract
It was the task of the two coordinating scientists of the Research Unit 967 to implement the framework and spirit for the free and timely exchange of ideas, methods, and results within the Unit as well as to provide an interface to the scientific community. Their DFG-sponsored secretary was responsible for handling of the common financial support for the participating groups, such as travelling- and publication-expenses and reimbursements for laboratory exchanges and visiting scientists. In addition, she organized a total of eight internal meetings plus three international meetings over the six-year funding period. Furthermore, a central homepage was established for the Research Unit that served as a public relations instrument as well as an internal platform for publications and lab protocols. Without any doubt, the key element for the stimulating atmosphere within the Research Unit were the internal symposia and the international conferences.
Publications
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(2010) BiP modulates the affinity of its co-chaperone ERj1 to ribosomes. J. Biol. Chem. 285, 36427-36433
Benedix, J., Lajoie, P., Jaiswal, H., Burgard, C., Greiner, M., Zimmermann, R., Rospert, S., Snapp, E.L., Dudek, J.
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(2010) Cooperation of stop-transfer and conservative sorting mechanisms in biogenesis of mitochondrial ABC transporter. Current Biol. 20, 1227-1232
Bohnert, M., Rehling, P., Guiard, B., Herrmann, J.M., Pfanner, N., van der Laan, M.
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(2010) Ribosome binding proteins Mdm38 and Mba1 display overlapping functions for regulation of mitochondrial translation. Mol. Biol. Cell 15, 1937-1944
Bauerschmitt, H., Mick, D.U., Deckers, M., Vollmer, C., Funes, S., Kehrein, K., Ott, M., Rehling, P., Herrmann, J.M.
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(2011) Mdm38 is a 14-3-3-like receptor and associates with the protein synthesis machinery at the inner mitochondrial membrane. Traffic 12, 1457-1466
Lupo, D., Vollmer, C., Deckers, M., Mick, D.U., Tews, I., Sinning, I., Rehling, P.
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(2011) Signal-sequence-independent SRP-SR complex formation at the membrane suggests alternative targeting pathway within the SRP cycle. Mol. Biol. Cell 22, 2309-2323
Braig, D., Mircheva, M., Sachelaru, I., van der Sluis, E.O., Sturm, L., Beckmann, R., Kock H.-G.
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(2012) Oxa1-ribosome complexes coordinate the assembly of cytochrome c oxidase in mitochondria. J. Biol. Chem. 287, 34484-34493
Keil, M., Bareth, B., Woellhaf, M.M., Peleh, V., Prestele, M. Rehling, P., Herrmann, J.M.
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(2012) The mitochondrial Oxidase Assembly Protein 1 (Oxa1) insertase forms a membrane pore in lipid bilayers. J. Biol. Chem. 287, 33314-33326
Krüger, V., Deckers, M., Hildenbeutel, M., van der Laan, M., Hellmers, M., Dreker, C., Preuss, M. Herrmann, J.M., Rehling, P., Wagner, R., Meinecke, M.
