skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Mycobacterium tuberculosis SatS is a chaperone for the SecA2 protein export pathway

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 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.

Authors:
ORCiD logo [1];  [2];  [1];  [1];  [1];  [1];  [2]; ORCiD logo [1]
  1. Department of Microbiology and Immunology, University of North Carolina at Chapel Hill, North Carolina, United States
  2. Department of Biochemistry and Biophysics, Texas A&M University, College Station, United States
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
UNIVERSITYNIAIDOTHERNIGMS
OSTI Identifier:
1497169
Resource Type:
Journal Article
Journal Name:
eLife
Additional Journal Information:
Journal Volume: 8; Journal Issue: 01, 2019; Journal ID: ISSN 2050-084X
Publisher:
eLife Sciences Publications, Ltd.
Country of Publication:
United States
Language:
ENGLISH

Citation Formats

Miller, Brittany K., Hughes, Ryan, Ligon, Lauren S., Rigel, Nathan W., Malik, Seidu, Anjuwon-Foster, Brandon R., Sacchettini, James C., and Braunstein, Miriam. Mycobacterium tuberculosis SatS is a chaperone for the SecA2 protein export pathway. United States: N. p., 2019. Web. doi:10.7554/eLife.40063.
Miller, Brittany K., Hughes, Ryan, Ligon, Lauren S., Rigel, Nathan W., Malik, Seidu, Anjuwon-Foster, Brandon R., Sacchettini, James C., & Braunstein, Miriam. Mycobacterium tuberculosis SatS is a chaperone for the SecA2 protein export pathway. United States. doi:10.7554/eLife.40063.
Miller, Brittany K., Hughes, Ryan, Ligon, Lauren S., Rigel, Nathan W., Malik, Seidu, Anjuwon-Foster, Brandon R., Sacchettini, James C., and Braunstein, Miriam. Thu . "Mycobacterium tuberculosis SatS is a chaperone for the SecA2 protein export pathway". United States. doi:10.7554/eLife.40063.
@article{osti_1497169,
title = {Mycobacterium tuberculosis SatS is a chaperone for the SecA2 protein export pathway},
author = {Miller, Brittany K. and Hughes, Ryan and Ligon, Lauren S. and Rigel, Nathan W. and Malik, Seidu and Anjuwon-Foster, Brandon R. and Sacchettini, James C. and Braunstein, Miriam},
abstractNote = {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.},
doi = {10.7554/eLife.40063},
journal = {eLife},
issn = {2050-084X},
number = 01, 2019,
volume = 8,
place = {United States},
year = {2019},
month = {1}
}