Human Lsg1 defines a family of essential GTPases that correlates with the evolution of compartmentalization

• Main Authors: Scheffzek Klaus, Knop Michael, Ly Thi, Bonneau Fabien, Andrade Miguel A, Reynaud Emmanuel G, Pepperkok Rainer
• Format: Article
• Language: English
• Published: BMC 2005-10-01
• Series: BMC Biology
• Online Access: http://www.biomedcentral.com/1741-7007/3/21

<p>Abstract</p> <p>Background</p> <p>Compartmentalization is a key feature of eukaryotic cells, but its evolution remains poorly understood. GTPases are the oldest enzymes that use nucleotides as substrates and they participate in a wide range of cellular processes. Therefore, they are ideal tools for comparative genomic studies aimed at understanding how aspects of biological complexity such as cellular compartmentalization evolved.</p> <p>Results</p> <p>We describe the identification and characterization of a unique family of circularly permuted GTPases represented by the human orthologue of yeast Lsg1p. We placed the members of this family in the phylogenetic context of the <b>Y</b>lqF <b>R</b>elated <b>G</b>TPase (YRG) family, which are present in Eukarya, Bacteria and Archea and include the stem cell regulator Nucleostemin. To extend the computational analysis, we showed that hLsg1 is an essential GTPase predominantly located in the endoplasmic reticulum and, in some cells, in Cajal bodies in the nucleus. Comparison of localization and siRNA datasets suggests that all members of the family are essential GTPases that have increased in number as the compartmentalization of the eukaryotic cell and the ribosome biogenesis pathway have evolved.</p> <p>Conclusion</p> <p>We propose a scenario, consistent with our data, for the evolution of this family: cytoplasmic components were first acquired, followed by nuclear components, and finally the mitochondrial and chloroplast elements were derived from different bacterial species, in parallel with the formation of the nucleolus and the specialization of nuclear components.</p>