A novel strategy for analyzing RNA-protein interactions by surface plasmon resonance biosensor.
Surface plasmon resonance (SPR) biosensor is a promising technology for its various advantages including the real-time measurement of biomolecular interactions without labeling. A method of hybridizing RNAs on the surface of the streptavidin-coated (SA) sensor chip to study RNA-protein interactions was described in this paper. In our study, it has been shown that the nucleocapsid (N) protein of severe acute respiratory syndrome coronavirus (SARS-CoV) has a high binding affinity for the leader sequence of SARS-CoV genome. Effect of temperature on the RNA-DNA hybridization was also examined. This method can provide the affinity of interactions with high sensitivity. Therefore, it will be useful in screening binding candidates for a given RNA target motif with one chip.
Yang
Yaling
Y
College of Life Sciences, Wuhan University, Wuhan 430072, People's Republic of China.
Wang
Quan
Q
Guo
Deyin
D
D001483:Base Sequence; D015374:Biosensing Techniques; D017931:DNA Primers; D024202:Electrophoretic Mobility Shift Assay; D009693:Nucleic Acid Hybridization; D012367:RNA, Viral / Q000378:metabolism*; D045473:Severe acute respiratory syndrome-related coronavirus / Q000235:genetics; D020349:Surface Plasmon Resonance / Q000295:instrumentation*; D014764:Viral Proteins / Q000378:metabolism*
D017931:DNA Primers; D012367:RNA, Viral; D014764:Viral Proteins