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- Title
Polar assembly and scaffolding proteins of the virulence-associated ESX-1 secretory apparatus in mycobacteria.
- Authors
Wirth, Samantha E.; Krywy, Janet A.; Aldridge, Bree B.; Fortune, Sarah M.; Fernandez-Suarez, Marta; Gray, Todd A.; Derbyshire, Keith M.
- Abstract
Summary The ESX-1 secretion system is required for pathogenicity of Mycobacterium tuberculosis ( Mtb). Despite considerable research, little is known about the structural components of ESX-1, or how these proteins are assembled into the active secretion apparatus. Here, we exploit the functionally related ESX-1 apparatus of Mycobacterium smegmatis ( Ms) to show that fluorescently tagged proteins required for ESX-1 activity consistently localize to the cell pole, identified by time-lapse fluoro-microscopy as the non-septal (old) pole. Deletions in Msesx1 prevented polar localization of tagged proteins, indicating the need for specific protein-protein interactions in polar trafficking. Remarkably, expression of the Mtbesx1 locus in Msesx1 mutants restored polar localization of tagged proteins, indicating establishment of the MtbESX-1 apparatus in M. smegmatis. This observation illustrates the cross-species conservation of protein interactions governing assembly of ESX-1, as well as polar localization. Importantly, we describe novel non- esx1-encoded proteins, which affect ESX-1 activity, which colocalize with ESX-1, and which are required for ESX-1 recruitment and assembly. This analysis provides new insights into the molecular assembly of this important determinant of Mtb virulence.
- Subjects
SECRETION; MYCOBACTERIUM tuberculosis; PROTEINS; MYCOBACTERIUM smegmatis; MICROBIAL virulence
- Publication
Molecular Microbiology, 2012, Vol 83, Issue 3, p654
- ISSN
0950-382X
- Publication type
Article
- DOI
10.1111/j.1365-2958.2011.07958.x