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Ribosomal protein L14 contributes to the early assembly of 60S ribosomal subunits in Saccharomyces cerevisiae.
Nucleic Acids Res. 2018 05 18; 46(9):4715-4732.NA

Abstract

The contribution of most ribosomal proteins to ribosome synthesis has been quite well analysed in Saccharomyces cerevisiae. However, few yeast ribosomal proteins still await characterization. Herein, we show that L14, an essential 60S ribosomal protein, assembles in the nucleolus at an early stage into pre-60S particles. Depletion of L14 results in a deficit in 60S subunits and defective processing of 27SA2 and 27SA3 to 27SB pre-rRNAs. As a result, 27S pre-rRNAs are subjected to turnover and export of pre-60S particles is blocked. These phenotypes likely appear as the direct consequence of the reduced pre-60S particle association not only of L14 upon its depletion but also of a set of neighboring ribosomal proteins located at the solvent interface of 60S subunits and the adjacent region surrounding the polypeptide exit tunnel. These pre-60S intermediates also lack some essential trans-acting factors required for 27SB pre-rRNA processing but accumulate practically all factors required for processing of 27SA3 pre-rRNA. We have also analysed the functional interaction between the eukaryote-specific carboxy-terminal extensions of the neighboring L14 and L16 proteins. Our results indicate that removal of the most distal parts of these extensions cause slight translation alterations in mature 60S subunits.

Authors+Show Affiliations

Instituto de Biomedicina de Sevilla (IBiS), Hospital Universitario Virgen del Rocío/CSIC/Universidad de Sevilla, and Departamento de Genética, Universidad de Sevilla, Seville, Spain. Avda. Manuel Siurot, E-41013 Seville, Spain.Instituto de Biomedicina de Sevilla (IBiS), Hospital Universitario Virgen del Rocío/CSIC/Universidad de Sevilla, and Departamento de Genética, Universidad de Sevilla, Seville, Spain. Avda. Manuel Siurot, E-41013 Seville, Spain.Instituto de Biomedicina de Sevilla (IBiS), Hospital Universitario Virgen del Rocío/CSIC/Universidad de Sevilla, and Departamento de Genética, Universidad de Sevilla, Seville, Spain. Avda. Manuel Siurot, E-41013 Seville, Spain.Institut für Biochemie III, Universität Regensburg, 93053, Regensburg, Germany.Instituto de Biomedicina de Sevilla (IBiS), Hospital Universitario Virgen del Rocío/CSIC/Universidad de Sevilla, and Departamento de Genética, Universidad de Sevilla, Seville, Spain. Avda. Manuel Siurot, E-41013 Seville, Spain.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

29788267

Citation

Espinar-Marchena, Francisco, et al. "Ribosomal Protein L14 Contributes to the Early Assembly of 60S Ribosomal Subunits in Saccharomyces Cerevisiae." Nucleic Acids Research, vol. 46, no. 9, 2018, pp. 4715-4732.
Espinar-Marchena F, Rodríguez-Galán O, Fernández-Fernández J, et al. Ribosomal protein L14 contributes to the early assembly of 60S ribosomal subunits in Saccharomyces cerevisiae. Nucleic Acids Res. 2018;46(9):4715-4732.
Espinar-Marchena, F., Rodríguez-Galán, O., Fernández-Fernández, J., Linnemann, J., & de la Cruz, J. (2018). Ribosomal protein L14 contributes to the early assembly of 60S ribosomal subunits in Saccharomyces cerevisiae. Nucleic Acids Research, 46(9), 4715-4732. https://doi.org/10.1093/nar/gky123
Espinar-Marchena F, et al. Ribosomal Protein L14 Contributes to the Early Assembly of 60S Ribosomal Subunits in Saccharomyces Cerevisiae. Nucleic Acids Res. 2018 05 18;46(9):4715-4732. PubMed PMID: 29788267.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Ribosomal protein L14 contributes to the early assembly of 60S ribosomal subunits in Saccharomyces cerevisiae. AU - Espinar-Marchena,Francisco, AU - Rodríguez-Galán,Olga, AU - Fernández-Fernández,José, AU - Linnemann,Jan, AU - de la Cruz,Jesús, PY - 2017/06/01/received PY - 2018/02/12/accepted PY - 2018/5/23/entrez PY - 2018/5/23/pubmed PY - 2019/7/23/medline SP - 4715 EP - 4732 JF - Nucleic acids research JO - Nucleic Acids Res. VL - 46 IS - 9 N2 - The contribution of most ribosomal proteins to ribosome synthesis has been quite well analysed in Saccharomyces cerevisiae. However, few yeast ribosomal proteins still await characterization. Herein, we show that L14, an essential 60S ribosomal protein, assembles in the nucleolus at an early stage into pre-60S particles. Depletion of L14 results in a deficit in 60S subunits and defective processing of 27SA2 and 27SA3 to 27SB pre-rRNAs. As a result, 27S pre-rRNAs are subjected to turnover and export of pre-60S particles is blocked. These phenotypes likely appear as the direct consequence of the reduced pre-60S particle association not only of L14 upon its depletion but also of a set of neighboring ribosomal proteins located at the solvent interface of 60S subunits and the adjacent region surrounding the polypeptide exit tunnel. These pre-60S intermediates also lack some essential trans-acting factors required for 27SB pre-rRNA processing but accumulate practically all factors required for processing of 27SA3 pre-rRNA. We have also analysed the functional interaction between the eukaryote-specific carboxy-terminal extensions of the neighboring L14 and L16 proteins. Our results indicate that removal of the most distal parts of these extensions cause slight translation alterations in mature 60S subunits. SN - 1362-4962 UR - https://www.unboundmedicine.com/medline/citation/29788267/Ribosomal_protein_L14_contributes_to_the_early_assembly_of_60S_ribosomal_subunits_in_Saccharomyces_cerevisiae_ L2 - https://academic.oup.com/nar/article-lookup/doi/10.1093/nar/gky123 DB - PRIME DP - Unbound Medicine ER -