Control of A Multisubunit DNA Motor by a Thermoresponsive Polymer Switch

• Published in: Journal of the American Chemical Society Vol. 126; no. 41; pp. 13208 - 13209
• Main Authors: Pennadam, Sivanand S, Lavigne, Matthieu D, Dutta, Christina F, Firman, Keith, Mernagh, Darren, Górecki, Dariusz C, Alexander, Cameron
• Format: Journal Article
• Language: English
• Published: WASHINGTON American Chemical Society 20.10.2004; Amer Chemical Soc
• Subjects: Acrylic Resins - chemistry; Analytical, structural and metabolic biochemistry; Bacterial Proteins - chemistry; Binding Sites; Biological and medical sciences; Biomimetic Materials - chemistry; Chemistry; Chemistry, Multidisciplinary; Deoxyribonucleases, Type I Site-Specific - chemistry; DNA - chemistry; DNA Methylation; DNA Restriction-Modification Enzymes - chemistry; Dna, deoxyribonucleoproteins; Electrophoresis, Polyacrylamide Gel; Fundamental and applied biological sciences. Psychology; Hot Temperature; Nucleic acids; Physical Sciences; Protein Subunits; Science & Technology; CLEAVAGE SITES; LIGAND; ENZYME-ACTIVITY; RESTRICTION-ENDONUCLEASE ECOR124I; Sequence specificity; Chemical modification; Biochemical analysis; Sample preparation; Gel electrophoresis; DNA; Aliphatic polymer; Molecular recognition; Qualitative analysis; Acrylamide derivative polymer
• ISSN: 0002-7863; 1520-5126
• DOI: 10.1021/ja045275j

The conjugation of thermoresponsive polymers to multisubunit, multifunctional hybrid type 1 DNA restriction−modification (R−M) enzymes enables temperature-controlled “switching” of DNA methylation by the conjugate. Polymers attached to the enzyme at a subunit distal to the methylation subunit allow retention of DNA recognition and ATPase activity while controlling methylation of plasmid DNA. This regulation of enzyme activity arises from the coil−globule phase transitions of the polymer as shown in light scattering and gel retardation assays.