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Single-molecule imaging reveals mechanisms of protein disruption by a DNA translocase

Author

Listed:
  • Ilya J. Finkelstein

    (Columbia University)

  • Mari-Liis Visnapuu

    (Columbia University)

  • Eric C. Greene

    (Howard Hughes Medical Institute, Columbia University, New York, New York 10032, USA
    Columbia University)

Abstract

DNA translocase in action Protein machineries that move along the DNA, such as DNA polymerases and helicases, will necessarily encounter other bound proteins interacting with specific sites. Using nanofabricated 'curtains' of labelled DNA, Finkelstein et al. set out to establish whether such bound proteins interfere with the activity of the bacterial DNA translocase RecBCD. They find that the enzyme is remarkably robust and can push proteins over non-specific sites for thousands of base pairs before they are displaced.

Suggested Citation

  • Ilya J. Finkelstein & Mari-Liis Visnapuu & Eric C. Greene, 2010. "Single-molecule imaging reveals mechanisms of protein disruption by a DNA translocase," Nature, Nature, vol. 468(7326), pages 983-987, December.
    • Handle: RePEc:nat:nature:v:468:y:2010:i:7326:d:10.1038_nature09561
    DOI: 10.1038/nature09561
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    Cited by:

    1. Jin Qian & Allison Cartee & Wenxuan Xu & Yan Yan & Bing Wang & Irina Artsimovitch & David Dunlap & Laura Finzi, 2024. "Reciprocating RNA Polymerase batters through roadblocks," Nature Communications, Nature, vol. 15(1), pages 1-11, December.

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