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Published online 10 February 2004

Nucleic Acids Research, 2004, Vol. 32, No. 3 1065-1074
© 2004 Oxford University Press

Physical and functional interaction of the archaeal single-stranded DNA-binding protein SSB with RNA polymerase

Derek J. Richard, Stephen D. Bell1 and Malcolm F. White*

Centre for Biomolecular Sciences, University of St Andrews, North Haugh, St Andrews, Fife KY16 9ST, UK and 1 MRC Cancer Cell Unit, Hutchison MRC Centre, Hills Road, Cambridge CB2 2XZ, UK

*To whom correspondence should be addressed. Tel: +44 1334 463432; Fax: +44 1334 462595; Email: mfw2{at}st-andrews.ac.uk

Archaeal transcription utilizes a complex multisubunit RNA polymerase and the basal transcription factors TBP and TF(II)B, closely resembling its eukaryal counterpart. We have uncovered a tight physical and functional interaction between RNA polymerase and the single-stranded DNA-binding protein SSB in Sulfolobus solfataricus. SSB stimulates transcription from promoters in vitro under TBP-limiting conditions and supports transcription in the absence of TBP. SSB also rescues transcription from repression by reconstituted chromatin. We demonstrate the potential for promoter melting by SSB, suggesting a plausible basis for the stimulation of transcription. This stimulation requires both the single-stranded DNA-binding domain and the acidic C-terminal tail of the SSB. The tail forms a stable interaction with RNA polymerase. These data reveal an unexpected role for single-stranded DNA-binding proteins in transcription in archaea.


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