Atomic force microscopy of the EcoKI Type I DNA restriction enzyme bound to DNA shows enzyme dimerization and DNA looping

• Published in: Nucleic acids research Vol. 37; no. 6; pp. 2053 - 2063
• Main Authors: Neaves, Kelly J, Cooper, Laurie P, White, John H, Carnally, Stewart M, Dryden, David T.F, Edwardson, J. Michael, Henderson, Robert M
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 01.04.2009; Oxford Publishing Limited (England)
• Subjects: Adenosine Triphosphate - analogs & derivatives; Adenosine Triphosphate - metabolism; Binding Sites; Data Interpretation, Statistical; Dimerization; DNA - chemistry; DNA - metabolism; DNA - ultrastructure; DNA Restriction Enzymes - metabolism; DNA Restriction Enzymes - ultrastructure; Microscopy, Atomic Force; Nucleic Acid Enzymes; Protein Binding; Protein Multimerization; Site-Specific DNA-Methyltransferase (Adenine-Specific) - metabolism; Site-Specific DNA-Methyltransferase (Adenine-Specific) - ultrastructure

Atomic force microscopy (AFM) allows the study of single protein-DNA interactions such as those observed with the Type I Restriction-Modification systems. The mechanisms employed by these systems are complicated and understanding them has proved problematic. It has been known for years that these en...