The twenty-nine amino acid C-terminal cytoplasmic domain of poliovirus 3AB is critical for nucleic acid chaperone activity.

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  • Author(s): Gangaramani DR;Gangaramani DR; Eden EL; Shah M; Destefano JJ
  • Source:
    RNA biology [RNA Biol] 2010 Nov-Dec; Vol. 7 (6), pp. 820-9. Date of Electronic Publication: 2010 Nov 01.
  • Publication Type:
    Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Taylor & Francis Country of Publication: United States NLM ID: 101235328 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1555-8584 (Electronic) Linking ISSN: 15476286 NLM ISO Abbreviation: RNA Biol Subsets: MEDLINE
    • Publication Information:
      Publication: 2015- : Philadelphia, PA : Taylor & Francis
      Original Publication: Georgetown, TX : Landes Bioscience,
    • Subject Terms:
      Amino Acids/*metabolism ; Cytoplasm/*metabolism ; Membrane Proteins/*metabolism ; Molecular Chaperones/*metabolism ; Nucleic Acids/*metabolism ; Poliovirus/*metabolism ; Viral Nonstructural Proteins/*metabolism; Amino Acid Sequence ; Amino Acids/chemistry ; Base Sequence ; Membrane Proteins/chemistry ; Membrane Proteins/genetics ; Models, Biological ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; Poliovirus/genetics ; Protein Structure, Tertiary ; RNA-Binding Proteins/metabolism ; Viral Nonstructural Proteins/chemistry ; Viral Nonstructural Proteins/genetics ; Virus Replication/physiology
    • Abstract:
      Poliovirus 3AB protein is the first picornavirus protein demonstrated to have nucleic acid chaperone activity. Further characterization of 3AB demonstrates that the C-terminal 22 amino acids (3B region (also referred to as VPg), amino acid 88-109) of the protein is required for chaperone activity, as mutations in this region abrogate nucleic acid binding and chaperone function. Protein 3B alone has no chaperone activity as determined by established assays that include the ability to stimulate nucleic acid hybridization in a primer-template annealing assay, helix-destabilization in a nucleic acid unwinding assay, or aggregation of nucleic acids. In contrast, the putative 3AB C-terminal cytoplasmic domain (C terminal amino acids 81-109, 3B + the last 7 C-terminal amino acids of 3A, termed 3B+7 in this report) possesses strong activity in these assays, albeit at much higher concentrations than 3AB. The characteristics of several mutations in 3B+7 are described here, as well as a model proposing that 3B+7 is the site of the "intrinsic" chaperone activity of 3AB while the 3A N-terminal region (amino acids 1-58) and/or membrane anchor domain (amino acids 59-80) serve to increase the effective concentration of the 3B+7 region leading to the potent chaperone activity of 3AB.
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    • Grant Information:
      GM051140 United States GM NIGMS NIH HHS; United States HHMI Howard Hughes Medical Institute; R29 GM051140 United States GM NIGMS NIH HHS; R01 GM051140-16 United States GM NIGMS NIH HHS; R01 GM051140 United States GM NIGMS NIH HHS
    • Accession Number:
      0 (3AB protein, poliovirus)
      0 (Amino Acids)
      0 (Membrane Proteins)
      0 (Molecular Chaperones)
      0 (Nucleic Acids)
      0 (RNA-Binding Proteins)
      0 (Viral Nonstructural Proteins)
    • Publication Date:
      Date Created: 20101104 Date Completed: 20110713 Latest Revision: 20211020
    • Publication Date:
      20221213
    • Accession Number:
      PMC3072266
    • Accession Number:
      10.4161/rna.7.6.13781
    • Accession Number:
      21045553