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A2: Membrane Transport Machineries

Coordinators

Robert Tampé
CEF Principal Investigator
Institute of Biochemistry
Goethe University Frankfurt
tampe@em.uni-frankfurt.de
Enrico Schleiff
CEF Principal Investigator
Institute of Molecular Biosciences
Goethe University Frankfurt
schleiff@bio.uni-frankfurt.de
Thomas Meier
CEF Adjunct Investigator
Structural Biology
Max-Planck-Institute of Biophysics
thomas.meier@mpibp-frankfurt.mpg.de
Martin Pos
CEF Investigator
Institute of Biochemistry
Goethe University Frankfurt
pos@em.uni-frankfurt.de

 

Researchers involved

Beate Averhoff
Clemens Glaubitz
Robert Tampé
Eckhard Boles
Werner Kühlbrandt
Bernhard Brutschy
Thomas Meier
Volker Dötsch
Martin Pos

 

Transporters provide the entry and exit sites for solutes and whole proteins in and out of all cells. Organized in complex networks and dynamic assemblies, they control and regulate cellular compartmentalization.

Their molecular architectures range from large macromolecular machineries to oligomeric complexes and monomers, some of which are organized on scaffolding proteins. At present, our knowledge of their oligomeric state, interaction partners, stoichiometry, and dynamic rearrangements is limited.

The structures of some key transport assemblies have been determined in Frankfurt. Within the context of this Cluster we plan to tackle the structure, assembly and trafficking of e.g. MHC class I peptide-loading complexes and the mitochondrial protein translocases TOM and TIM. Numerous techniques for detecting protein interactions in vivo, and for quantifying them in vitro are already in place. The objective for the coming years is to add methods for studying membrane protein interactions, for dissecting multi-protein complexes and for increasing throughput.

AcrB pump of E. coli

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