Citation: YANG Xiao-Jing, LIU Xi-Li, LOU Chun-Bo, OUYANG Qi. End Effects during the Binding of Protein to Linear DNA Fragments[J]. Acta Physico-Chimica Sinica, ;2010, 26(07): 2007-2014. doi: 10.3866/PKU.WHXB20100701
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Many in vitro techniques have been employed to elucidate the interaction between DNA and protein. However, one of the most significant differences between in vitro and in vivo studies is that DNA fragments used for in vitro experiments are usually much shorter than genomic DNA. Therefore, several investigators have sought to examine the effects of linear DNA ends on DNA-protein interactions in different systems. Surprisingly, the various efforts have led to contradictory results. Here, we revisit this issue using the DNA-Mnt repressor interaction system. Using surface plasmon resonance (SPR), we monitor both the association and dissociation of the Mnt repressor with a series of DNA fragments. We conclude that Mnt repressor dissociation from DNA near the ends occurs faster than that frominternal positions. In addition, we find that proximity to the end can directly influence protein-specific binding for binding sites near the end.
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