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Updated: Jun 14, 2026

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
Published on: September 2, 2019
Multiple moonlighting functions of mycobacterial molecular chaperones
Brian Henderson1, Peter A Lund, Anthony R M Coates
1Department of Microbial Diseases, UCL-Eastman Dental Institute, University College London, 256 Gray's Inn Road, London WC1X 8LD, United Kingdom. b.henderson@eastman.ucl.ac.uk <b.henderson@eastman.ucl.ac.uk>
None:
Molecular chaperones and protein folding catalysts are normally thought of as intracellular proteins involved in protein folding quality control. However, in the mycobacteria there is increasing evidence to support the hypothesis that molecular chaperones are also secreted intercellular signalling molecules or can control actions at the cell wall or indeed control the composition of the cell wall. The most recent evidence for protein moonlighting in the mycobacteria is the report that chaperonin 60.2 of Mycobacterium tuberculosis is important in the key event in tuberculosis - the entry of the bacterium into the macrophage. This brief overview highlights the potential importance of the moonlighting functions of molecular chaperones in the biology and pathobiology of the mycobacteria.
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