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| Format: | Artículo científico |
| Language: | en |
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Proceedings of the National Academy of Sciences of the United States of America
2025
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| Online Access: | https://pubmed.ncbi.nlm.nih.gov/41364767/ |
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| author | Wang, Ning Westermann, Linda M Li, Mingyu Li, Chun-Yang Murphy, Andrew R J Gu, Zengtian Silvano, Eleonora Blindauer, Claudia A Lidbury, Ian D E A Zhang, Yu-Zhong Scanlan, David J Chen, Yin |
| author_facet | Wang, Ning Westermann, Linda M Li, Mingyu Li, Chun-Yang Murphy, Andrew R J Gu, Zengtian Silvano, Eleonora Blindauer, Claudia A Lidbury, Ian D E A Zhang, Yu-Zhong Scanlan, David J Chen, Yin Wang, Ning Westermann, Linda M Li, Mingyu Li, Chun-Yang Murphy, Andrew R J Gu, Zengtian Silvano, Eleonora Blindauer, Claudia A Lidbury, Ian D E A Zhang, Yu-Zhong Scanlan, David J Chen, Yin |
| collection | PubMed - marine biology |
| contents | Structural basis and evolutionary pathways of glycerol-1-phosphate transport in marine bacteria. Wang, Ning Westermann, Linda M Li, Mingyu Li, Chun-Yang Murphy, Andrew R J Gu, Zengtian Silvano, Eleonora Blindauer, Claudia A Lidbury, Ian D E A Zhang, Yu-Zhong Scanlan, David J Chen, Yin Phylogeny Glycerophosphates Evolution, Molecular Bacterial Proteins Biological Transport Bacteria Aquatic Organisms Seawater Membrane Transport Proteins All cells use lipid membranes to maintain cellular integrity and function, though Archaea utilize lipids composed of glycerol-1-phosphate (G1P), while Bacteria and Eukaryotes use glycerol-3-phosphate (G3P). Given that Archaea contribute significantly to global marine biomass, accounting for 0.3 gigatonnes (Gt) of carbon in the oceans, we aimed to uncover how archaeal G1P is recycled by marine microorganisms. Through a multidisciplinary approach combining microbiology, biochemistry, and structural biology, we identified a G1P transporter in marine bacteria, which we named GpxB. Phylogenetic analysis revealed that GpxB belongs to the organic phosphonate transporter (PhnT) family and is widely distributed in the marine microbiome, found in approximately 5 to 10% of microbial cells in surface marine waters. Strikingly, we also identified a second G1P transporter, UgpB, that is known to transport G3P and belongs to the carbohydrate uptake transporter-1 (CUT1) family, in the model bacterium sp. MED193. To explore the evolutionary pathways that led to the formation of G1P binding sites in both the PhnT and CUT1 families, we determined the structures of GpxB and UgpB bound to G1P and G3P. Using structure-guided mutagenesis and a comparative analysis of the binding pockets within the PhnT and CUT1 families, we traced their evolutionary trajectories, highlighting the distinct strategies through which G1P-binding sites developed in these two protein families. |
| format | Artículo científico |
| id | pubmed_41364767 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | Proceedings of the National Academy of Sciences of the United States of America |
| record_format | pubmed |
| spellingShingle | Structural basis and evolutionary pathways of glycerol-1-phosphate transport in marine bacteria. Wang, Ning Westermann, Linda M Li, Mingyu Li, Chun-Yang Murphy, Andrew R J Gu, Zengtian Silvano, Eleonora Blindauer, Claudia A Lidbury, Ian D E A Zhang, Yu-Zhong Scanlan, David J Chen, Yin Phylogeny Glycerophosphates Evolution, Molecular Bacterial Proteins Biological Transport Bacteria Aquatic Organisms Seawater Membrane Transport Proteins Structural basis and evolutionary pathways of glycerol-1-phosphate transport in marine bacteria. Wang, Ning Westermann, Linda M Li, Mingyu Li, Chun-Yang Murphy, Andrew R J Gu, Zengtian Silvano, Eleonora Blindauer, Claudia A Lidbury, Ian D E A Zhang, Yu-Zhong Scanlan, David J Chen, Yin Phylogeny Glycerophosphates Evolution, Molecular Bacterial Proteins Biological Transport Bacteria Aquatic Organisms Seawater Membrane Transport Proteins All cells use lipid membranes to maintain cellular integrity and function, though Archaea utilize lipids composed of glycerol-1-phosphate (G1P), while Bacteria and Eukaryotes use glycerol-3-phosphate (G3P). Given that Archaea contribute significantly to global marine biomass, accounting for 0.3 gigatonnes (Gt) of carbon in the oceans, we aimed to uncover how archaeal G1P is recycled by marine microorganisms. Through a multidisciplinary approach combining microbiology, biochemistry, and structural biology, we identified a G1P transporter in marine bacteria, which we named GpxB. Phylogenetic analysis revealed that GpxB belongs to the organic phosphonate transporter (PhnT) family and is widely distributed in the marine microbiome, found in approximately 5 to 10% of microbial cells in surface marine waters. Strikingly, we also identified a second G1P transporter, UgpB, that is known to transport G3P and belongs to the carbohydrate uptake transporter-1 (CUT1) family, in the model bacterium sp. MED193. To explore the evolutionary pathways that led to the formation of G1P binding sites in both the PhnT and CUT1 families, we determined the structures of GpxB and UgpB bound to G1P and G3P. Using structure-guided mutagenesis and a comparative analysis of the binding pockets within the PhnT and CUT1 families, we traced their evolutionary trajectories, highlighting the distinct strategies through which G1P-binding sites developed in these two protein families. |
| title | Structural basis and evolutionary pathways of glycerol-1-phosphate transport in marine bacteria. |
| topic | Phylogeny Glycerophosphates Evolution, Molecular Bacterial Proteins Biological Transport Bacteria Aquatic Organisms Seawater Membrane Transport Proteins |
| url | https://pubmed.ncbi.nlm.nih.gov/41364767/ |