Oligomerization of the response regulator come from streptococcus mutans is affected by phosphorylation

David C.I. Hung, Jennifer S. Downey, Jens Kreth, Fengxia Qi, Wenyuan Shi, Dennis G. Cvitkovitch, Steven D. Goodman

Research output: Contribution to journalArticle

11 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)1127-1135
Number of pages9
JournalJournal of bacteriology
Volume194
Issue number5
DOIs
StatePublished - Mar 1 2012

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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    Hung, D. C. I., Downey, J. S., Kreth, J., Qi, F., Shi, W., Cvitkovitch, D. G., & Goodman, S. D. (2012). Oligomerization of the response regulator come from streptococcus mutans is affected by phosphorylation. Journal of bacteriology, 194(5), 1127-1135. https://doi.org/10.1128/JB.06565-11