ArticleMicrobiologyOpen2019
Glycolipid composition of the heterocyst envelope of Anabaena sp. PCC 7120 is crucial for diazotrophic growth and relies on the UDP-galactose 4-epimerase HgdA.
Article in MicrobiologyOpen, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Towards the control of biofilm formation in Anabaena (Nostoc) sp. PCC7120: novel insights into the genes involved and their regulation.The New phytologist · 2025Article
- Emergence and evolution of heterocyte glycolipid biosynthesis enabled specialized nitrogen fixation in cyanobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Exploring the mechanism of seed shattering in Psathyrostachys juncea through histological analysis and comparative transcriptomics.BMC plant biology · 2024Article
- The Role of MreB, MreC and MreD in the Morphology of the Diazotrophic Filament ofLife (Basel, Switzerland) · 2022Article
- The Dual Role of the Glycolipid Envelope in Different Cell Types of the Multicellular CyanobacteriumFrontiers in microbiology · 2021Article
- Extracellular Vesicles: An Overlooked Secretion System in Cyanobacteria.Life (Basel, Switzerland) · 2020Review
- Glycolipid composition of the heterocyst envelope of Anabaena sp. PCC 7120 is crucial for diazotrophic growth and relies on the UDP-galactose 4-epimerase HgdA.MicrobiologyOpen · 2019Article
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3 authors.
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Abstract
The nitrogenase complex in the heterocysts of the filamentous freshwater cyanobacterium Anabaenasp. PCC 7120 fixes atmospheric nitrogen to allow diazotrophic growth. The heterocyst cell envelope protects the nitrogenase from oxygen and consists of a polysaccharide and a glycolipid layer that are formed by a complex process involving the recruitment of different proteins. Here, we studied the function of the putative nucleoside-diphosphate-sugar epimerase HgdA, which along with HgdB and HgdC is essential for deposition of the glycolipid layer and growth without a combined nitrogen source. Using site-directed mutagenesis and single homologous recombination approach, we performed a thoroughly functional characterization of HgdA and confirmed that the glycolipid layer of the hgdAmutant heterocyst is aberrant as shown by transmission electron microscopy and chemical analysis. The hgdA gene was expressed during late stages of the heterocyst differentiation. GFP-tagged HgdA protein localized inside the heterocysts. The purified HgdA protein had UDP-galactose 4-epimerase activity in vitro. This enzyme could be responsible for synthesis of heterocyst-specific glycolipid precursors, which could be transported over the cell wall by the ABC transporter components HgdB/HgdC.
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