ArticleThe Journal of biological chemistry2011
A molecular chaperone mediates a two-protein enzyme complex and glycosylation of serine-rich streptococcal adhesins.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 41 citations in OpenAlex.
- Identification of an uncharacterized protein as a novel regulator ofJournal of virology · 2025Article
- Identification and genetic engineering of pneumococcal capsule-like polysaccharides in commensal oral streptococci.Microbiology spectrum · 2024Article
- Serine-rich repeat proteins: well-known yet little-understood bacterial adhesins.Journal of bacteriology · 2024Review
- Structural basis for SdgB- and SdgA-mediated glycosylation of staphylococcal adhesive proteins.Acta crystallographica. Section D, Structural biology · 2021Article
- Opportunities and Challenges of Bacterial Glycosylation for the Development of Novel Antibacterial Strategies.Frontiers in microbiology · 2021Review
- Processivity in Bacterial Glycosyltransferases.ACS chemical biology · 2020Review
- Quantitative Proteomics Uncovers the Interaction between a Virulence Factor and Mutanobactin Synthetases inmSphere · 2019Article
- Serine-rich repeat protein adhesins from Lactobacillus reuteri display strain specific glycosylation profiles.Glycobiology · 2019Article
- Effects of the nitric oxide releasing biomimetic nanomatrix gel on pulp-dentin regeneration: Pilot study.PloS one · 2018Article
- Transcriptional organization of pneumococcal psrP-secY2A2 and impact of GtfA and GtfB deletion on PsrP-associated virulence properties.Microbes and infection · 2017Article
- Defining the enzymatic pathway for polymorphicThe Journal of biological chemistry · 2017Article
- 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
- Mechanism of a cytosolic O-glycosyltransferase essential for the synthesis of a bacterial adhesion protein.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Cyclic di-AMP mediates biofilm formation.Molecular microbiology · 2016Article
- Insights into bacterial protein glycosylation in human microbiota.Science China. Life sciences · 2016Review
- Glycosyltransferase-mediated Sweet Modification in Oral Streptococci.Journal of dental research · 2015Review
- A conserved domain is crucial for acceptor substrate binding in a family of glucosyltransferases.Journal of bacteriology · 2015Article
- The sweet tooth of bacteria: common themes in bacterial glycoconjugates.Microbiology and molecular biology reviews : MMBR · 2014Review
- Both GtfA and GtfB are required for SraP glycosylation in Staphylococcus aureus.Current microbiology · 2014Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Serine-rich repeat glycoproteins identified from streptococci and staphylococci are important for bacterial adhesion and biofilm formation. Two putative glycosyltransferases, Gtf1 and Gtf2, from Streptococcus parasanguinis form a two-protein enzyme complex that is required for glycosylation of a serine-rich repeat adhesin, Fap1. Gtf1 is a glycosyltransferase; however, the function of Gtf2 is unknown. Here, we demonstrate that Gtf2 enhances the enzymatic activity of Gtf1 by its chaperone-like property. Gtf2 interacted with Gtf1, mediated the subcellular localization of Gtf1, and stabilized Gtf1. Deletion of invariable amino acid residues in a conserved domain of unknown function (DUF1975) at the N terminus of Gtf2 had a greater impact on Fap1 glycosylation than deletion of the C-terminal non-DUF1975 residues. The DUF1975 deletions concurrently reduced the interaction between Gtf1 and Gtf2, altered the subcellular localization of Gtf1, and destabilized Gtf1, suggesting that DUF1975 is crucial for the chaperone activity of Gtf2. Homologous GtfA and GtfB from Streptococcus agalactiae rescued the glycosylation defect in the gtf1gtf2 mutant; like Gtf2, GtfB also possesses chaperone-like activity. Taken together, our studies suggest that Gtf2 and its homologs possess the conserved molecular chaperone activity that mediates protein glycosylation of bacterial adhesins.
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