Event Information
Structural characterization of the hSRI/PCTD complexes
- Abstract:
Through different phosphorylation states, the C-terminal domain (CTD) of the largest subunit (Rpb1) of RNA polymerase II serves as a loading dock to recruit different nuclear factors during gene transcription and other nuclear events. The CTD and its phosphorylation states (PCTD) have been reported to be intrinsically unstructured. For a PCTD interacting domain (PCID), the recognition is believed to occur through the binding-induced folding of the PCTD within the given PCID. Recently, the Set2-Rpb1 interacting (SRI) domain was found as a novel PCID in yeast Set2 histone methyltransferase and the solution structure of its human counterpart (hSRI) was reported. The hSRI was shown to interact with two distinct PCTD peptides with similar affinity. We propose to determine these hSRI/PCTD complexes because they provide an excellent model and for better understanding the mechanism of PCTD recognition.
We have already mapped the binding surfaces for the different hSRI/PCTD interactions. Based on these results, a disulfide cross-linked hSRI*/PCTD complex was constructed that showed promising preliminary results. In the future, we will 1) optimize the design of the covalent complexes, 2) solve the structures of these complexes and 3) analyze the molecular mechanisms that form the binding interfaces of different PCTD peptides.
Preliminary Examination Seminar
Student Exams Seminar