Yoder-Himes Deborah R, Kroos Lee
Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA.
J Bacteriol. 2006 Jul;188(14):5167-76. doi: 10.1128/JB.00318-06.
The bacterium Myxococcus xanthus employs extracellular signals to coordinate aggregation and sporulation during multicellular development. Extracellular, contact-dependent signaling that involves the CsgA protein (called C-signaling) activates FruA, a putative response regulator that governs a branched signaling pathway inside cells. One branch regulates cell movement, leading to aggregation. The other branch regulates gene expression, leading to sporulation. C-signaling is required for full expression of most genes induced after 6 h into development, including the gene identified by Tn5 lac insertion Omega4400. To determine if FruA is a direct regulator of Omega4400 transcription, a combination of in vivo and in vitro experiments was performed. Omega4400 expression was abolished in a fruA mutant. The DNA-binding domain of FruA bound specifically to DNA upstream of the promoter -35 region in vitro. Mutations between bp -86 and -77 greatly reduced binding. One of these mutations had been shown previously to reduce Omega4400 expression in vivo and make it independent of C-signaling. For the first time, chromatin immunoprecipitation (ChIP) experiments were performed on M. xanthus. The ChIP experiments demonstrated that FruA is associated with the Omega4400 promoter region late in development, even in the absence of C-signaling. Based on these results, we propose that FruA directly activates Omega4400 transcription to a moderate level prior to C-signaling and, in response to C-signaling, binds near bp -80 and activates transcription to a higher level. Also, the highly localized effects of mutations between bp -86 and -77 on DNA binding in vitro, together with recently published footprints, allow us to predict a consensus binding site of GTCG/CGA/G for the FruA DNA-binding domain.
黄色粘球菌利用细胞外信号在多细胞发育过程中协调聚集和孢子形成。涉及CsgA蛋白的细胞外接触依赖性信号传导(称为C信号传导)激活FruA,FruA是一种假定的应答调节因子,在细胞内控制一条分支信号通路。一个分支调节细胞运动,导致聚集。另一个分支调节基因表达,导致孢子形成。C信号传导是发育6小时后诱导的大多数基因充分表达所必需的,包括通过Tn5 lac插入鉴定的Omega4400基因。为了确定FruA是否是Omega4400转录的直接调节因子,进行了体内和体外实验相结合的研究。在fruA突变体中,Omega4400表达被消除。FruA的DNA结合结构域在体外与启动子-35区域上游的DNA特异性结合。-86至-77碱基对之间的突变大大降低了结合。这些突变之一先前已被证明可在体内降低Omega4400表达并使其独立于C信号传导。首次对黄色粘球菌进行了染色质免疫沉淀(ChIP)实验。ChIP实验表明,即使在没有C信号传导的情况下,FruA在发育后期也与Omega4400启动子区域相关联。基于这些结果,我们提出FruA在C信号传导之前直接将Omega4400转录激活至中等水平,并响应C信号传导,在-80碱基对附近结合并将转录激活至更高水平。此外,-86至-77碱基对之间的突变对体外DNA结合的高度局部化影响,以及最近发表的足迹,使我们能够预测FruA DNA结合结构域的共有结合位点为GTCG/CGA/G。