A conserved structural module regulates transcriptional responses to diverse stress signals in bacteria
A conserved structural module regulates transcriptional responses to diverse stress signals in bacteria
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DOI：
10.1016/j.molcel.2007.07.009
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发表时间：
2007-09-07
期刊：
影响因子：
16
通讯作者：
Darst, Seth A.
中科院分区：
文献类型：
--
作者：
Campbell, Elizabeth A.;Greenwell, Roger;Darst, Seth A.
球形红杆菌中对单线态氧的转录反应由 IV 族 sigma 因子 sigma(E) 及其同源抗 sigma ChrR 控制。 sigma(E)/ChrR 复合物的晶体结构揭示了 ChrR 的模块化、两域结构。 ChrR N 端反 sigma 结构域 (ASID) 结合 Zn2+ 离子，接触 sigma(E)，并足以抑制 sigma(E) 依赖性转录。 ChrR C 末端结构域采用 cupin 折叠，可以协调额外的 Zn2+，并且是对单线态氧的转录反应所必需的。基于结构的序列分析预测 ASID 定义了预测的 IV 组 antias 中的共同结构折叠。这些 ASD 与不同的 C 端结构域融合，这些结构域可能参与响应控制其同源 sigma 因子活性的特定环境信号。
A transcriptional response to singlet oxygen in Rhodobacter sphaeroides is controlled by the group IV sigma factor sigma(E) and its cognate anti-sigma ChrR. Crystal structures of the sigma(E)/ChrR complex reveal a modular, two-domain architecture for ChrR. The ChrR N-terminal anti-sigma domain (ASID) binds a Zn2+ ion, contacts sigma(E), and is sufficient to inhibit sigma(E)-dependent transcription. The ChrR C-terminal domain adopts a cupin fold, can coordinate an additional Zn2+, and is required for the transcriptional response to singlet oxygen. Structure-based sequence analyses predict that the ASID defines a common structural fold among predicted group IV antias. These ASDs are fused to diverse C-terminal domains that are likely involved in responding to specific environmental signals that control the activity of their cognate sigma factor.