Category BI L09 Computational and Experimental Studies of Human SLX4 Protein BTB

domain

Abstract As the race to cure cancer reaches a feverish pitch, being able to repair

DNA and ultimately cure cancer is of the utmost importance. The human

SLX4 (Synthetic Lethal of Unknown Function) protein serves as a scaffold

protein which associates with other proteins to execute multiple functions

in DNA repair. It contains an evolutionarily conserved BTB domain, a

versatile protein-protein interaction module. To investigate the structure

and function of SLX4 protein, homology modeling was used to create a 3D

structure of the BTB domain in SLX4. Searching a template library yielded

one template which shares a 21% sequence similarity. This template was

used to generate a 3D model for the BTB-SLX4 domain which consists of

five alpha-helices and three beta-sheets. The alpha-helices and beta-

sheets arrange in the order of beta1-beta2-alpha1-alpha2-beta3-alpha3-

alpha4-alpha5, representing the conserved core BTB fold. A recombinant

protein (rBTB-SLX4) was designed to include this core BTB fold and

additional alpha-helices at both the N- and C-terminus. During our

experiment, rBTB-SLX4 was cloned, expressed and purified from E. coli.

Limited proteolysis of rBTB-SLX4 revealed that Trypsin removes 44 amino

acids from C-terminus of protein. We were able to show that this Trypsin-

digested rBTB-SLX4 protein is responsible for protein-protein interactions

in vitro using the cross-linking reagent DSS. Protein cross-linking analysis

showed dimerization is the predominant form of interaction. Together,

these experiments demonstrate that the BTB domain of SLX4 allows

multiple copies of protein to interact with each other.

Bibliography 1) Svendsen, JM et al (10 July 2009). Mammalian BTBD12/SLX4 assembles

a Holliday junction resolvase and is required for DNA repair. Cell 138 (1):

63–77



2) Peter J Stogios et al (2005) Sequence and structural analysis of BTB

domain proteins. Genome Biology 6:R82 3) Arnold K., Bordoli L., Kopp J.,

and Schwede T. (2006). The SWISS-MODEL Workspace: A web-based

environment for protein structure homology modelling. Bioinformatics,

22,195-201.
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