Structural highlights
Publication Abstract from PubMed
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 SecA2 (two) Suppressor. 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.
Mycobacterium tuberculosis SatS is a chaperone for the SecA2 protein export pathway.,Miller BK, Hughes R, Ligon LS, Rigel NW, Malik S, Anjuwon-Foster BR, Sacchettini JC, Braunstein M Elife. 2019 Jan 3;8. pii: 40063. doi: 10.7554/eLife.40063. PMID:30604681[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Miller BK, Hughes R, Ligon LS, Rigel NW, Malik S, Anjuwon-Foster BR, Sacchettini JC, Braunstein M. Mycobacterium tuberculosis SatS is a chaperone for the SecA2 protein export pathway. Elife. 2019 Jan 3;8. pii: 40063. doi: 10.7554/eLife.40063. PMID:30604681 doi:http://dx.doi.org/10.7554/eLife.40063
