Author: Lee, Na-Ra; Kwon, Hyun-Mi; Park, Kkothanahreum; Oh, Sangtaek; Jeong, Yong-Joo; Kim, Dong-Eun
Title: Cooperative translocation enhances the unwinding of duplex DNA by SARS coronavirus helicase nsP13 Document date: 2010_7_29
ID: 1k99yv4i_29
Snippet: In order to investigate whether oligomerization of the nsP13 monomer is facilitated in the presence of ssDNA and ATP, we used a chemical cross-linking assay to examine the oligomeric state of nsP13 in the presence or absence of ligands. Chemical cross-linking with DMS showed that the degree of cross-linking was slightly altered in the presence of ligands; a higher order oligomers were observed in the presence of longer ssDNA (arrowheads in Figure.....
Document: In order to investigate whether oligomerization of the nsP13 monomer is facilitated in the presence of ssDNA and ATP, we used a chemical cross-linking assay to examine the oligomeric state of nsP13 in the presence or absence of ligands. Chemical cross-linking with DMS showed that the degree of cross-linking was slightly altered in the presence of ligands; a higher order oligomers were observed in the presence of longer ssDNA (arrowheads in Figure 6 ). Interestingly, the nsP13 protein itself readily formed a dimer and trimer in the absence of any ligands. Thus, oligomerization of nsP13 is an intrinsic property of the protein, which is facilitated in the presence of long ssDNA and ATP. However, we could not determine the definite oligomeric state of the helicase in this study, suggesting that a dynamic oligomeric status of the helicase might exist in the presence of ss DNA.
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