Control of a multisubunit DNA motor by a thermoresponsive polymer switch

Sivanand S Pennadam; Matthieu D Lavigne; Christina F Dutta; Keith Firman; Darren Mernagh; Dariusz C Górecki; Cameron Alexander

doi:10.1021/ja045275j

Control of a multisubunit DNA motor by a thermoresponsive polymer switch

J Am Chem Soc. 2004 Oct 20;126(41):13208-9. doi: 10.1021/ja045275j.

Authors

Sivanand S Pennadam¹, Matthieu D Lavigne, Christina F Dutta, Keith Firman, Darren Mernagh, Dariusz C Górecki, Cameron Alexander

Affiliation

¹ School of Pharmacy and Biomedical Sciences, Institute of Biomedical and Biomolecular Sciences, University of Portsmouth, Portsmouth PO1 2DT, United Kingdom.

PMID: 15479059
DOI: 10.1021/ja045275j

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Acrylic Resins / chemistry*
Bacterial Proteins / chemistry
Binding Sites
Biomimetic Materials / chemistry
DNA / chemistry*
DNA Methylation
DNA Restriction-Modification Enzymes / chemistry
Deoxyribonucleases, Type I Site-Specific / chemistry*
Electrophoresis, Polyacrylamide Gel
Hot Temperature
Protein Subunits

Substances

Acrylic Resins
Bacterial Proteins
DNA Restriction-Modification Enzymes
Protein Subunits
poly-N-isopropylacrylamide
DNA
HsdM protein, Bacteria
endodeoxyribonuclease EcoR124I
Deoxyribonucleases, Type I Site-Specific