Conformational change in the herpes simplex single-strand binding protein induced by DNA
K C Dudas1, S K Scouten, W T Ruyechan
1Department of Microbiology, Witebsky Center for Microbial Pathogenesis and Immunology, State University of New York at Buffalo, 3435 Main Street, Buffalo, NY 14214, USA.
Abstract:
Protease digestion of the herpes simplex virus type 1 major single-strand DNA binding protein ICP8 showed that the cleavage patterns observed in the presence and absence of single-stranded DNA oligonucleotides are substantially different with protection of cleavage sites between amino acids 293 and 806 observed in the presence of oligonucleotide. Experiments using ICP8 modified with fluorescein-5-maleimide (FM) showed that the fluorescence signal exhibited increased susceptibility to antibody quenching and a significant decrease in polarization of the FM fluorescence was observed in the presence compared to the absence of oligonucleotide. Taken together, these results indicate that ICP8 undergoes a conformational change upon binding to single-stranded DNA.
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