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Adjustments, extinction, and remains of selenocysteine incorporation machinery in the nematode lineage

Selenocysteine (Sec) is encoded by an UGA codon with the help of a SECIS element present in selenoprotein mRNAs. SECIS-binding protein (SBP2/SCBP-2) mediates Sec insertion, but the roles of its domains and the impact of its deficiency on Sec insertion are not fully understood. We used Caenorhabditis...

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Autores principales: Otero, Lucía, Romanelli-Cedrez, Laura, Turanov, Anton A., Gladyshev, Vadim N., Miranda-Vizuete, Antonio, Salinas, Gustavo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory Press 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4114682/
https://www.ncbi.nlm.nih.gov/pubmed/24817701
http://dx.doi.org/10.1261/rna.043877.113
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author Otero, Lucía
Romanelli-Cedrez, Laura
Turanov, Anton A.
Gladyshev, Vadim N.
Miranda-Vizuete, Antonio
Salinas, Gustavo
author_facet Otero, Lucía
Romanelli-Cedrez, Laura
Turanov, Anton A.
Gladyshev, Vadim N.
Miranda-Vizuete, Antonio
Salinas, Gustavo
author_sort Otero, Lucía
collection PubMed
description Selenocysteine (Sec) is encoded by an UGA codon with the help of a SECIS element present in selenoprotein mRNAs. SECIS-binding protein (SBP2/SCBP-2) mediates Sec insertion, but the roles of its domains and the impact of its deficiency on Sec insertion are not fully understood. We used Caenorhabditis elegans to examine SBP2 function since it possesses a single selenoprotein, thioredoxin reductase-1 (TRXR-1). All SBP2 described so far have an RNA-binding domain (RBD) and a Sec-incorporation domain (SID). Surprisingly, C. elegans SBP2 lacks SID and consists only of an RBD. An sbp2 deletion mutant strain ablated Sec incorporation demonstrating SBP2 essentiality for Sec incorporation. Further in silico analyses of nematode genomes revealed conservation of SBP2 lacking SID and maintenance of Sec incorporation linked to TRXR-1. Remarkably, parasitic plant nematodes lost the ability to incorporate Sec, but retained SecP43, a gene associated with Sec incorporation. Interestingly, both selenophosphate synthetase (SPS) genes are absent in plant parasitic nematodes, while only Cys-containing SPS2 is present in Sec-incorporating nematodes. Our results indicate that C. elegans and the nematode lineage provide key insights into Sec incorporation and the evolution of Sec utilization trait, selenoproteomes, selenoproteins, and Sec residues. Finally, our study provides evidence of noncanonical translation initiation in C. elegans, not previously known for this well-established animal model.
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spelling pubmed-41146822015-07-01 Adjustments, extinction, and remains of selenocysteine incorporation machinery in the nematode lineage Otero, Lucía Romanelli-Cedrez, Laura Turanov, Anton A. Gladyshev, Vadim N. Miranda-Vizuete, Antonio Salinas, Gustavo RNA Articles Selenocysteine (Sec) is encoded by an UGA codon with the help of a SECIS element present in selenoprotein mRNAs. SECIS-binding protein (SBP2/SCBP-2) mediates Sec insertion, but the roles of its domains and the impact of its deficiency on Sec insertion are not fully understood. We used Caenorhabditis elegans to examine SBP2 function since it possesses a single selenoprotein, thioredoxin reductase-1 (TRXR-1). All SBP2 described so far have an RNA-binding domain (RBD) and a Sec-incorporation domain (SID). Surprisingly, C. elegans SBP2 lacks SID and consists only of an RBD. An sbp2 deletion mutant strain ablated Sec incorporation demonstrating SBP2 essentiality for Sec incorporation. Further in silico analyses of nematode genomes revealed conservation of SBP2 lacking SID and maintenance of Sec incorporation linked to TRXR-1. Remarkably, parasitic plant nematodes lost the ability to incorporate Sec, but retained SecP43, a gene associated with Sec incorporation. Interestingly, both selenophosphate synthetase (SPS) genes are absent in plant parasitic nematodes, while only Cys-containing SPS2 is present in Sec-incorporating nematodes. Our results indicate that C. elegans and the nematode lineage provide key insights into Sec incorporation and the evolution of Sec utilization trait, selenoproteomes, selenoproteins, and Sec residues. Finally, our study provides evidence of noncanonical translation initiation in C. elegans, not previously known for this well-established animal model. Cold Spring Harbor Laboratory Press 2014-07 /pmc/articles/PMC4114682/ /pubmed/24817701 http://dx.doi.org/10.1261/rna.043877.113 Text en © 2014 Otero et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society http://creativecommons.org/licenses/by-nc/4.0/ This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.
spellingShingle Articles
Otero, Lucía
Romanelli-Cedrez, Laura
Turanov, Anton A.
Gladyshev, Vadim N.
Miranda-Vizuete, Antonio
Salinas, Gustavo
Adjustments, extinction, and remains of selenocysteine incorporation machinery in the nematode lineage
title Adjustments, extinction, and remains of selenocysteine incorporation machinery in the nematode lineage
title_full Adjustments, extinction, and remains of selenocysteine incorporation machinery in the nematode lineage
title_fullStr Adjustments, extinction, and remains of selenocysteine incorporation machinery in the nematode lineage
title_full_unstemmed Adjustments, extinction, and remains of selenocysteine incorporation machinery in the nematode lineage
title_short Adjustments, extinction, and remains of selenocysteine incorporation machinery in the nematode lineage
title_sort adjustments, extinction, and remains of selenocysteine incorporation machinery in the nematode lineage
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4114682/
https://www.ncbi.nlm.nih.gov/pubmed/24817701
http://dx.doi.org/10.1261/rna.043877.113
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