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C100567200v1
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Papers In Press, published online ahead of print October 17, 2001
J. Biol. Chem, 10.1074/jbc.C100567200
Submitted on October 1, 2001
Revised on October 13, 2001
Accepted on October 16, 2001

Identification of a conserved archaeal RNA polymerase subunit contacted by the basal transcription factor TFB

Christine P. Magill, Stephen P. Jackson, and Stephen D. Bell

MRC Cancer Cell Unit, Cambridge CB2 2XZ

Corresponding Author: sdb{at}mole.bio.cam.ac.uk

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 2-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).


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