Single-molecule Approaches to Probe the Structure, Kinetics, and Thermodynamics of Nucleoprotein Complexes That Regulate Transcription

• Type of Material: Article
• Authors: Laura Finzi, Emory University; David Dunlap, Emory University
• Language: English
• Date: 2010-06-18
• Publisher: American Society for Biochemistry and Molecular Biology
• Publication Version: Final Published Version
• Copyright Statement: © 2010 by The American Society for Biochemistry and Molecular Biology, Inc.
• Final Published Version (URL): http://www.jbc.org/content/285/25/18973
• Title of Journal or Parent Work: Journal of Biological Chemistry
• ISSN: 0021-9258
• Volume: 285
• Issue: 25
• Start Page: 18973
• End Page: 18978
• Grant/Funding Information: This work was supported, in whole or in part, by National Institutes of Health Grant RGM084070A (to L. F.).; This work was also supported by the Italian Funding of Basic Research (FIRB) (to L. F. and D. D. D.), the Human Frontier Science Program, and the Emory University Research Council.
• Keywords: DNA; DNA/Operators; DNA/Transcription; DNA-Protein Interaction; GENE/Regulation; Nucleic Acid/Structure; Biophysics/Single Molecule; Transcription/Regulation
• Research Categories: Biophysics, General; Chemistry, Biochemistry; Biology, Cell

Abstract

Single-molecule experimentation has contributed significantly to our understanding of the mechanics of nucleoprotein complexes that regulate epigenetic switches. In this minireview, we will discuss the application of the tethered-particle motion technique, magnetic tweezers, and atomic force microscopy to (i) directly visualize and thermodynamically characterize DNA loops induced by the lac, gal, and λ repressors and (ii) understand the mechanistic role of DNA-supercoiling and DNA-bending cofactors in both prokaryotic and eukaryotic systems.