Architectural proteins play a key role in the folding, organization and compaction of genomic DNA in all organisms. By bending, bridging or wrapping DNA, these proteins ensure that its effective volume is reduced sufficiently to fit inside the cell or a dedicated cellular organelle, the nucleus (in bacteria/archaea and in eukaryotes respectively). In addition, the properties of many of these proteins permit them to play specific roles as architectural cofactors in a large variety of DNA transactions. However, as architectural proteins often bind DNA with low sequence specificity and affinity, it is hard to investigate their interaction using biochemical ensemble techniques. Single-molecule micromanipulation approaches that probe the properties of DNA-binding proteins by pulling on individual protein–DNA complexes have, in this respect, proved to be a very powerful alternative. Besides revealing architectural properties, these approaches can also reveal unique parameters not accessible to biochemical approaches, such as the binding kinetics and unbinding forces of individual proteins.
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August 2008
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Conference Article|
July 22 2008
Single-molecule micromanipulation studies of DNA and architectural proteins
Remus Th. Dame
Remus Th. Dame
1
1Department of Physics and Astronomy and Laser Centre, VU University Amsterdam, Amsterdam, The Netherlands
1email [email protected]
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Publisher: Portland Press Ltd
Received:
February 19 2008
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2008 Biochemical Society
2008
Biochem Soc Trans (2008) 36 (4): 732–737.
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Received:
February 19 2008
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Remus Th. Dame; Single-molecule micromanipulation studies of DNA and architectural proteins. Biochem Soc Trans 1 August 2008; 36 (4): 732–737. doi: https://doi.org/10.1042/BST0360732
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