全长的1组细菌σ因子采用与DNA结合不相容的紧密结构。
A full-length group 1 bacterial sigma factor adopts a compact structure incompatible with DNA binding.
作者信息
Schwartz Edmund C, Shekhtman Alexander, Dutta Kaushik, Pratt Matthew R, Cowburn David, Darst Seth, Muir Tom W
机构信息
Laboratory of Synthetic Protein Chemistry, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
出版信息
Chem Biol. 2008 Oct 20;15(10):1091-103. doi: 10.1016/j.chembiol.2008.09.008.
Abstract
The sigma factors are the key regulators of bacterial transcription initiation. Through direct read-out of promoter DNA sequence, they recruit the core RNA polymerase to sites of initiation, thereby dictating the RNA polymerase promoter-specificity. The group 1 sigma factors, which direct the vast majority of transcription initiation during log phase growth and are essential for viability, are autoregulated by an N-terminal sequence known as sigma1.1. We report the solution structure of Thermotoga maritima sigmaA sigma1.1. We additionally demonstrate by using chemical crosslinking strategies that sigma1.1 is in close proximity to the promoter recognition domains of sigmaA. We therefore propose that sigma1.1 autoinhibits promoter DNA binding of free sigmaA by stabilizing a compact organization of the sigma factor domains that is unable to bind DNA.
摘要
σ因子是细菌转录起始的关键调节因子。通过直接读取启动子DNA序列，它们将核心RNA聚合酶招募到起始位点，从而决定RNA聚合酶的启动子特异性。第1组σ因子在对数期生长期间指导绝大多数转录起始，并且对于生存力至关重要，它由一个称为σ1.1的N端序列进行自动调节。我们报道了嗜热栖热菌σA σ1.1的溶液结构。我们还通过化学交联策略证明，σ1.1与σA的启动子识别结构域紧密相邻。因此，我们提出σ1.1通过稳定无法结合DNA的σ因子结构域的紧密组织来自动抑制游离σA与启动子DNA的结合。
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