Comparison of EMSA and SPR for the characterization of RNA-RNase II complexes.
RNases are enzymes that process and degrade RNA molecules. As such, the study of the interactions between these enzymes and RNA molecules is essential in order to better understand their mechanism of action. In this report, our aim was to use E. coli RNase II as a model to compare two different techniques for the characterization and interpretation of the stability of RNA-protein complexes: Surface Plasmon Resonance and Electrophoretic Mobility Shift Assay.
Matos
Rute G
RG
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Apartado 127, 2781-901 Oeiras, Portugal.
Barbas
Ana
A
Arraiano
Cecília M
CM
D004229:Dithiothreitol; D024202:Electrophoretic Mobility Shift Assay / Q000379:methods*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism; D005095:Exoribonucleases / Q000737:chemistry* / Q000378:metabolism; D007700:Kinetics; D046911:Macromolecular Substances / Q000737:chemistry* / Q000378:metabolism; D009690:Nucleic Acid Conformation; D012313:RNA / Q000737:chemistry* / Q000378:metabolism; D020349:Surface Plasmon Resonance / Q000379:methods*; D013696:Temperature
D029968:Escherichia coli Proteins; D046911:Macromolecular Substances; D012313:RNA; D005095:Exoribonucleases; C022535:exoribonuclease II; D004229:Dithiothreitol