Reading the Evolution of Compartmentalization in the Ribosome Assembly Toolbox: The YRG Protein Family
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Title: | Reading the Evolution of Compartmentalization in the Ribosome Assembly Toolbox: The YRG Protein Family | Authors: | Mier, Pablo; Pérez-Pulido, Antonio J.; Reynaud, Emmanuel G.; Andrade, Miguel A. | Permanent link: | http://hdl.handle.net/10197/11793 | Date: | 10-Jan-2017 | Online since: | 2020-12-08T14:16:59Z | Abstract: | Reconstructing the transition from a single compartment bacterium to a highly compartmentalized eukaryotic cell is one of the most studied problems of evolutionary cell biology. However, timing and details of the establishment of compartmentalization are unclear and difficult to assess. Here, we propose the use of molecular markers specific to cellular compartments to set up a framework to advance the understanding of this complex intracellular process. Specifically, we use a protein family related to ribosome biogenesis, YRG (YlqF related GTPases), whose evolution is linked to the establishment of cellular compartments, leveraging the current genomic data. We analyzed orthologous proteins of the YRG family in a set of 171 proteomes for a total of 370 proteins. We identified ten YRG protein subfamilies that can be associated to six subcellular compartments (nuclear bodies, nucleolus, nucleus, cytosol, mitochondria, and chloroplast), and which were found in archaeal, bacterial and eukaryotic proteomes. Our analysis reveals organism streamlining related events in specific taxonomic groups such as Fungi. We conclude that the YRG family could be used as a compartmentalization marker, which could help to trace the evolutionary path relating cellular compartments with ribosome biogenesis. | Type of material: | Journal Article | Publisher: | PLoS | Journal: | PLoS ONE | Volume: | 12 | Issue: | 1 | Copyright (published version): | 2017 the Authors | Keywords: | Ribosomes; Animals; GTP phosphohydrolases; Archaeal proteins; Bacterial proteins; Fungal proteins; Molecular evolution; Cell compartmentation; Protein transport | DOI: | 10.1371/journal.pone.0169750 | Language: | en | Status of Item: | Peer reviewed | ISSN: | 1932-6203 | This item is made available under a Creative Commons License: | https://creativecommons.org/licenses/by-nc-nd/3.0/ie/ |
Appears in Collections: | Biomolecular and Biomedical Science Research Collection |
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