ArticleJournal of bacteriology2011
Asp2 and Asp3 interact directly with GspB, the export substrate of the Streptococcus gordonii accessory Sec System.
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
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 26 citations in OpenAlex.
- Serine-rich repeat proteins: well-known yet little-understood bacterial adhesins.Journal of bacteriology · 2024Review
- Streptococcal Serine-Rich Repeat Proteins in Colonization and Disease.Frontiers in microbiology · 2020Review
- 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
- Serine-rich repeat protein adhesins from Lactobacillus reuteri display strain specific glycosylation profiles.Glycobiology · 2019Article
- Unraveling the sequence of cytosolic reactions in the export of GspB adhesin fromThe Journal of biological chemistry · 2018Article
- O-acetylation of the serine-rich repeat glycoprotein GspB is coordinated with accessory Sec transport.PLoS pathogens · 2017Article
- Composition and Activity of the Non-canonical Gram-positive SecY2 Complex.The Journal of biological chemistry · 2016Article
- 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
- The accessory Sec protein Asp2 modulates GlcNAc deposition onto the serine-rich repeat glycoprotein GspB.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
- Canonical SecA associates with an accessory secretory protein complex involved in biogenesis of a streptococcal serine-rich repeat glycoprotein.Journal of bacteriology · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
GspB is a serine-rich glycoprotein adhesin of Streptococcus gordonii that is exported to the bacterial surface by the accessory Sec system. This dedicated export pathway is comprised of seven components (SecA2, SecY2, and five accessory Sec proteins [Asp1 to Asp5]). The latter proteins have no known homologs beyond the Asps of other species. Asp1 to Asp3 are absolutely required for export of the substrate GspB, but their roles in this process are unknown. Using copurification analysis and far-Western blotting, we found that Asp2 and Asp3 could individually bind the serine-rich repeat (SRR) domains of GspB. Deletion of both SRR regions of GspB led to a decrease in its export, suggesting that binding of the Asps to the SRR regions is important for GspB transport by the accessory Sec system. The Asps also bound a heterologous substrate for the accessory Sec system containing a slow-folding MalE variant, but they did not bind wild-type MalE. The combined results indicate that the Asps may recognize the export substrate through preferential interactions with its unstructured or unfolded regions. Glycosylation of the SRR domains on GspB prevented Asp binding, suggesting that binding of the Asps to the preprotein occurs prior to its full glycosylation. Together, these findings suggest that Asp2 and Asp3 are likely to function in part as chaperones in the early phase of GspB transport.
Indexed as
Identifiers
What OpenQuestion holds
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.