Oligomerization of the response regulator ComE from Streptococcus mutans is affected by phosphorylation.
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.
Division of Biomedical Science, Herman Ostrow School of Dentistry of University of Southern California, Los Angeles, California, USA.
David C I
DC
Hung
Jennifer S
JS
Downey
Jens
J
Kreth
Fengxia
F
Qi
Wenyuan
W
Shi
Dennis G
DG
Cvitkovitch
Steven D
SD
Goodman
D001426:Bacterial Proteins / Q000378:metabolism*; D004269:DNA, Bacterial / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism*; D010766:Phosphorylation; D011485:Protein Binding; D055503:Protein Multimerization; D013295:Streptococcus mutans / Q000378:metabolism*
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D004268:DNA-Binding Proteins