Proteins of the MucR/Ros family play a crucial role in bacterial infection or symbiosis with eukaryotic hosts. MucR from plays a regulatory role in establishing symbiosis with the host plant, both dependent and independent of Quorum Sensing. Here, we report the first characterization of MucR isolated from by mass spectrometry and demonstrate that this protein forms higher-order oligomers in its native condition of expression by SEC-MALS.
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