ArticleThe Journal of biological chemistry2012
A Specific interaction between SecA2 and a region of the preprotein adjacent to the signal peptide occurs during transport via the accessory Sec system.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Biogenesis, quality control, and structural dynamics of proteins as explored in living cells via site-directed photocrosslinking.Protein science : a publication of the Protein Society · 2019Review
- 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
- O-acetylation of the serine-rich repeat glycoprotein GspB is coordinated with accessory Sec transport.PLoS pathogens · 2017Article
- Activity of a bacterial cell envelope stress response is controlled by the interaction of a protein binding domain with different partners.The Journal of biological chemistry · 2015Article
- Illumination of growth, division and secretion by metabolic labeling of the bacterial cell surface.FEMS microbiology reviews · 2015Review
- Selective transport by SecA2: an expanding family of customized motor proteins.Biochimica et biophysica acta · 2014Review
- Protein export by the mycobacterial SecA2 system is determined by the preprotein mature domain.Journal of bacteriology · 2013Article
- Differential localization of the streptococcal accessory sec components and implications for substrate export.Journal of bacteriology · 2013Article
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Authors and funding
4 authors.
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Abstract
The accessory Sec systems of streptococci and staphylococci mediate the transport of a family of large, serine-rich glycoproteins to the bacterial cell surface. These systems are comprised of SecA2, SecY2, and three core accessory Sec proteins (Asp1-3). In Streptococcus gordonii, transport of the serine-rich glycoprotein GspB requires both a unique 90-residue N-terminal signal peptide and an adjacent 24-residue segment (the AST domain). We used in vivo site-specific photo-cross-linking to identify proteins that interact with the AST domain during transport. To facilitate this analysis, the entire accessory Sec system of S. gordonii was expressed in Escherichia coli. The determinants of GspB trafficking to the accessory Sec system in E. coli matched those in S. gordonii, establishing the validity of this approach. When the photo-cross-linker was placed within the AST domain, the preprotein was found to cross-link to SecA2. Importantly, no cross-linking to SecA was detected. Cross-linking of the N-terminal end of the AST domain to SecA2 occurred regardless of whether Asp1-3 were present. However, cross-linking to the C-terminal end was dependent on the Asps. The combined results indicate that full engagement of the AST domain by SecA2 is modulated by one or more of the Asps, and suggest that this process is important for initiating transport.
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