ArticleJournal of molecular evolution2009
Sulfate activation enzymes: phylogeny and association with pyrophosphatase.
Article in Journal of molecular evolution, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
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- Review
- Unique Features ofInternational journal of molecular sciences · 2019Review
- Structure and mechanism of soybean ATP sulfurylase and the committed step in plant sulfur assimilation.The Journal of biological chemistry · 2014Article
- Transport proteins of parasitic protists and their role in nutrient salvage.Frontiers in plant science · 2014Review
- Diversity and regulation of ATP sulfurylase in photosynthetic organisms.Frontiers in plant science · 2014Review
- Kinetic mechanism of the dimeric ATP sulfurylase from plants.Bioscience reports · 2013Article
- Adenosine-5'-phosphosulfate--a multifaceted modulator of bifunctional 3'-phospho-adenosine-5'-phosphosulfate synthases and related enzymes.The FEBS journal · 2013Review
- Cloning, expression and bioinformatics analysis of ATP sulfurylase from Acidithiobacillus ferrooxidans ATCC 23270 in Escherichia coli.Bioinformation · 2012Article
- Sulfate activation in mitosomes plays an important role in the proliferation of Entamoeba histolytica.PLoS neglected tropical diseases · 2011Article
- Mitosomes in Entamoeba histolytica contain a sulfate activation pathway.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The enzymes catalyzing the first two reactions in the sulfate activation pathway, ATP-sulfurylase (S) and APS-kinase (K), are fused as 'KS' in animals but are fused as 'SK' in select bacteria and fungi. We have discovered a novel triple fusion protein of K, S, and pyrophosphatase (P) in several protozoan genomes within the Stramenopile lineage. These triple domain fusion proteins led us to hypothesize that pyrophosphatase enzymes and sulfate activation enzymes physically interact to impact the thermodynamics of the sulfate activation pathway. In support of this hypothesis, we demonstrate through biochemical assays that separately encoded KS and P proteins physically interact and that KS/P complexes activate more sulfate than KS alone. We also conclude on the basis of phylogenetic analyses that all known KS fusions originate from a single fusion event early in the eukaryotic lineage. Strikingly, our analyses support the same conclusion for all known SK fusions. These observations indicate that the patchwork of fused and nonfused S and K genes observed in modern-day eukaryotes and prokaryotes are the result of the two ancestral fusion genes evolving by an assortment of gene fissions, duplications, deletions, and horizontal transfers in different lineages. Our integrative use of genomics, phylogenetics, and biochemistry to characterize pyrophosphatase as a new member of the sulfate activation pathway should be effective at identifying new protein members and connections in other molecular pathways.
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