Revised subunit structure of yeast transcription factor IIH (TFIIH) and reconciliation with human TFIIH Journal Article


Authors: Takagi, Y.; Komori, H.; Chang, W. H.; Hudmon, A.; Erdjument-Bromage, H.; Tempst, P.; Kornberg, R. D.
Article Title: Revised subunit structure of yeast transcription factor IIH (TFIIH) and reconciliation with human TFIIH
Abstract: Tfb4 is identified as a subunit of the core complex of yeast RNA polymerase II general transcription factor IIH (TFIIH) by affinity purification, by peptide sequence analysis, and by expression of the entire complex in insect cells. Tfb3, previously identified as a component of the core complex, is shown instead to form a complex with cdk and cyclin subunits of TFIIH. This reassignment of subunits resolves a longstanding discrepancy between yeast and human TFIIH complexes.
Keywords: controlled study; protein expression; unclassified drug; sequence analysis; nonhuman; polymerase chain reaction; protein analysis; animal cell; animals; complex formation; gene expression; protein; transcription factor; animalia; genetic vectors; rna; amino acid sequence; molecular sequence data; recombinant fusion proteins; protein purification; saccharomyces cerevisiae; glutathione transferase; spodoptera; yeast; saccharomyces cerevisiae proteins; cycline; protein subunit; protein subunits; protein structure; structure analysis; cyclin-dependent kinases; cyclins; cyclin dependent kinase; rna polymerase ii; electrophoresis, polyacrylamide gel; transcription factor iih; transcription factor tfiih; spectrometry, mass, matrix-assisted laser desorption-ionization; polymers; insect cell; baculoviridae; tata-binding protein associated factors; transcription factor tfiid; transcription factors, tfii; insecta; humans; human; priority journal; article; affinity purification; protein tfb3; protein tfb4
Journal Title: Journal of Biological Chemistry
Volume: 278
Issue: 45
ISSN: 0021-9258
Publisher: American Society for Biochemistry and Molecular Biology  
Date Published: 2003-11-07
Start Page: 43897
End Page: 43900
Language: English
DOI: 10.1074/jbc.C300417200
PUBMED: 14500720
PROVIDER: scopus
DOI/URL:
Notes: Export Date: 12 September 2014 -- Source: Scopus
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  1. Paul J Tempst
    324 Tempst