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

D Richard, SD Bell, Malcolm Frederick White

Research output: Contribution to journalArticlepeer-review

44 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)1065-1074
Number of pages10
JournalNucleic Acids Research
Volume32
Issue number3
DOIs
Publication statusPublished - Feb 2004

Keywords

  • TRANSCRIPTION PREINITIATION COMPLEX
  • SULFOLOBUS-SHIBATAE
  • FACTOR REQUIREMENTS
  • CHROMATIN PROTEIN
  • CRYSTAL-STRUCTURE
  • REPLICATION
  • INITIATION
  • BOX
  • IDENTIFICATION
  • RECOGNITION

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