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Roles of intrinsic disorder in protein-nucleic acid interactions

Academic Article
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Overview

authors

  • Dyson, Jane

publication date

  • 2012

journal

  • Molecular Biosystems  Journal

abstract

  • Interactions between proteins and nucleic acids typify the role of disordered segments, linkers, tails and other entities in the function of complexes that must form with high affinity and specificity but which must be capable of dissociating when no longer needed. While much of the emphasis in the literature has been on the interactions of disordered proteins with other proteins, disorder is also frequently observed in nucleic acids (particularly RNA) and in the proteins that interact with them. The interactions of disordered proteins with DNA most often manifest as molding of the protein onto the B-form DNA structure, although some well-known instances involve remodeling of the DNA structure that seems to require that the interacting proteins be disordered to various extents in the free state. By contrast, induced fit in RNA-protein interactions has been recognized for many years-the existence and prevalence of this phenomenon provides the clearest possible evidence that RNA and its interactions with proteins must be considered as highly dynamic, and the dynamic nature of RNA and its multiplicity of folded and unfolded states is an integral part of its nature and function.

subject areas

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Chromatin Assembly and Disassembly
  • Humans
  • Molecular Sequence Data
  • Nucleic Acids
  • Protein Binding
  • Protein Conformation
  • Protein Folding
  • Proteins
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Identity

PubMed Central ID

  • PMC3600845

International Standard Serial Number (ISSN)

  • 1742-206X

Digital Object Identifier (DOI)

  • 10.1039/c1mb05258f

PubMed ID

  • 21874205
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Additional Document Info

start page

  • 97

end page

  • 104

volume

  • 8

issue

  • 1

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