Stressed mycobacteria use the chaperone ClpB to sequester irreversibly oxidized proteins asymmetrically within and between cells.

@article{Vaubourgeix2015StressedMU,
  title={Stressed mycobacteria use the chaperone ClpB to sequester irreversibly oxidized proteins asymmetrically within and between cells.},
  author={Julien Vaubourgeix and Gang Lin and Neeraj Dhar and Nicolas Chenouard and Xiuju Jiang and H{\'e}l{\`e}ne Botella and Tania J. Lupoli and Olivia Mariani and Guangli Yang and Ouathek Ouerfelli and Michael Unser and Dirk Schnappinger and John D McKinney and Carl Nathan},
  journal={Cell host & microbe},
  year={2015},
  volume={17 2},
  pages={178-90}
}
Mycobacterium tuberculosis (Mtb) defends itself against host immunity and chemotherapy at several levels, including the repair or degradation of irreversibly oxidized proteins (IOPs). To investigate how Mtb deals with IOPs that can neither be repaired nor degraded, we used new chemical and biochemical probes and improved image analysis algorithms for time-lapse microscopy to reveal a defense against stationary phase stress, oxidants, and antibiotics--the sequestration of IOPs into aggregates in… CONTINUE READING
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