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Molecular-basis for specific recognition of both RNA and DNA by a zinc finger protein

Academic Article
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Overview

authors

  • Clemens, K. R.
  • Wolf, V.
  • McBryant, S. J.
  • Zhang, P. H.
  • Liao, X. B.
  • Wright, Peter
  • Gottesfeld, Joel

publication date

  • April 1993

journal

  • Science  Journal

abstract

  • Transcription factor IIIA (TFIIIA) from Xenopus oocytes binds both the internal control region of the 5S ribosomal RNA genes and the 5S RNA transcript itself. The nucleic acid binding domain of TFIIIA contains nine tandemly repeated zinc finger motifs. A series of precisely truncated forms of this protein have been constructed and assayed for 5S RNA and DNA binding. Different sets of zinc fingers were found to be responsible for high affinity interactions with RNA and with DNA. These results explain how a single protein can exhibit equal affinities for these two very different nucleic acids.

subject areas

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • DNA
  • DNA-Binding Proteins
  • Female
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Oocytes
  • RNA, Ribosomal, 5S
  • Transcription Factor TFIIIA
  • Transcription Factors
  • Xenopus
  • Zinc Fingers
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Identity

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.8475383

PubMed ID

  • 8475383
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Additional Document Info

start page

  • 530

end page

  • 533

volume

  • 260

issue

  • 5107

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