ArticleJournal of bacteriology2013
Suppressor analysis reveals a role for SecY in the SecA2-dependent protein export pathway of Mycobacteria.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Sec and Tat Mediated Secretion Safeguards Mycobacterium tuberculosis Membrane Homeostasis.Molecular & cellular proteomics : MCP · 2026Article
- Screening of Novel Inhibitors Targeting the Non-ATP-binding Domain ofMedicinal chemistry (Shariqah (United Arab Emirates)) · 2026Article
- Programmed Transformation of Osteogenesis Microenvironment by a Multifunctional Hydrogel to Enhance Repair of Infectious Bone Defects.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Mycobacterium smegmatis: The Vanguard of Mycobacterial Research.Journal of bacteriology · 2023Review
- Genetic Determinants of Intrinsic Antibiotic Tolerance in Mycobacterium avium.Microbiology spectrum · 2021Article
- Evidence for the Mycobacterial Mce4 Transporter Being a Multiprotein Complex.Journal of bacteriology · 2021Article
- Protein Export into and across the Atypical Diderm Cell Envelope of Mycobacteria.Microbiology spectrum · 2019Review
- The Two Distinct Types of SecA2-Dependent Export Systems.Microbiology spectrum · 2019Review
- Article
- Structural Similarities and Differences between Two Functionally Distinct SecA Proteins, Mycobacterium tuberculosis SecA1 and SecA2.Journal of bacteriology · 2015Article
- Label-free Quantitative Proteomics Reveals a Role for the Mycobacterium tuberculosis SecA2 Pathway in Exporting Solute Binding Proteins and Mce Transporters to the Cell Wall.Molecular & cellular proteomics : MCP · 2015Article
- A prl mutation in SecY suppresses secretion and virulence defects of Listeria monocytogenes secA2 mutants.Journal of bacteriology · 2015Article
- In Vitro Interaction of the Housekeeping SecA1 with the Accessory SecA2 Protein of Mycobacterium tuberculosis.PloS one · 2015Article
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Authors and funding
5 authors.
Funding
Abstract
All bacteria use the conserved Sec pathway to transport proteins across the cytoplasmic membrane, with the SecA ATPase playing a central role in the process. Mycobacteria are part of a small group of bacteria that have two SecA proteins: the canonical SecA (SecA1) and a second, specialized SecA (SecA2). The SecA2-dependent pathway exports a small subset of proteins and is required for Mycobacterium tuberculosis virulence. The mechanism by which SecA2 drives export of proteins across the cytoplasmic membrane remains poorly understood. Here we performed suppressor analysis on a dominant negative secA2 mutant (secA2 K129R) of the model mycobacterium Mycobacterium smegmatis to better understand the pathway used by SecA2 to export proteins. Two extragenic suppressor mutations were identified as mapping to the promoter region of secY, which encodes the central component of the canonical Sec export channel. These suppressor mutations increased secY expression, and this effect was sufficient to alleviate the secA2 K129R phenotype. We also discovered that the level of SecY protein was greatly diminished in the secA2 K129R mutant, but at least partially restored in the suppressors. Furthermore, the level of SecY in a suppressor strongly correlated with the degree of suppression. Our findings reveal a detrimental effect of SecA2 K129R on SecY, arguing for an integrated system in which SecA2 works with SecY and the canonical Sec translocase to export proteins.
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