Stretching DNA and RNA to probe their interactions with proteins.
When interacting with a single stretched DNA, many proteins modify its end-to-end distance. This distance can be monitored in real time using various micromanipulation techniques that were initially used to determine the elastic properties of bare nucleic acids and their mechanically induced structural transitions. These methods are currently being applied to the study of DNA enzymes such as DNA and RNA polymerases, topoisomerases and structural proteins such as RecA. They permit the measurement of the probability distributions of the rate, processivity, on-time, affinity and efficiency for a large variety of DNA-based molecular motors.
Allemand
Jean-François
JF
Ecole Normale Supérieure, Laboratoire de Physique Statistique, 24 rue Lhomond, 75005, Paris, France.
Bensimon
David
D
Croquette
Vincent
V
D004247:DNA / Q000737:chemistry* / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry*; D007535:Isomerases / Q000737:chemistry*; D008846:Micromanipulation; D018625:Microscopy, Atomic Force; D009690:Nucleic Acid Conformation; D009713:Nucleotidyltransferases / Q000737:chemistry*
D004268:DNA-Binding Proteins; D004247:DNA; D009713:Nucleotidyltransferases; D007535:Isomerases