Studying protein-DNA interactions using atomic force microscopy.

Autor: Beckwitt EC; Program in Molecular Biophysics and Structural Biology, University of Pittsburgh, Pittsburgh, PA 15261, USA; The University of Pittsburgh Cancer Institute, Hillman Cancer Center, Pittsburgh, PA 15213, USA., Kong M; Program in Molecular Biophysics and Structural Biology, University of Pittsburgh, Pittsburgh, PA 15261, USA; The University of Pittsburgh Cancer Institute, Hillman Cancer Center, Pittsburgh, PA 15213, USA., Van Houten B; Program in Molecular Biophysics and Structural Biology, University of Pittsburgh, Pittsburgh, PA 15261, USA; The University of Pittsburgh Cancer Institute, Hillman Cancer Center, Pittsburgh, PA 15213, USA; Department of Pharmacology and Chemical Biology, University of Pittsburgh, Pittsburgh, PA 15261, USA. Electronic address: vanhoutenb@upmc.edu.
Jazyk: angličtina
Zdroj: Seminars in cell & developmental biology [Semin Cell Dev Biol] 2018 Jan; Vol. 73, pp. 220-230. Date of Electronic Publication: 2017 Jun 30.
DOI: 10.1016/j.semcdb.2017.06.028
Abstrakt: Atomic force microscopy (AFM) has made significant contributions to the study of protein-DNA interactions by making it possible to topographically image biological samples. A single protein-DNA binding reaction imaged by AFM can reveal protein binding specificity and affinity, protein-induced DNA bending, and protein binding stoichiometry. Changes in DNA structure, complex conformation, and cooperativity, can also be analyzed. In this review we highlight some important examples in the literature and discuss the advantages and limitations of these measurements. We also discuss important advances in technology that will facilitate the progress of AFM in the future.
(Copyright © 2017 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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