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

Ilya J. Finkelstein, Mari-Liis Visnapuu and Eric C. Greene ()
Additional contact information
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

Nature, 2010, vol. 468, issue 7326, 983-987

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.

Date: 2010
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/nature09561 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:468:y:2010:i:7326:d:10.1038_nature09561

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature09561

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().