ArticleJournal of bacteriology2011
Canonical SecA associates with an accessory secretory protein complex involved in biogenesis of a streptococcal serine-rich repeat glycoprotein.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
17 citing papers in PubMed, 22 citations in OpenAlex.
- Serine-rich repeat proteins: well-known yet little-understood bacterial adhesins.Journal of bacteriology · 2024Review
- Unraveling the sequence of cytosolic reactions in the export of GspB adhesin fromThe Journal of biological chemistry · 2018Article
- Engineering and Dissecting the Glycosylation Pathway of a Streptococcal Serine-rich Repeat Adhesin.The Journal of biological chemistry · 2016Article
- New Helical Binding Domain Mediates a Glycosyltransferase Activity of a Bifunctional Protein.The Journal of biological chemistry · 2016Article
- Breaking the bacterial protein targeting and translocation model: oral organisms as a case in point.Molecular oral microbiology · 2015Review
- A prl mutation in SecY suppresses secretion and virulence defects of Listeria monocytogenes secA2 mutants.Journal of bacteriology · 2015Article
- A conserved domain is crucial for acceptor substrate binding in a family of glucosyltransferases.Journal of bacteriology · 2015Article
- In Vitro Interaction of the Housekeeping SecA1 with the Accessory SecA2 Protein of Mycobacterium tuberculosis.PloS one · 2015Article
- The sweet tooth of bacteria: common themes in bacterial glycoconjugates.Microbiology and molecular biology reviews : MMBR · 2014Review
- Selective transport by SecA2: an expanding family of customized motor proteins.Biochimica et biophysica acta · 2014Review
- Gap2 promotes the formation of a stable protein complex required for mature Fap1 biogenesis.Journal of bacteriology · 2013Article
- Differential localization of the streptococcal accessory sec components and implications for substrate export.Journal of bacteriology · 2013Article
- Emerging themes in SecA2-mediated protein export.Nature reviews. Microbiology · 2012Review
- 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
- Gap1 functions as a molecular chaperone to stabilize its interactive partner Gap3 during biogenesis of serine-rich repeat bacterial adhesin.Molecular microbiology · 2012Article
- The accessory Sec system (SecY2A2) in Streptococcus pneumoniae is involved in export of pneumolysin toxin, adhesion and biofilm formation.Microbes and infectionArticle
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Fap1, a serine-rich repeat glycoprotein (SRRP), is required for bacterial biofilm formation of Streptococcus parasanguinis. Fap1-like SRRPs are found in many gram-positive bacteria and have been implicated in bacterial fitness and virulence. A conserved five-gene cluster, secY2-gap1-gap2-gap3-secA2, located immediately downstream of fap1, is required for Fap1 biogenesis. secA2, gap1, and gap3 encode three putative accessory Sec proteins. SecA2 mediates export of mature Fap1, and Gap1 and Gap3 are required for Fap1 biogenesis. Interestingly, gap1 and gap3 mutants exhibited the same phenotype as a secA2 mutant, implying that Gap1 and Gap3 may interact with SecA2 to mediate Fap1 biogenesis. Glutathione S-transferase pulldown experiments revealed a direct interaction between SecA2, Gap1, and Gap3 in vitro. Coimmunoprecipitation analysis demonstrated the formation of a SecA2-Gap1-Gap3 complex. Homologues of SecA2, Gap1, and Gap3 are conserved in many streptococci and staphylococci. The corresponding homologues from Streptococcus agalactiae also interacted with each other and formed a protein complex. Furthermore, the Gap1 homologues from S. agalactiae and Streptococcus sanguinis rescued the Fap1 defect in the Gap1 mutant, indicating the functional conservation of the accessory Sec complex. Importantly, canonical SecA interacted with the accessory Sec protein complex, suggesting that the biogenesis of SRRPs mediated by the accessory Sec system is linked to the canonical Sec system.
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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.