Page 16 - U. Protein structure and function

[U. Protein structure and function-11]

Biochemical studies on human chromatin remodeling

components by NMR, fluorescence and crosslinking

experiments

Gye-young Park¹˙#, Jeongmin Han¹˙#, Jae-Hyun Park¹, Ji-Hye Yun¹, Weontae Lee¹˙*

¹Department of Biochemistry, College of Life Science & Biotechnology, Seoul 03722, Republic of Korea

To accomplish viral life cycle, HIV virus hijacks host proteins, the so-called co-factors of replication. Lens epithelium
derived growth factor, LEDGF is a co-factor of HIV-1 integrase (HIV-1 IN) and it is required for the tethering and
correct integration of the viral genome into the host chromatin. hSNF5 is the core subunit of SWI/SNF chromatin-

remodeling complexes, modulating HIV viral replication in multiple ways. Several studies revealed that the pre
integration complex (PIC) contains HIV-1 IN, LEDGF, hSNF5 and other co-factors. Our studies between HIV-1 IN and

hSNF5Rpt1 were performed using pull down assays, fluorescence assays, and nuclear magnetic resonance (NMR)
spectroscopy. The binding constant (Kd) between hSNF5Rpt1 and HIV-1 IN was determined as ~2 mM, which is

relatively weak. Data from cross-linking experiments supports that HIV-1 IN, LEDGF, and hSNF5 forms a complex.
Our results support the detailed molecular mechanism of protein-protein interaction during AIDS infection pathways.