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    CMUR > College of Medicine > School of Medicine > Journal articles >  Item 310903500/1912
    Please use this identifier to cite or link to this item: http://ir.cmu.edu.tw/ir/handle/310903500/1912


    Title: Mutagenesis identifies the critical regions and amino acid residues of suid herpesvirus 1 DNA-binding protein required for DNA binding and strand invasion
    Authors: 吳世祿(Shih-Lu Wu);李佳橙(Chia-Cheng Li);侯庭鏞(Tin-Yun Ho)*;項千芸(Chien-Yun Hsiang)*
    Contributors: 醫學院醫學系學士班生化學科
    Keywords: Suid herpesvirus 1;DNA-binding protein;Chemical modification;Site-directed mutagenesis;DNA binding;Strand invasion
    Date: 2009-03
    Issue Date: 2009-08-19 17:23:01 (UTC+8)
    Abstract: Herpesviral DNA-binding protein (DBP) is a unique protein involved in viral DNA replication and genomic recombination. It binds and stabilizes the single-stranded DNA. It also forms the D-loops and promotes the strand invasion. To identify the functional regions and amino acid residues required for DNA binding and D-loop formation, we characterized several DBP mutants of suid herpesvirus 1 (SuHV-1). Acetic anhydride modification assay showed that lysine residues were critical for DNA binding and D-loop formation. Replacement of highly conserved lysine residues with alanine revealed that Lys-756 and Lys-970 were critical for DNA binding, while Lys-161 participated in DNA binding and D-loop formation. Analysis of nested deleted mutants showed that N-terminal 201 amino acid residues and C-terminal 305 amino acid residues were required for D-loop formation and DNA binding, respectively. In conclusion, these findings suggested that SuHV-1 DBP contained critical regions for DNA binding and D-loop formation, and Lys-161, Lys-756, and Lys-970 were required for DNA binding or D-loop formation.
    Relation: VIRUS RESEARCH 140(1-2):147~154
    Appears in Collections:[School of Medicine] Journal articles

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