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- Title
Evolution of the Selenoproteome in Helicobacter pylori and Epsilonproteobacteria.
- Authors
Cravedi, Pietro; Mori, Giulia; Fischer, Frédéric; Percudani, Riccardo
- Abstract
By competing for the acquisition of essential nutrients,Helicobacter pylori has the unique ability to persist in the human stomach, also causing nutritional insufficiencies in the host. Although the H. pylori genome apparently encodes selenocysteine synthase (SelA,HP1513), a key pyridoxal phosphate (PLP)-dependent enzymefor the incorporation of selenium into bacterial proteins, nothing is known about the use of this essential element in protein synthesis by this pathogen.We analyzed the evolution of the complete machinery for incorporation of selenium into proteins and the selenoproteome of several H. pylori strains and related Epsilonproteobacteria. Our searches identified the presence of selenoproteins—including the previously unknown DUF466 family—in various Epsilonproteobacteria, but not in H. pylori. We found that a complete system for selenocysteine incorporation was present in the Helicobacteriaceae ancestor and has been recently lost before the split of Helicobacter acinonychis and H. pylori. Ourresults indicate that H.pylori, at variance withother gastric andenterohepatic Helicobacter,does not use selenocysteine inprotein synthesis and does not use selenium for tRNAwobble basemodification.However, selAhas survived as a functional gene, having lost the domain for the binding of selenocysteine tRNA, but maintaining the ability to bind the PLP cofactor. The evolutionary modifications described for the SelA protein of H. pylori find parallels in other bacterial and archaeal species, suggesting that an alternative enzymatic function is hidden in many proteins annotated as selenocysteinyl-tRNA synthase.
- Publication
Genome Biology & Evolution, 2015, Vol 7, Issue 9, p2692
- ISSN
1759-6653
- Publication type
Article
- DOI
10.1093/gbe/evv177