Work

NMR Analysis of the Architecture and Functional Remodeling of a Modular Multidomain Protein, RPA

Year: 2009

Type: article

Abstract: Modular proteins with multiple domains tethered by flexible linkers have variable global architectures. Using the eukaryotic ssDNA binding protein, Replication Protein A (RPA), we demonstrate that NMR spectroscopy is a powerful tool to characterize the remodeling of architecture in different functional states. The first direct evidence is obtained for the remodeling of RPA upon binding ssDNA, including an alteration in the availability of the RPA32N domain that may help explain its damage-dependent phosphorylation.

Source: Journal of the American Chemical Society

DOI: 10.1021/ja9013634

Authors: Chris A. Brosey, Marie-Eve Chagot, Mark Ehrhardt, Dalyir I. Pretto, Brian E. Weiner, Walter J. Chazin

Institution: Vanderbilt University

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Institutes of Health, National Cancer Institute, National Institute of General Medical Sciences, National Institute of Environmental Health Sciences