ArticleJournal of molecular evolution2007
Protein disulfide oxidoreductases and the evolution of thermophily: was the last common ancestor a heat-loving microbe?
Article in Journal of molecular evolution, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Can the origin of biosynthetic routes be explained by a Frankenstein's monster-like spontaneous assembly of prebiotic reactants?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Article
- The Last Universal Common Ancestor of Ribosome-Encoding Organisms: Portrait of LUCA.Journal of molecular evolution · 2024Review
- Exploration and isolation of novel thermophiles in frozen enrichment cultures derived from a terrestrial acidic hot spring.Extremophiles : life under extreme conditions · 2016Article
- The putative herpes simplex virus 1 chaperone protein UL32 modulates disulfide bond formation during infection.Journal of virology · 2015Article
- Experimental evidence for the thermophilicity of ancestral life.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Widespread disulfide bonding in proteins from thermophilic archaea.Archaea (Vancouver, B.C.) · 2011Article
- Multiple catalytically active thioredoxin folds: a winning strategy for many functions.Cellular and molecular life sciences : CMLS · 2010Review
- Deep phylogeny--how a tree can help characterize early life on Earth.Cold Spring Harbor perspectives in biology · 2010Review
- Redox-dependent dynamics of a dual thioredoxin fold protein: evolution of specialized folds.Biochemistry · 2009Article
- The last universal common ancestor: emergence, constitution and genetic legacy of an elusive forerunner.Biology direct · 2008Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein disulfide oxidoreductases (PDOs) are redox enzymes that catalyze dithiol-disulfide exchange reactions. Their sequences and structure reveal the presence of two thioredoxin fold units, each of which is endowed with a catalytic site CXXC motif. PDOs are the outcome of an ancient gene duplication event. They have been described in a number of thermophilic and hyperthermophilic species, where they play a critical role in the structural stabilization of intracellular proteins. PDOs are homologous to both the N-terminal domain of the bacterial alkyl hydroperoxide reductase (AhpF) and to the eukaryotic protein disulfide isomerase (PDI). Phylogenetic analysis of PDOs suggests that they first evolved in the crenarchaeota, spreading from them into the Bacteria via the euryarchaeota. These results imply that the last common ancestor (LCA) of all extant living beings lacked a PDO and argue, albeit weakly, against a thermophilic LCA.
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