Oligomerization of the Response Regulator ComE from Streptococcus mutans Is Affected by Phosphorylation
Oligomerization of the Response Regulator ComE from Streptococcus mutans Is Affected by Phosphorylation
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DOI：
10.1128/jb.06565-11
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发表时间：
2012-03-01
影响因子：
3.2
通讯作者：
Goodman, Steven D.
中科院分区：
文献类型：
--
作者：
Hung, David C. I.;Downey, Jennifer S.;Goodman, Steven D.
我们之前通过 DNase I 足迹和电泳迁移率变动分析分析了变形链球菌响应调节因子 ComE 与 DNA 结合位点之间的相互作用。由于反应调节器功能经常受到磷酸化状态的影响，我们研究了磷酸化如何影响 ComE 的生化功能。与许多反应调节剂不同，我们发现 ComE 的磷酸化状态不太可能在 DNA 结合亲和力中发挥作用，但似乎会诱导蛋白质寡聚形式的形成。讨论了这种寡聚状态对于 ComE 功能的作用。
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.