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

机译:古细菌单链DNA结合蛋白SSB与RNA聚合酶的物理和功能相互作用

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摘要

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.
机译:古细菌转录利用复杂的多亚基RNA聚合酶和基础转录因子TBP和TF(II)B,与真核生物类似。我们发现了Sulfolobus solfataricus中的RNA聚合酶和单链DNA结合蛋白SSB之间紧密的物理和功能相互作用。 SSB在限制TBP的条件下体外刺激启动子的转录,并在不存在TBP的情况下支持转录。 SSB还通过重构的染色质从抑制中拯救转录。我们证明了SSB启动子融化的潜力,为转录的刺激提供了合理的依据。这种刺激既需要单链DNA结合结构域,又需要SSB的酸性C末端尾巴。尾巴与RNA聚合酶形成稳定的相互作用。这些数据揭示了单链DNA结合蛋白在古细菌转录中出乎意料的作用。

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