ArticleScientific reports2017
A novel c-di-GMP binding domain in glycosyltransferase BgsA is responsible for the synthesis of a mixed-linkage β-glucan.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- TolC Is Required for a Mixed-Linkage β-Glucan (MLG) Biosynthesis: Engineering Bacteria for MLG Overproduction.Microbial biotechnology · 2026Article
- Review
- Quantification of Mixed-Linkage β-Glucan (MLG) in Bacteria.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Article
- Nucleotide second messengers in bacterial decision making.Current opinion in microbiology · 2020Review
- Transcriptomic Studies Reveal that theInternational journal of molecular sciences · 2019Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
BgsA is the glycosyltransferase (GT) involved in the synthesis of a linear mixed-linkage β-glucan (MLG), a recently described exopolysaccharide activated by c-di-GMP in Sinorhizobium meliloti and other Rhizobiales. Although BgsA displays sequence and structural homology with bacterial cellulose synthases (CS), it does not contain any predictable c-di-GMP binding domain. In this work we demonstrate that the cytoplasmic C-terminal domain of BgsA (C-BgsA) binds c-di-GMP with both high affinity (K
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