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Lia, G, Praly, E, Ferreira, H, Stockdale, C, Tse-Dinh, YC, Dunlap, D, Croquette, V, Bensimon, D and Owen-Hughes, T (2006) Direct observation of DNA distortion by the RSC complex. Mol. Cell 21:417-25


The Snf2 family represents a functionally diverse class of ATPase sharing the ability to modify DNA structure. Here, we use a magnetic trap and an atomic force microscope to monitor the activity of a member of this class: the RSC complex. This enzyme caused transient shortenings in DNA length involving translocation of typically 400 bp within 2 s, resulting in the formation of a loop whose size depended on both the force applied to the DNA and the ATP concentration. The majority of loops then decrease in size within a time similar to that with which they are formed, suggesting that the motor has the ability to reverse its direction. Loop formation was also associated with the generation of negative DNA supercoils. These observations support the idea that the ATPase motors of the Snf2 family of proteins act as DNA translocases specialized to generate transient distortions in DNA structure.


PubMed PMC3443744 Online version:10.1016/j.molcel.2005.12.013


Adenosine Triphosphatases/metabolism; DNA/chemistry; DNA/metabolism; DNA/ultrastructure; DNA Topoisomerases/metabolism; DNA, Superhelical/chemistry; DNA, Superhelical/metabolism; DNA-Binding Proteins/metabolism; Macromolecular Substances; Microscopy, Atomic Force; Nucleic Acid Conformation; Saccharomyces cerevisiae Proteins/metabolism; Stress, Mechanical; Transcription Factors/metabolism



Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status



GO:0015616: DNA translocase activity

ECO:0000314: direct assay evidence used in manual assertion


Seeded From UniProt


See also


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