Abstract
Archaea possess two general transcription factors that are required to recruit RNA polymerase (RNAP) to promoters in vitro. These are TBP, the TATA-box-binding protein and TFB, the archaeal homologue of TFIIB. Thus, the archaeal and eucaryal transcription machineries are fundamentally related. In both RNAP II and archaeal transcription systems, direct contacts between TFB/TFIIB and the RNAP have been demonstrated to mediate recruitment of the polymerase to the promoter. However the subunit(s) directly contacted by these factors has not been identified. Using systematic yeast two-hybrid and biochemical analyses we have identified an interaction between the N-terminal domain of TFB and an evolutionarily conserved subunit of the RNA polymerase, RpoK. Intriguingly, homologues of RpoK are found in all three nuclear RNA polymerases (Rpb6) and also in the bacterial RNA polymerase (omega-subunit).
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Archaea / enzymology*
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Archaeal Proteins / biosynthesis*
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Archaeal Proteins / chemistry*
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Archaeal Proteins / genetics
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DNA-Directed RNA Polymerases / biosynthesis*
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DNA-Directed RNA Polymerases / chemistry*
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DNA-Directed RNA Polymerases / genetics
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DNA-Directed RNA Polymerases / metabolism
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Molecular Sequence Data
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Nuclear Proteins / chemistry*
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Nuclear Proteins / genetics
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Nuclear Proteins / metabolism*
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Plasmids / metabolism
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Point Mutation
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Promoter Regions, Genetic
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Protein Binding
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Protein Structure, Tertiary
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Sequence Homology, Amino Acid
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Transcription Factor TFIIB*
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Transcription Factors / chemistry*
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Transcription Factors / genetics
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Transcription Factors / metabolism*
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Transcription, Genetic
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Two-Hybrid System Techniques
Substances
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Archaeal Proteins
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Nuclear Proteins
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Transcription Factor TFIIB
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Transcription Factors
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transcription factor B, Archaea
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RpoK protein, Sulfolobus solfataricus
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DNA-Directed RNA Polymerases