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The role of the tata-binding protein in the assembly and function of the multisubunit yeast rna polymerase-iii transcription factor, tfiiib

Academic Article
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Overview

authors

  • Kassavetis, G. A.
  • Joazeiro, Claudio Antonio
  • Pisano, M.
  • Geiduschek, E. P.
  • Colbert, T.
  • Hahn, S.
  • Blanco, J. A.

publication date

  • December 1992

journal

  • Cell  Journal

abstract

  • The Saccharomyces cerevisiae RNA polymerase III transcription factor (TF)IIIB has been assembled from three components. An assembly pathway of these polypeptides, which specifies their interactions, has been determined. The TATA-binding protein, TBP, and the TFIIB-related BRF1 gene product BRF, together reconstitute the transcription factor activity and TFIIC-dependent DNA-binding activity of the B' component of TFIIIB. BRF alone weakly binds to a TFIIIC-tRNA gene complex; TBP greatly stabilizes this interaction. B" transcription factor activity is recovered with its previously identified 90 kd polypeptide from SDS-polyacrylamide gels. Incorporation of the 90 kd B" protein into the transcription complex requires TBP. The heparin-resistant TFIIIB-DNA complex retains all three of its constituent proteins, TBP, BRF, and B".

subject areas

  • Base Sequence
  • DNA-Binding Proteins
  • Molecular Sequence Data
  • Protein Conformation
  • Saccharomyces cerevisiae
  • TATA-Box Binding Protein
  • Transcription Factor TFIIIB
  • Transcription Factors
  • Transcription, Genetic
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Identity

International Standard Serial Number (ISSN)

  • 0092-8674

Digital Object Identifier (DOI)

  • 10.1016/0092-8674(92)90399-w

PubMed ID

  • 1458536
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Additional Document Info

start page

  • 1055

end page

  • 1064

volume

  • 71

issue

  • 6

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