Single-molecule views of protein movement on single-stranded DNA

Taekjip Ha, Alexander G. Kozlov, Timothy M. Lohman

Research output: Contribution to journalReview articlepeer-review


The advent of new technologies allowing the study of single biological molecules continues to have a major impact on studies of interacting systems as well as enzyme reactions. These approaches (fluorescence, optical, and magnetic tweezers), in combination with ensemble methods, have been particularly useful for mechanistic studies of proteinnucleic acid interactions and enzymes that function on nucleic acids. We review progress in the use of single-molecule methods to observe and perturb the activities of proteins and enzymes that function on flexible single-stranded DNA. These include single-stranded DNA binding proteins, recombinases (RecARad51), and helicasestranslocases that operate as motor proteins and play central roles in genome maintenance. We emphasize methods that have been used to detect and study the movement of these proteins (both ATP-dependent directional and random movement) along the single-stranded DNA and the mechanistic and functional information that can result from detailed analysis of such movement.

Original languageEnglish (US)
Pages (from-to)295-319
Number of pages25
JournalAnnual Review of Biophysics
Issue number1
StatePublished - Jun 9 2012


  • FRET
  • Helicases
  • Optical tweezers
  • Rad51
  • RecA
  • SSB

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Bioengineering
  • Biochemistry
  • Cell Biology


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