Phylogenetic and genomic analyses of the ribosomal oxygenases Riox1 (No66) and Riox2 (Mina53) provide new insights into their evolution

Autor:	Jasmin Moneer, Annette Feuchtinger, Katharina E Bräuer, Kevin Brockers, Andreas Lengeling, Evi Wollscheid-Lengeling, Alexander Wolf
Jazyk:	angličtina
Rok vydání:	2018
Předmět:	0301 basic medicine Chromosomal Proteins Non-Histone Hydra Ribosome Conserved Sequence Phylogeny Single exon genes Histone Demethylases Mina53 Phylogenetic tree Nuclear Proteins Translation (biology) Genomics Ribosomal Oxygenases Fe(ii) And 2-oxoglutarate Dependent Oxygenases Hydroxylation Jmjc Jumonji No66 Single Exon Genes Intronless Retroposed Gene Copies Neoplasm Proteins Fe(II) and 2-oxoglutarate dependent oxygenases JmjC Protein Transport Oxygenases Lernaean Hydra Genetics & genetic processes [F10] [Life sciences] Génétique & processus génétiques [F10] [Sciences du vivant] NO66 Research Article Evolution Protein domain Biology Dioxygenases Evolution Molecular 03 medical and health sciences Protein Domains Species Specificity Ribosomal protein QH359-425 Animals Humans Amino Acid Sequence Gene Ecology Evolution Behavior and Systematics Cell Nucleus Intronless retroposed gene copies Ribosomal RNA 030104 developmental biology Evolutionary biology Ribosomes Ribosomal oxygenases HeLa Cells
Zdroj:	BMC Evolutionary Biology, Vol 18, Iss 1, Pp 1-16 (2018) BMC Evolutionary Biology Bräuer, K E, Brockers, K, Moneer, J, Feuchtinger, A, Wollscheid-Lengeling, E, Lengeling, A & Wolf, A 2018, ' Phylogenetic and genomic analyses of the ribosomal oxygenases Riox1 (No66) and Riox2 (Mina53) provide new insights into their evolution ', BMC Evolutionary Biology, vol. 18, no. 1, pp. 96 . https://doi.org/10.1186/s12862-018-1215-0 BMC Evol. Biol. 18:96 (2018)
ISSN:	1471-2148
DOI:	10.1186/s12862-018-1215-0
Popis:	Background Translation of specific mRNAs can be highly regulated in different cells, tissues or under pathological conditions. Ribosome heterogeneity can originate from variable expression or post-translational modifications of ribosomal proteins. The ribosomal oxygenases RIOX1 (NO66) and RIOX2 (MINA53) modify ribosomal proteins by histidine hydroxylation. A similar mechanism is present in prokaryotes. Thus, ribosome hydroxylation may be a well-conserved regulatory mechanism with implications in disease and development. However, little is known about the evolutionary history of Riox1 and Riox2 genes and their encoded proteins across eukaryotic taxa. Results In this study, we have analysed Riox1 and Riox2 orthologous genes from 49 metazoen species and have constructed phylogenomic trees for both genes. Our genomic and phylogenetic analyses revealed that Arthropoda, Annelida, Nematoda and Mollusca lack the Riox2 gene, although in the early phylum Cnidaria both genes, Riox1 and Riox2, are present and expressed. Riox1 is an intronless single-exon-gene in several species, including humans. In contrast to Riox2, Riox1 is ubiquitously present throughout the animal kingdom suggesting that Riox1 is the phylogenetically older gene from which Riox2 has evolved. Both proteins have maintained a unique protein architecture with conservation of active sites within the JmjC domains, a dimerization domain, and a winged-helix domain. In addition, Riox1 proteins possess a unique N-terminal extension domain. Immunofluorescence analyses in Hela cells and in Hydra vulgaris identified a nucleolar localisation signal within the extended N-terminal domain of human RIOX1 and an altered subnuclear localisation for the Hydra Riox2. Conclusions Conserved active site residues and uniform protein domain architecture suggest a consistent enzymatic activity within the Riox orthologs throughout evolution. However, differences in genomic architecture, like single exon genes and alterations in subnuclear localisation, as described for Hydra, point towards adaption mechanisms that may correlate with taxa- or species-specific requirements. The diversification of Riox1/Riox2 gene structures throughout evolution suggest that functional requirements in expression of protein isoforms and/or subcellular localisation of proteins may have evolved by adaptation to lifestyle. Electronic supplementary material The online version of this article (10.1186/s12862-018-1215-0) contains supplementary material, which is available to authorized users.
Databáze:	OpenAIRE
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