Structural and functional analysis of the yeast protein Sec13 with an qmphasis on its protein interaction interface

Gogala, Marko (2009) Structural and functional analysis of the yeast protein Sec13 with an qmphasis on its protein interaction interface. Diploma thesis, Faculty of Science > Department of Biology.

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Abstract

Possession of an envelope-coated nucleus is the defining trait of eukaryotes. Since the nuclear pore complex (NPC) is the only known mediator of nucleo-cytoplasmic traffic, elucidating its structure is important for understanding eukaryotic cells. Sec13 is a component of the NPC whose importance for the stability of the complex is unclear. Its dual role in binding proteins Nup145 in the NPC and Sec31 in COPII vesicles makes mutational analysis of Sec13 function difficult. The goal of this project was solving a structure of Sec13 in complex with the Nup145C insertion blade that would provide a clear view of the Sec13/Nup145C interface. The obtained structure was compared to the structures of the Sec13/Sec31 complex. Based on the differences between the interaction sites of the structures, a mutant Sec13 protein was designed, that binds specifically to Sec31, but has lost affinity for Nup145C. The effect of this mutation was confirmed by in vitro experiments.

Item Type: Thesis (Diploma thesis)
Keywords: NPC, Sec13, Sec31, Nup145C, x-ray crystallography
Supervisor: Schwartz, Thomas
Date: 2009
Number of Pages: 77
Subjects: NATURAL SCIENCES > Biology
Divisions: Faculty of Science > Department of Biology
Depositing User: Silvana Šehić
Date Deposited: 10 Sep 2014 11:33
Last Modified: 10 Sep 2014 11:33
URI: http://digre.pmf.unizg.hr/id/eprint/2699

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