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BP: Fachverband Biologische Physik

BP 8: Posters: Proteins

BP 8.4: Poster

Montag, 11. März 2013, 17:30–19:30, Poster B2

Dual-Color Fluorescence Cross-Correlation Spectroscopy of the macromolecular spliceosomal complex — •Mira Prior¹, Thomas Ohrt², Julia Dannenberg², Ingo Gregor¹, Reinhard Lührmann², and Jörg Enderlein¹ — ¹Drittes Physikalisches Institut-Biophysik, Göttingen — ²Max Planck Institut für Biophysikalische Chemie, Göttingen

The spliceosome is the cellular machinery responsible for removing non-coding introns from precursor mRNA. During its catalytic action the spliceosome undergoes compositional and conformational changes. We are investigating the conditions for recruitment and release of particular proteins during the splicing steps. We determine how the changes occur (stepwise or in a correlated manner) and the roles of certain spliceosomal RNA helicases in the restructuring of the complex. The spectroscopic method we use is Dual-Color-Fluorescence Cross-Correlation Spectroscopy (2-color-FCCS) which allows for studying structural and dynamical properties of proteins. We observed the thermally stable splicing factor Cwc25. We could determine, under which conditions it binds to the complex, when it is released and the conditions for stable binding of Cwc25 to the spliceosome. By measuring several mutants we could answer the question whether Cwc25 is released before or during the second catalytic step. Furthermore, we detected the binding of the proteins Slu7 and Prp16. These proteins are necessary for the second catalytic step and are involved in the binding behavior of Cwc25.