Characterization of the Trypanosoma cruzi ortholog of the SBDS protein reveals an intrinsically disordered extended C-terminal region showing RNA-interacting activity |
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Authors: | Juliana Ferreira de Oliveira Beatriz A Castilho Mauricio L Sforça Marco Aurélio Krieger Ana Carolina Zeri Beatriz G Guimarães Nilson IT Zanchin |
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Institution: | 1. Center for Structural Molecular Biology, Brazilian Synchrotron Light Laboratory, LNLS, Rua Giuseppe Maximo Scolfaro 10000, PO Box 6192, CEP13083-970, Campinas SP, Brazil;2. Department of Microbiology, Immunology and Parasitology, Universidade Federal de São Paulo, Rua Botucatu 862, São Paulo, SP 04023-062, Brazil;3. Instituto de Biologia Molecular do Paraná, IBMP, Curitiba Paraná, Brazil |
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Abstract: | The human SBDS gene and its yeast ortholog SDO1 encode essential proteins that are involved in ribosome biosynthesis. SDO1 has been implicated in recycling of the ribosomal biogenesis factor Tif6p from pre-66S particles as well as in translation activation of 60S ribosomes. The SBDS protein is highly conserved, containing approximately 250 amino acid residues in animals, fungi and Archaea, while SBDS orthologs of plants and a group of protists contain an extended C-terminal region. In this work, we describe the characterization of the Trypanosoma cruzi SBDS ortholog (TcSBDS). TcSBDS co-fractionates with polysomes in sucrose density gradients, which is consistent with a role in ribosome biosynthesis. We show that TcSBDS contains a C-terminal extension of 200 amino acids that displays the features of intrinsically disordered proteins as determined by proteolytic, circular dichroism and NMR analyses. Interestingly, the C-terminal extension is responsible for TcSBDS–RNA interaction activity in electrophoretic mobility shift assays. This finding suggests that Trypanosomatidae and possibly also other organisms containing SBDS with extended C-terminal regions have evolved an additional function for SBDS in ribosome biogenesis. |
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Keywords: | SBDS ortholog Trypanosoma cruzi RNA-protein interaction Protein structure |
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