Single-molecule FRET unravels how Gap Endonuclease I resolves the Holliday junction intermediate structure during DNA recombination DATE:
Monday, March 27, 2017TIME:
2:00 - 3:00 p.m.LOCATION:
Building 2 · Level 5 · Room 5220
Gap Endonuclease 1 (GEN1), is eukaryotic homologous recombination protein essential for resolving four-way DNA (Holliday) junctions inside the cells. Holliday junction is known to exist as interchanging stacked-X isomers. Using Single-Molecule Fӧrster Resonance Energy Transfer (smFRET), we study the structural changes in real time upon binding and cleavage of the Holliday junction by GEN1. Upon GEN1 association, the resolution of the junction proceeds without any detectable intermediary structure but acts in coordinated manner with protein dimerization at the junction.
Dr. Mohamed Sobhy got his doctoral degree in Chemistry from Pennsylvania State University (USA). Then he moved to University of Michigan (USA) to do post-doctoral work in single-molecule fluorescence spectroscopy where he was awarded the National Institute of Health post-doctoral fellowship. He authored and co-authored several scientific papers in different journals of the American Chemical Society, American Institute of Physics and Nature Publishing Group. He participated in several international conferences in the fields of femtochemistry, nanotechnology and single molecule imaging. Currently, he is a research scientist in the laboratory of DNA Replication and Recombination (PI: Professor Samir Hamdan) in KAUST.