Insight into helicase mechanism and function revealed through single-molecule approaches

Research output: Contribution to journalReview articleContributedpeer-review

Contributors

  • Jaya G. Yodh - , University of Illinois at Urbana-Champaign (Author)
  • Michael Schlierf - , Chair of Molecular Biophysics, University of Illinois at Urbana-Champaign (Author)
  • Taekjip Ha - , Univ Illinois, Howard Hughes Medical Institute, University of Illinois System, University of Illinois Urbana-Champaign, Howard Hughes Med Inst (Author)

Abstract

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.

Details

Original languageEnglish
Pages (from-to)185-217
Number of pages33
JournalQuarterly reviews of biophysics
Volume43
Issue number2
Publication statusPublished - May 2010
Peer-reviewedYes

External IDs

Scopus 77957141376

Keywords

Keywords

  • 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