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| Format: | Artículo científico |
| Sprache: | en |
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Nature communications
2024
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| Online-Zugang: | https://pubmed.ncbi.nlm.nih.gov/39406702/ |
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| author | Wegner, Helen Roitman, Sheila Kupczok, Anne Braun, Vanessa Woodhouse, Jason Nicholas Grossart, Hans-Peter Zehner, Susanne Béjà, Oded Frankenberg-Dinkel, Nicole |
| author_facet | Wegner, Helen Roitman, Sheila Kupczok, Anne Braun, Vanessa Woodhouse, Jason Nicholas Grossart, Hans-Peter Zehner, Susanne Béjà, Oded Frankenberg-Dinkel, Nicole Wegner, Helen Roitman, Sheila Kupczok, Anne Braun, Vanessa Woodhouse, Jason Nicholas Grossart, Hans-Peter Zehner, Susanne Béjà, Oded Frankenberg-Dinkel, Nicole |
| collection | PubMed - marine biology |
| contents | Identification of Shemin pathway genes for tetrapyrrole biosynthesis in bacteriophage sequences from aquatic environments. Wegner, Helen Roitman, Sheila Kupczok, Anne Braun, Vanessa Woodhouse, Jason Nicholas Grossart, Hans-Peter Zehner, Susanne Béjà, Oded Frankenberg-Dinkel, Nicole Tetrapyrroles Bacteriophages Escherichia coli 5-Aminolevulinate Synthetase Amino Acid Sequence Heme Aminolevulinic Acid Phylogeny Fresh Water Biosynthetic Pathways Tetrapyrroles such as heme, chlorophyll, and vitamin B are essential for various metabolic pathways. They derive from 5-aminolevulinic acid (5-ALA), which can be synthesized by a single enzyme (5-ALA synthase or AlaS, Shemin pathway) or by a two-enzyme pathway. The genomes of some bacteriophages from aquatic environments carry various tetrapyrrole biosynthesis genes. Here, we analyze available metagenomic datasets and identify alaS homologs (viral alaS, or valaS) in sequences corresponding to marine and freshwater phages. The genes are found individually or as part of complete or truncated three-gene loci encoding heme-catabolizing enzymes. Amino-acid sequence alignments and three-dimensional structure prediction support that the valaS sequences likely encode functional enzymes. Indeed, we demonstrate that is the case for a freshwater phage valaS sequence, as it can complement an Escherichia coli 5-ALA auxotroph, and an E. coli strain overexpressing the gene converts the typical AlaS substrates glycine and succinyl-CoA into 5-ALA. Thus, our work identifies valaS as an auxiliary metabolic gene in phage sequences from aquatic environments, further supporting the importance of tetrapyrrole metabolism in bacteriophage biology. |
| format | Artículo científico |
| id | pubmed_39406702 |
| institution | PubMed |
| language | en |
| publishDate | 2024 |
| publisher | Nature communications |
| record_format | pubmed |
| spellingShingle | Identification of Shemin pathway genes for tetrapyrrole biosynthesis in bacteriophage sequences from aquatic environments. Wegner, Helen Roitman, Sheila Kupczok, Anne Braun, Vanessa Woodhouse, Jason Nicholas Grossart, Hans-Peter Zehner, Susanne Béjà, Oded Frankenberg-Dinkel, Nicole Tetrapyrroles Bacteriophages Escherichia coli 5-Aminolevulinate Synthetase Amino Acid Sequence Heme Aminolevulinic Acid Phylogeny Fresh Water Biosynthetic Pathways Identification of Shemin pathway genes for tetrapyrrole biosynthesis in bacteriophage sequences from aquatic environments. Wegner, Helen Roitman, Sheila Kupczok, Anne Braun, Vanessa Woodhouse, Jason Nicholas Grossart, Hans-Peter Zehner, Susanne Béjà, Oded Frankenberg-Dinkel, Nicole Tetrapyrroles Bacteriophages Escherichia coli 5-Aminolevulinate Synthetase Amino Acid Sequence Heme Aminolevulinic Acid Phylogeny Fresh Water Biosynthetic Pathways Tetrapyrroles such as heme, chlorophyll, and vitamin B are essential for various metabolic pathways. They derive from 5-aminolevulinic acid (5-ALA), which can be synthesized by a single enzyme (5-ALA synthase or AlaS, Shemin pathway) or by a two-enzyme pathway. The genomes of some bacteriophages from aquatic environments carry various tetrapyrrole biosynthesis genes. Here, we analyze available metagenomic datasets and identify alaS homologs (viral alaS, or valaS) in sequences corresponding to marine and freshwater phages. The genes are found individually or as part of complete or truncated three-gene loci encoding heme-catabolizing enzymes. Amino-acid sequence alignments and three-dimensional structure prediction support that the valaS sequences likely encode functional enzymes. Indeed, we demonstrate that is the case for a freshwater phage valaS sequence, as it can complement an Escherichia coli 5-ALA auxotroph, and an E. coli strain overexpressing the gene converts the typical AlaS substrates glycine and succinyl-CoA into 5-ALA. Thus, our work identifies valaS as an auxiliary metabolic gene in phage sequences from aquatic environments, further supporting the importance of tetrapyrrole metabolism in bacteriophage biology. |
| title | Identification of Shemin pathway genes for tetrapyrrole biosynthesis in bacteriophage sequences from aquatic environments. |
| topic | Tetrapyrroles Bacteriophages Escherichia coli 5-Aminolevulinate Synthetase Amino Acid Sequence Heme Aminolevulinic Acid Phylogeny Fresh Water Biosynthetic Pathways |
| url | https://pubmed.ncbi.nlm.nih.gov/39406702/ |