Download MendeleyMycobacterium tuberculosisSatS is a chaperone for the SecA2 protein export pathway.
Miller, B.K., Hughes, R., Ligon, L.S., Rigel, N.W., Malik, S., Anjuwon-Foster, B.R., Sacchettini, J.C., Braunstein, M.(2019) Elife 8
- PubMed: 30604681
- DOI: https://doi.org/10.7554/eLife.40063
- Primary Citation of Related Structures:
6DNM, 6DRQ - PubMed Abstract:
The SecA2 protein export system is critical for the virulence of Mycobacterium tuberculosis . However, the mechanism of this export pathway remains unclear. Through a screen for suppressors of a secA2 mutant, we identified a new player in the mycobacterial SecA2 pathway that we named SatS for S ec A 2 ( t wo) S uppressor. In M. tuberculosis , SatS is required for the export of a subset of SecA2 substrates and for growth in macrophages. We further identify a role for SatS as a protein export chaperone. SatS exhibits multiple properties of a chaperone, including the ability to bind to and protect substrates from aggregation. Our structural studies of SatS reveal a distinct combination of a new fold and hydrophobic grooves resembling preprotein-binding sites of the SecB chaperone. These results are significant in better defining a molecular pathway for M. tuberculosis pathogenesis and in expanding our appreciation of the diversity among chaperones and protein export systems.
Organizational Affiliation:
Department of Microbiology and Immunology, University of North Carolina at Chapel Hill, North Carolina, United States.
