Helicases are a class of nucleic acid (NA) motors that catalyze NTP-dependent unwinding of NA duplexes into single strands, a reaction essential to all areas of NA metabolism. In the last decade, single-molecule (sm) technology has proven to be highly useful in revealing mechanistic insight into helicase activity that is not always detectable via ensemble assays. A combination of methods based on fluorescence, optical and magnetic tweezers, and flow-induced DNA stretching has enabled the study of helicase conformational dynamics, force generation, step size, pausing, reversal and repetitive behaviors during translocation and unwinding by helicases working alone and as part of multiprotein complexes. The contributions of these sm investigations to our understanding of helicase mechanism and function will be discussed.
|Number of pages
|Quarterly reviews of biophysics
|Published - May 2010
- ESCHERICHIA-COLI UVRD, DEAD BOX HELICASE, ATP-DEPENDENT TRANSLOCATION, STRANDED-DNA TRANSLOCATION, NUCLEIC-ACID TRANSLOCASES, LOADING PROTEIN GP59, VIRUS NS3 HELICASE, PCRA HELICASE, POLYMERASE GP43, REPLICATION FORK