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Data from: Evolution and diversification of the organellar release factor family


Duarte, Isabel; Nabuurs, Sander B.; Magno, Ramiro; Huynen, Martijn (2012), Data from: Evolution and diversification of the organellar release factor family, Dryad, Dataset,


Translation termination is accomplished by proteins of the Class I release factor family (RF) that recognize stop codons and catalyze the ribosomal release of the newly synthesized peptide. Bacteria have two canonical RFs: RF1 recognizes UAA and UAG, RF2 recognizes UAA and UGA. Despite that these 2 release factor proteins are sufficient for de facto translation termination, the eukaryotic organellar RF protein family, which has evolved from bacterial release factors, has expanded considerably, comprising multiple subfamilies, most of which have not been functionally characterized or formally classified. Here we integrate multiple sources of information to analyze the remarkable differentiation of the RF family among organelles. We document the origin, phylogenetic distribution and sequence structure features of the mitochondrial and plastidial release factors: mtRF1a, mtRF1, mtRF2a, mtRF2b, mtRF2c, ICT1, C12orf65, pRF1 and pRF2, and review published relevant experimental data. The canonical release factors (mtRF1a, mtRF2a, pRF1 and pRF2) and ICT1 are derived from bacterial ancestors, while the others have resulted from gene duplications of another release factor. These new RF family members have all lost one or more specific motifs relevant for bona fide release factor function but are mostly targeted to the same organelle as their ancestor. We also characterize the subset of canonical release factor proteins that bear non-classical PxT/SPF tripeptide motifs, and provide a molecular-model-based rationale for their retained ability to recognize stop codons. Finally we analyze the co-evolution of canonical RFs with the organellar genetic code. Although the RF presence in an organelle and its stop codon usage tend to co-evolve, we find three taxa that encode an RF2 without using UGA stop codons, and one reverse scenario, where mamiellales green algae use UGA stop codons in their mitochondria without having a mitochondrial type RF2. For the latter we put forward a “stop-codon re-invention” hypothesis that involves the retargeting of the plastid release factor to the mitochondrion.

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