ArticleThe Journal of biological chemistry2009
The Accessory SecA2 System of Mycobacteria Requires ATP Binding and the Canonical SecA1.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 52 citations in OpenAlex.
- Epigenetic Reprogramming byAntibiotics (Basel, Switzerland) · 2026Review
- Sec and Tat Mediated Secretion Safeguards Mycobacterium tuberculosis Membrane Homeostasis.Molecular & cellular proteomics : MCP · 2026Article
- Article
- Mycobacterium tuberculosis SecA2-dependent activation of host Rig-I/MAVs signaling is not conserved in Mycobacterium marinum.PloS one · 2024Article
- Pneumococcal Surface Proteins as Virulence Factors, Immunogens, and Conserved Vaccine Targets.Frontiers in cellular and infection microbiology · 2022Review
- The Structure ofInternational journal of molecular sciences · 2020Article
- 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
- Defining the Transcriptional and Post-transcriptional Landscapes ofFrontiers in microbiology · 2019Article
- An alternate mode of oligomerization for E. coli SecA.Scientific reports · 2017Article
- Structural Similarities and Differences between Two Functionally Distinct SecA Proteins, Mycobacterium tuberculosis SecA1 and SecA2.Journal of bacteriology · 2015Article
- The Etiologic Role of Infectious Antigens in Sarcoidosis Pathogenesis.Clinics in chest medicine · 2015Review
- Breaking the bacterial protein targeting and translocation model: oral organisms as a case in point.Molecular oral microbiology · 2015Review
- 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
- Selective transport by SecA2: an expanding family of customized motor proteins.Biochimica et biophysica acta · 2014Review
- ADP-dependent conformational changes distinguish Mycobacterium tuberculosis SecA2 from SecA1.The Journal of biological chemistry · 2014Article
- Multitasking SecB chaperones in bacteria.Frontiers in microbiology · 2014Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
In bacteria, the majority of exported proteins are transported by the general Sec pathway from their site of synthesis in the cytoplasm across the cytoplasmic membrane. The essential SecA ATPase powers this Sec-mediated export. Mycobacteria possess two nonredundant SecA homologs: SecA1 and SecA2. In pathogenic Mycobacterium tuberculosis and the nonpathogenic model mycobacterium Mycobacterium smegmatis, SecA1 is essential for protein export and is the "housekeeping" SecA, whereas SecA2 is an accessory SecA that exports a specific subset of proteins. In M. tuberculosis the accessory SecA2 pathway plays a role in virulence. In this study, we uncovered basic properties of the mycobacterial SecA2 protein and its pathway for exporting select proteins. By constructing secA2 mutant alleles that encode proteins defective in ATP binding, we showed that ATP binding is required for SecA2 function. SecA2 mutant proteins unable to bind ATP were nonfunctional and dominant negative. By evaluating the subcellular distribution of each SecA, SecA1 was shown to be equally divided between cytosolic and cell envelope fractions, whereas SecA2 was predominantly localized to the cytosol. Finally, we showed that the canonical SecA1 has a role in the process of SecA2-dependent export. The accessory SecA2 export system is important to the physiology and virulence of mycobacteria. These studies help establish the mechanism of this new type of specialized protein export pathway.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.