Division of Biomedical Science, Herman Ostrow School of Dentistry of University of Southern California, Los Angeles, California, USA.
J Bacteriol. 2012 Mar;194(5):1127-35. doi: 10.1128/JB.06565-11. Epub 2011 Dec 30.
We have previously characterized the interactions of the response regulator ComE from Streptococcus mutans and DNA binding sites through DNase I footprinting and electrophoretic mobility shift assay analysis. Since response regulator functions are often affected by their phosphorylation state, we investigated how phosphorylation affects the biochemical function of ComE. Unlike many response regulators, we found that the phosphorylation state of ComE does not likely play a role in DNA binding affinity but rather seems to induce the formation of an oligomeric form of the protein. The role of this oligomerization state for ComE function is discussed.
我们之前通过 DNA 酶 I 足迹分析和电泳迁移率变动分析,对变形链球菌应答调节子 ComE 的相互作用和 DNA 结合位点进行了表征。由于应答调节子的功能通常受其磷酸化状态的影响,我们研究了磷酸化如何影响 ComE 的生化功能。与许多应答调节子不同,我们发现 ComE 的磷酸化状态不太可能影响 DNA 结合亲和力,而是似乎诱导蛋白质形成寡聚形式。本文讨论了这种寡聚状态对 ComE 功能的作用。