Cargando…
Crucial role of the Rcl1p–Bms1p interaction for yeast pre-ribosomal RNA processing
The essential Rcl1p and Bms1p proteins form a complex required for 40S ribosomal subunit maturation. Bms1p is a GTPase and Rcl1p has been proposed to catalyse the endonucleolytic cleavage at site A(2) separating the pre-40S and pre-60S maturation pathways. We determined the 2.0 Å crystal structure o...
Autores principales: | , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4150785/ https://www.ncbi.nlm.nih.gov/pubmed/25064857 http://dx.doi.org/10.1093/nar/gku682 |
_version_ | 1782332955147894784 |
---|---|
author | Delprato, Anna Kadri, Yasmine Al Pérébaskine, Natacha Monfoulet, Cécile Henry, Yves Henras, Anthony K. Fribourg, Sébastien |
author_facet | Delprato, Anna Kadri, Yasmine Al Pérébaskine, Natacha Monfoulet, Cécile Henry, Yves Henras, Anthony K. Fribourg, Sébastien |
author_sort | Delprato, Anna |
collection | PubMed |
description | The essential Rcl1p and Bms1p proteins form a complex required for 40S ribosomal subunit maturation. Bms1p is a GTPase and Rcl1p has been proposed to catalyse the endonucleolytic cleavage at site A(2) separating the pre-40S and pre-60S maturation pathways. We determined the 2.0 Å crystal structure of Bms1p associated with Rcl1p. We demonstrate that Rcl1p nuclear import depends on Bms1p and that the two proteins are loaded into pre-ribosomes at a similar stage of the maturation pathway and remain present within pre-ribosomes after cleavage at A(2). Importantly, GTP binding to Bms1p is not required for the import in the nucleus nor for the incorporation of Rcl1p into pre-ribosomes, but is essential for early pre-rRNA processing. We propose that GTP binding to Bms1p and/or GTP hydrolysis may induce conformational rearrangements within the Bms1p-Rcl1p complex allowing the interaction of Rcl1p with its RNA substrate. |
format | Online Article Text |
id | pubmed-4150785 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-41507852014-12-01 Crucial role of the Rcl1p–Bms1p interaction for yeast pre-ribosomal RNA processing Delprato, Anna Kadri, Yasmine Al Pérébaskine, Natacha Monfoulet, Cécile Henry, Yves Henras, Anthony K. Fribourg, Sébastien Nucleic Acids Res Structural Biology The essential Rcl1p and Bms1p proteins form a complex required for 40S ribosomal subunit maturation. Bms1p is a GTPase and Rcl1p has been proposed to catalyse the endonucleolytic cleavage at site A(2) separating the pre-40S and pre-60S maturation pathways. We determined the 2.0 Å crystal structure of Bms1p associated with Rcl1p. We demonstrate that Rcl1p nuclear import depends on Bms1p and that the two proteins are loaded into pre-ribosomes at a similar stage of the maturation pathway and remain present within pre-ribosomes after cleavage at A(2). Importantly, GTP binding to Bms1p is not required for the import in the nucleus nor for the incorporation of Rcl1p into pre-ribosomes, but is essential for early pre-rRNA processing. We propose that GTP binding to Bms1p and/or GTP hydrolysis may induce conformational rearrangements within the Bms1p-Rcl1p complex allowing the interaction of Rcl1p with its RNA substrate. Oxford University Press 2014-09-02 2014-07-26 /pmc/articles/PMC4150785/ /pubmed/25064857 http://dx.doi.org/10.1093/nar/gku682 Text en © The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Structural Biology Delprato, Anna Kadri, Yasmine Al Pérébaskine, Natacha Monfoulet, Cécile Henry, Yves Henras, Anthony K. Fribourg, Sébastien Crucial role of the Rcl1p–Bms1p interaction for yeast pre-ribosomal RNA processing |
title | Crucial role of the Rcl1p–Bms1p interaction for yeast pre-ribosomal RNA processing |
title_full | Crucial role of the Rcl1p–Bms1p interaction for yeast pre-ribosomal RNA processing |
title_fullStr | Crucial role of the Rcl1p–Bms1p interaction for yeast pre-ribosomal RNA processing |
title_full_unstemmed | Crucial role of the Rcl1p–Bms1p interaction for yeast pre-ribosomal RNA processing |
title_short | Crucial role of the Rcl1p–Bms1p interaction for yeast pre-ribosomal RNA processing |
title_sort | crucial role of the rcl1p–bms1p interaction for yeast pre-ribosomal rna processing |
topic | Structural Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4150785/ https://www.ncbi.nlm.nih.gov/pubmed/25064857 http://dx.doi.org/10.1093/nar/gku682 |
work_keys_str_mv | AT delpratoanna crucialroleofthercl1pbms1pinteractionforyeastpreribosomalrnaprocessing AT kadriyasmineal crucialroleofthercl1pbms1pinteractionforyeastpreribosomalrnaprocessing AT perebaskinenatacha crucialroleofthercl1pbms1pinteractionforyeastpreribosomalrnaprocessing AT monfouletcecile crucialroleofthercl1pbms1pinteractionforyeastpreribosomalrnaprocessing AT henryyves crucialroleofthercl1pbms1pinteractionforyeastpreribosomalrnaprocessing AT henrasanthonyk crucialroleofthercl1pbms1pinteractionforyeastpreribosomalrnaprocessing AT fribourgsebastien crucialroleofthercl1pbms1pinteractionforyeastpreribosomalrnaprocessing |