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BP: Fachverband Biologische Physik
BP 11: Posters: Single-Molecule Biophysics
BP 11.11: Poster
Monday, March 14, 2011, 17:15–20:00, P3
Coronavirus nsp7-nsp8 complex formation investigated by single-molecule methods — •Henning Seidel1, Yibei Xiao2, Rolf Hilgenfeld2, and Christian G. Hübner1 — 1Institute of Physics, Ratzeburger Allee 160, 23562 Lübeck, Germany — 2Institute of Biochemistry, Ratzeburger Allee 160, 23562 Lübeck, Germany
The self-organized structure building capabilities of proteins are fascinating biophysicists since decades. With the advent of single-molecule methods, namely fluorescence correlation spectroscopy (FCS) and fluorescence resonance energy transfer (FRET), the process of complex formation is becoming accessible to direct observation.
Coronaviruses are enveloped positive-stranded RNA viruses. For SARS-CoV, it was shown that coronaviruses encode a RNA-dependent RNA-polymerase (RdRp) build from non-structural protein 7 (nsp7) and non-structural protein 8 (nsp8). This hexadecameric nsp7-nsp8 complex is a hollow, cylinder-like structure assembled from eight copies of nsp8 and held together by eight nsp7 molecules. We are aiming at understanding the assembly process and conformational changes of the complex for the related Feline Coronavirus. The structural and functional examination of the nsp7-nsp8 complex formation should help in understanding the replication and transcription mechanisms of Fe-CoV and other coronaviruses like SARS-CoV.