(Q27640838)

2

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Jimin Wang

3

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E Peter Geiduschek

4

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Paul B Sigler

A universal nomenclature for subunits of the RNA polymerase III transcription initiation factor TFIIIB

5

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language of work or name

English

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publication date

3 April 2003

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published in

Nature

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volume

422

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issue

6931

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page(s)

534-9

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cites work

1 reference

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A cryptic DNA binding domain at the COOH terminus of TFIIIB70 affects formation, stability, and function of preinitiation complexes.

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Use of TLS parameters to model anisotropic displacements in macromolecular refinement

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The RNA polymerase III transcription apparatus

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Recruitment of RNA polymerase III to its target promoters

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Conserved functional domains of the RNA polymerase III general transcription factor BRF.

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Structure and function of a human transcription factor TFIIIB subunit that is evolutionarily conserved and contains both TFIIB- and high-mobility-group protein 2-related domains

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Complex interactions between yeast TFIIIB and TFIIIC.

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Functional and structural organization of Brf, the TFIIB-related component of the RNA polymerase III transcription initiation complex

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Eukaryotic transcription factor-DNA complexes.

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Crystal structure of yeast TATA-binding protein and model for interaction with DNA

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PHD: predicting one-dimensional protein structure by profile-based neural networks

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Solution Structure of the KIX Domain of CBP Bound to the Transactivation Domain of CREB: A Model for Activator:Coactivator Interactions

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Architecture of protein and DNA contacts within the TFIIIB-DNA complex

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Polymerase (Pol) III TATA box-binding protein (TBP)-associated factor Brf binds to a surface on TBP also required for activated Pol II transcription

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Regional codon randomization: defining a TATA-binding protein surface required for RNA polymerase III transcription

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A unified nomenclature for TATA box binding protein (TBP)-associated factors (TAFs) involved in RNA polymerase II transcription.

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Evidence that TAF-TATA box-binding protein interactions are required for activated transcription in mammalian cells

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Crystal structure of a yeast TFIIA/TBP/DNA complex

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Processing of X-ray diffraction data collected in oscillation mode

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[27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods.

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Mutagenesis of yeast TFIIIB70 reveals C-terminal residues critical for interaction with TBP and C34 1 1Edited by M. Yaniv

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A suppressor of mutations in the class III transcription system encodes a component of yeast TFIIIB

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