核糖体相关的大肠杆菌EngA的GTPase活性和细胞功能中两个G结构域的协同和关键作用。
Cooperative and critical roles for both G domains in the GTPase activity and cellular function of ribosome-associated Escherichia coli EngA.
作者信息
Bharat Amrita, Jiang Mengxi, Sullivan Susan M, Maddock Janine R, Brown Eric D
机构信息
Antimicrobial Research Centre, Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario L8N 3Z5, Canada.
出版信息
J Bacteriol. 2006 Nov;188(22):7992-6. doi: 10.1128/JB.00959-06. Epub 2006 Sep 8.
Abstract
To probe the cellular phenotype and biochemical function associated with the G domains of Escherichia coli EngA (YfgK, Der), mutations were created in the phosphate binding loop of each. Neither an S16A nor an S217A variant of G domain 1 or 2, respectively, was able to support growth of an engA conditional null. Polysome profiles of EngA-depleted cells were significantly altered, and His(6)-EngA was found to cofractionate with the 50S ribosomal subunit. The variants were unable to complement the abnormal polysome profile and were furthermore significantly impacted with respect to in vitro GTPase activity. Together, these observations suggest that the G domains have a cooperative function in ribosome stability and/or biogenesis.
摘要
为探究与大肠杆菌EngA（YfgK，Der）的G结构域相关的细胞表型和生化功能，在每个结构域的磷酸结合环中引入了突变。G结构域1或2的S16A变体和S217A变体分别均无法支持engA条件性缺失菌株的生长。EngA缺失细胞的多核糖体图谱发生了显著改变，并且发现His(6)-EngA与50S核糖体亚基共分离。这些变体无法弥补异常的多核糖体图谱，并且其体外GTPase活性也受到显著影响。这些观察结果共同表明，G结构域在核糖体稳定性和/或生物发生中具有协同功能。
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