Revealing the base pair stepping dynamics of nucleic acid motor proteins with optical traps.
Nearly all aspects of nucleic acid metabolism involve motor proteins. This diverse group of enzymes, which includes DNA and RNA polymerases, the ribosome, helicases, and other translocases, converts chemical energy in the form of bond hydrolysis into concerted motion along nucleic acid filaments. The direct observation of this motion at its fundamental distance scale of one base pair has required the development of new ultrasensitive techniques. Recent advances in optical traps have now made these length scales, once the exclusive realm of crystallographic techniques, accessible. Several new studies using optical traps have revealed for the first time how motor proteins translocate along their substrates in a stepwise fashion. Though these techniques have only begun to be applied to biological problems, the unprecedented access into nucleic acid motor protein movement has already provided important insights into their mechanism. In this perspective, we review these advances and offer our view on the future of this exciting development.
Department of Physics, Center for the Physics of Living Cells, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA. ychemla@illinois.edu
Yann R
YR
Chemla
D020029:Base Pairing; D004247:DNA / Q000737:chemistry*; D004265:DNA Helicases / Q000737:chemistry / Q000235:genetics; D012321:DNA-Directed RNA Polymerases / Q000737:chemistry / Q000235:genetics; D007700:Kinetics; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000235:genetics; D014176:Protein Biosynthesis; D012313:RNA / Q000737:chemistry*; D020365:RNA Helicases / Q000737:chemistry / Q000235:genetics; D014158:Transcription, Genetic
D020409:Molecular Motor Proteins; D012313:RNA; D004247:DNA; D012321:DNA-Directed RNA Polymerases; D004265:DNA Helicases; D020365:RNA Helicases