ArticleProceedings of the National Academy of Sciences of the United States of America2010
Identification of a gene essential for protoporphyrinogen IX oxidase activity in the cyanobacterium Synechocystis sp. PCC6803.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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32 citing papers in PubMed.
- Milestones in the Elucidation of Heme Biosynthesis.Chemical reviews · 2026Review
- Safety assessment of membrane-associated protoporphyrinogen IX oxidase fromGM crops & food · 2025Article
- Epigenetic control of tetrapyrrole biosynthesis by m4C DNA methylation in a cyanobacterium.DNA research : an international journal for rapid publication of reports on genes and genomes · 2024Article
- Article
- Photosynthesis, Water Status and KPlants (Basel, Switzerland) · 2023Article
- Microbial Synthesis of HemeMolecules (Basel, Switzerland) · 2023Review
- Distribution and functional analysis of the two types of 8-vinyl reductase involved in chlorophyll biosynthesis in marine cyanobacteria.Archives of microbiology · 2021Article
- Genetic, Genomics, and Responses to Stresses in Cyanobacteria: Biotechnological Implications.Genes · 2021Review
- Biosynthesis of the modified tetrapyrroles-the pigments of life.The Journal of biological chemistry · 2020Review
- Article
- Characterization of HemY-type protoporphyrinogen IX oxidase genes from cyanobacteria and their functioning in transgenic Arabidopsis.Plant molecular biology · 2019Article
- Making and breaking heme.Current opinion in structural biology · 2019Review
- Design and Synthesis ofMolecules (Basel, Switzerland) · 2019Article
- Genomic erosion and extensive horizontal gene transfer in gut-associated Acetobacteraceae.BMC genomics · 2019Article
- The cyanobacterial protoporphyrinogen oxidase HemJ is a newThe Journal of biological chemistry · 2018Article
- WhollymBio · 2017Article
- Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.Microbiology and molecular biology reviews : MMBR · 2017Review
- The Complex Transcriptional Response ofG3 (Bethesda, Md.) · 2017Article
- Transcriptomic analysis illuminates genes involved in chlorophyll synthesis after nitrogen starvation in Acaryochloris sp. CCMEE 5410.Photosynthesis research · 2016Article
- Establishment of the forward genetic analysis of the chlorophyll d-dominated cyanobacterium Acaryochloris marina MBIC 11017 by applying in vivo transposon mutagenesis system.Photosynthesis research · 2015Article
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5 authors.
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Abstract
Protoporphyrinogen oxidase (Protox) catalyses the oxidation of protoporphyrinogen IX to protoporphyrin IX during the synthesis of tetrapyrrole molecules. Protox is encoded by the hemY gene in eukaryotes and by the hemG gene in many γ-proteobacteria, including Escherichia coli. It has been suggested that other bacteria possess a yet unidentified type of Protox. To identify a unique bacterial gene encoding Protox, we first introduced the Arabidopsis hemY gene into the genome of the cyanobacterium, Synechocystis sp. PCC6803. We subsequently mutagenized the cells by transposon tagging and screened the tagged lines for mutants that were sensitive to acifluorfen, which is a specific inhibitor of the hemY-type Protox. Several cell lines containing the tagged slr1790 locus exhibited acifluorfen sensitivity. The slr1790 gene encodes a putative membrane-spanning protein that is distantly related to the M subunit of NADH dehydrogenase complex I. We attempted to disrupt this gene in the wild-type background of Synechocystis, but we were only able to obtain heteroplasmic disruptants. These cells accumulated a substantial amount of protoporphyrin IX, suggesting that the slr1790 gene is essential for growth and Protox activity of cells. We found that most cyanobacteria and many other bacteria possess slr1790 homologs. We overexpressed an slr1790 homolog of Rhodobacter sphaeroides in Escherichia coli and found that this recombinant protein possesses Protox activity in vitro. These results collectively demonstrate that slr1790 encodes a unique Protox enzyme and we propose naming the slr1790 gene "hemJ."
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