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Interaction of the RNA-binding fingers of Xenopus transcription factor IIIA with specific regions of 5-S ribosomal-RNA

Academic Article
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Overview

authors

  • McBryant, S. J.
  • Veldhoen, N.
  • Gedulin, B.
  • Leresche, A.
  • Foster, M. P.
  • Wright, Peter
  • Romaniuk, P. J.
  • Gottesfeld, Joel

publication date

  • April 1995

journal

  • Journal of Molecular Biology  Journal

abstract

  • Zinc fingers 4 to 7 of Xenopus transcription factor IIIA (TFIIIA) represent the minimal polypeptide necessary for high-affinity binding to 5 S RNA. Mutations covering the entire 5 S RNA structure have been compared for their effects on the binding affinity of full-length TFIIIA and a polypeptide consisting of fingers 4 to 7 of TFIIIA (zf4-7). In addition, ribonuclease footprinting was used to compare the binding sites of TFIIIA and zf4-7 on 5 S RNA. The consistency between the data obtained from these two approaches provided a clear indication that zinc fingers 4 to 7 of TFIIIA bind to a central core region on the 5 S RNA molecule consisting of loop B/helix II/loop A/helix V/region E. This information was used to design a truncated 75-nucleotide-long RNA molecule that retains high affinity for zf4-7. Therefore, we conclude that the specific interaction of TFIIIA with 5 S RNA can be represented by a complex formed between a four zinc finger polypeptide and a truncated 5 S RNA molecule.

subject areas

  • Animals
  • Base Sequence
  • Binding Sites
  • DNA Primers
  • DNA-Binding Proteins
  • Female
  • Helix-Loop-Helix Motifs
  • Kinetics
  • Molecular Sequence Data
  • Mutagenesis
  • Nucleic Acid Conformation
  • Oocytes
  • Polymerase Chain Reaction
  • RNA, Ribosomal, 5S
  • RNA-Binding Proteins
  • Templates, Genetic
  • Transcription Factor TFIIIA
  • Transcription Factors
  • Xenopus laevis
  • Zinc Fingers
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Research

keywords

  • 5 S RNA
  • PROTEIN
  • RNA
  • TFIIIA
  • ZINC FINGER PROTEIN
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Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1006/jmbi.1995.0201

PubMed ID

  • 7731045
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Additional Document Info

start page

  • 44

end page

  • 57

volume

  • 248

issue

  • 1

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