Cellular Logistics - 'Traceless' protein modification by small high-affinity tags in living cells

Labeling and modification of intracellular proteins remain a major challenge in life sciences, often limited by large fusion domains, high quantities of costly probes, and long reaction times. Here, we will guide protein trans-splicing by minimal high-affinity interaction pairs to trace proteins´ function and assembly in living cells. In addition, we aim at modulating cellular processes by light with high resolution in time and space. Combined with super-resolution microscopy and single-molecule analysis, these traceless approaches shall provide valuable insights into the co-operative function and suprastructures of proteins in particular at intracellular membranes.

Prof. Dr. Robert Tampé
Goethe-Universität Frankfurt am Main

Tel.: +49 69 798 29475
Fax: +49 69 798 29495

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Publications within the SPP 1623 project

A. Blees, D. Januliene, T. Hofmann, N. Koller, C. Schmidt, S. Trowitzsch, A. Moeller, R. Tampé
Nature 2017, 551, 525-528
Structure of the human MHC-I peptide-loading complex
Link to the article

M. Braner, R. Wieneke, R. Tampé
Chem.Commun. 2017, 53, 545-548
Nanomolar affinity protein trans-splicing monitored in real-time by fluorophore-quencher pairs.
Link to the article

A. Guesdon, F. Bazile, R.M. Buey, R. Mohan, S. Monier, R.R. Garcia, M. Angevin, C. Heichette, R. Wieneke, R. Tampé, L. Duchesne, A. Akhmanova, M.O. Steinmetz, D. Chrétien
Nature Cell Biology 2016, 8, 1102-1108
EB1 interacts with outwardly curved and straight regions of the microtubule lattice.
Link to the article