NMR analysis of the architecture and functional remodeling of a modular multidomain protein, RPA.

Brosey CA, Chagot ME, Ehrhardt M, Pretto DI, Weiner BE, Chazin WJ
J Am Chem Soc. 2009 131 (18): 6346-7

PMID: 19378948 · PMCID: PMC2711642 · DOI:10.1021/ja9013634

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.

MeSH Terms (7)

DNA, Single-Stranded DNA-Binding Proteins Magnetic Resonance Spectroscopy Phosphorylation Protein Binding Protein Conformation Replication Protein A

Connections (1)

This publication is referenced by other Labnodes entities:

Links