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

J Am Chem Soc. 2009 May 13;131(18):6346-7. doi: 10.1021/ja9013634.

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.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • DNA, Single-Stranded / metabolism
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism
  • Magnetic Resonance Spectroscopy / methods*
  • Phosphorylation
  • Protein Binding
  • Protein Conformation
  • Replication Protein A / chemistry*
  • Replication Protein A / metabolism

Substances

  • DNA, Single-Stranded
  • DNA-Binding Proteins
  • Replication Protein A

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