Stretching DNA and RNA to probe their interactions with proteins

Publication Type:

Journal Article

Source:

CURRENT OPINION IN STRUCTURAL BIOLOGY, CURRENT BIOLOGY LTD, Volume 13, Number 3, 84 THEOBALDS RD, LONDON WC1X 8RR, ENGLAND, p.266-274 (2003)

DOI:

10.1016/S0959-440X(03)00067-8

Keywords:

CHROMATIN FIBERS; COMPLEMENTARY STRANDS; DOUBLE HELIX; DOUBLE-STRANDED DNA; INDIVIDUAL NUCLEOSOMES; MECHANICAL FORCE; OPTICAL TWEEZERS; POLYMERASE; SINGLE-MOLECULE ANALYSIS; SUPERCOILED DNA

Abstract:

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.