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Evolutionary Conservation of the Ribosomal Biogenesis Factor Rbm19/Mrd1: Implications for Function
Karolinska Institutet, Stockholm, Sweden.
Stockholm University, Sweden.
Stockholm University, Sweden.
Linköping University, Department of Physics, Chemistry and Biology, Bioinformatics. Linköping University, The Institute of Technology.
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2012 (English)In: PLoS ONE, ISSN 1932-6203, Vol. 7, no 9Article in journal (Refereed) Published
Abstract [en]

Ribosome biogenesis in eukaryotes requires coordinated folding and assembly of a pre-rRNA into sequential pre-rRNA-protein complexes in which chemical modifications and RNA cleavages occur. These processes require many small nucleolar RNAs (snoRNAs) and proteins. Rbm19/Mrd1 is one such protein that is built from multiple RNA-binding domains (RBDs). We find that Rbm19/Mrd1 with five RBDs is present in all branches of the eukaryotic phylogenetic tree, except in animals and Choanoflagellates, that instead have a version with six RBDs and Microsporidia which have a minimal Rbm19/Mrd1 protein with four RBDs. Rbm19/Mrd1 therefore evolved as a multi-RBD protein very early in eukaryotes. The linkers between the RBDs have conserved properties; they are disordered, except for linker 3, and position the RBDs at conserved relative distances from each other. All but one of the RBDs have conserved properties for RNA-binding and each RBD has a specific consensus sequence and a conserved position in the protein, suggesting a functionally important modular design. The patterns of evolutionary conservation provide information for experimental analyses of the function of Rbm19/Mrd1. In vivo mutational analysis confirmed that a highly conserved loop 5-β4-strand in RBD6 is essential for function.

Place, publisher, year, edition, pages
2012. Vol. 7, no 9
National Category
Bioinformatics and Systems Biology
URN: urn:nbn:se:liu:diva-81955DOI: 10.1371/journal.pone.0043786ISI: 000308738500022OAI: diva2:556845

funding agencies|Swedish Research Council||Carl Tryggers Stiftelse||Linkoping University||

Available from: 2012-09-26 Created: 2012-09-26 Last updated: 2012-11-28

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