ArticleJournal of bacteriology2010
Transport of preproteins by the accessory Sec system requires a specific domain adjacent to the signal peptide.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Comparative pangenomics ofMicrobial genomics · 2025Article
- Serine-rich repeat proteins: well-known yet little-understood bacterial adhesins.Journal of bacteriology · 2024Review
- Recognition of specific sialoglycan structures by oral streptococci impacts the severity of endocardial infection.PLoS pathogens · 2019Article
- The Two Distinct Types of SecA2-Dependent Export Systems.Microbiology spectrum · 2019Review
- Membrane trafficking of the bacterial adhesin GspB and the accessory Sec transport machinery.The Journal of biological chemistry · 2019Article
- Unraveling the sequence of cytosolic reactions in the export of GspB adhesin fromThe Journal of biological chemistry · 2018Article
- Bacillus anthracis SlaQ Promotes S-Layer Protein Assembly.Journal of bacteriology · 2015Article
- A prl mutation in SecY suppresses secretion and virulence defects of Listeria monocytogenes secA2 mutants.Journal of bacteriology · 2015Article
- Selective transport by SecA2: an expanding family of customized motor proteins.Biochimica et biophysica acta · 2014Review
- N-acetylglucosaminylation of serine-aspartate repeat proteins promotes Staphylococcus aureus bloodstream infection.The Journal of biological chemistry · 2014Article
- Differential localization of the streptococcal accessory sec components and implications for substrate export.Journal of bacteriology · 2013Article
- Protein export by the mycobacterial SecA2 system is determined by the preprotein mature domain.Journal of bacteriology · 2013Article
- Emerging themes in SecA2-mediated protein export.Nature reviews. Microbiology · 2012Review
- Secretion genes as determinants of Bacillus anthracis chain length.Journal of bacteriology · 2012Article
- A role for glycosylated serine-rich repeat proteins in gram-positive bacterial pathogenesis.Molecular oral microbiology · 2012Review
- A Specific interaction between SecA2 and a region of the preprotein adjacent to the signal peptide occurs during transport via the accessory Sec system.The Journal of biological chemistry · 2012Article
- Protein secretion and surface display in Gram-positive bacteria.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- Asp2 and Asp3 interact directly with GspB, the export substrate of the Streptococcus gordonii accessory Sec System.Journal of bacteriology · 2011Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The accessory Sec (SecA2/Y2) systems of streptococci and staphylococci are dedicated to the transport of large serine-rich repeat (SRR) glycoproteins to the bacterial cell surface. The means by which the glycosylated preproteins are selectively recognized by the accessory Sec system have not been fully characterized. In Streptococcus gordonii, the SRR glycoprotein GspB has a 90-residue amino-terminal signal sequence that is essential for transport by SecA2/Y2 but is not sufficient to mediate the transport of heterologous proteins by this specialized transporter. We now report that a preprotein must remain at least partially unfolded prior to transport by the accessory Sec system. In addition, a region of approximately 20 residues from the amino-terminal end of mature GspB (the accessory Sec transport or AST domain) is essential for SecA2/Y2-dependent transport. The replacement of several AST domain residues with glycine strongly interferes with export, which suggests that a helical conformation may be important. Analysis of GspB variants with alterations in the AST domain, in combination with the results with a SecY2 variant, indicates that the AST domain is essential both for targeting to the SecA2/Y2 translocase and for initiating translocation through the SecY2 channel. The combined results suggest a unique mechanism that ensures the transport of a single substrate by the SecA2/Y2 system.
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