RNA mimicry by the fap7 adenylate kinase in ribosome biogenesis.

During biogenesis of the 40S and 60S ribosomal subunits, the pre-40S particles are exported to the cytoplasm prior to final cleavage of the 20S pre-rRNA to mature 18S rRNA. Amongst the factors involved in this maturation step, Fap7 is unusual, as it both interacts with ribosomal protein Rps14 and ha...

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Autores principales:	Jérôme Loc'h, Magali Blaud, Stéphane Réty, Simon Lebaron, Patrick Deschamps, Joseph Bareille, Julie Jombart, Julien Robert-Paganin, Lila Delbos, Florian Chardon, Elodie Zhang, Clément Charenton, David Tollervey, Nicolas Leulliot
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/b5bc28e3f7a5415191a558049d3855ae
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spelling	oai:doaj.org-article:b5bc28e3f7a5415191a558049d3855ae2021-11-18T05:37:27ZRNA mimicry by the fap7 adenylate kinase in ribosome biogenesis.1544-91731545-788510.1371/journal.pbio.1001860https://doaj.org/article/b5bc28e3f7a5415191a558049d3855ae2014-05-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24823650/?tool=EBIhttps://doaj.org/toc/1544-9173https://doaj.org/toc/1545-7885During biogenesis of the 40S and 60S ribosomal subunits, the pre-40S particles are exported to the cytoplasm prior to final cleavage of the 20S pre-rRNA to mature 18S rRNA. Amongst the factors involved in this maturation step, Fap7 is unusual, as it both interacts with ribosomal protein Rps14 and harbors adenylate kinase activity, a function not usually associated with ribonucleoprotein assembly. Human hFap7 also regulates Cajal body assembly and cell cycle progression via the p53-MDM2 pathway. This work presents the functional and structural characterization of the Fap7-Rps14 complex. We report that Fap7 association blocks the RNA binding surface of Rps14 and, conversely, Rps14 binding inhibits adenylate kinase activity of Fap7. In addition, the affinity of Fap7 for Rps14 is higher with bound ADP, whereas ATP hydrolysis dissociates the complex. These results suggest that Fap7 chaperones Rps14 assembly into pre-40S particles via RNA mimicry in an ATP-dependent manner. Incorporation of Rps14 by Fap7 leads to a structural rearrangement of the platform domain necessary for the pre-rRNA to acquire a cleavage competent conformation.Jérôme Loc'hMagali BlaudStéphane RétySimon LebaronPatrick DeschampsJoseph BareilleJulie JombartJulien Robert-PaganinLila DelbosFlorian ChardonElodie ZhangClément CharentonDavid TollerveyNicolas LeulliotPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 12, Iss 5, p e1001860 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Jérôme Loc'h Magali Blaud Stéphane Réty Simon Lebaron Patrick Deschamps Joseph Bareille Julie Jombart Julien Robert-Paganin Lila Delbos Florian Chardon Elodie Zhang Clément Charenton David Tollervey Nicolas Leulliot RNA mimicry by the fap7 adenylate kinase in ribosome biogenesis.
description	During biogenesis of the 40S and 60S ribosomal subunits, the pre-40S particles are exported to the cytoplasm prior to final cleavage of the 20S pre-rRNA to mature 18S rRNA. Amongst the factors involved in this maturation step, Fap7 is unusual, as it both interacts with ribosomal protein Rps14 and harbors adenylate kinase activity, a function not usually associated with ribonucleoprotein assembly. Human hFap7 also regulates Cajal body assembly and cell cycle progression via the p53-MDM2 pathway. This work presents the functional and structural characterization of the Fap7-Rps14 complex. We report that Fap7 association blocks the RNA binding surface of Rps14 and, conversely, Rps14 binding inhibits adenylate kinase activity of Fap7. In addition, the affinity of Fap7 for Rps14 is higher with bound ADP, whereas ATP hydrolysis dissociates the complex. These results suggest that Fap7 chaperones Rps14 assembly into pre-40S particles via RNA mimicry in an ATP-dependent manner. Incorporation of Rps14 by Fap7 leads to a structural rearrangement of the platform domain necessary for the pre-rRNA to acquire a cleavage competent conformation.
format	article
author	Jérôme Loc'h Magali Blaud Stéphane Réty Simon Lebaron Patrick Deschamps Joseph Bareille Julie Jombart Julien Robert-Paganin Lila Delbos Florian Chardon Elodie Zhang Clément Charenton David Tollervey Nicolas Leulliot
author_facet	Jérôme Loc'h Magali Blaud Stéphane Réty Simon Lebaron Patrick Deschamps Joseph Bareille Julie Jombart Julien Robert-Paganin Lila Delbos Florian Chardon Elodie Zhang Clément Charenton David Tollervey Nicolas Leulliot
author_sort	Jérôme Loc'h
title	RNA mimicry by the fap7 adenylate kinase in ribosome biogenesis.
title_short	RNA mimicry by the fap7 adenylate kinase in ribosome biogenesis.
title_full	RNA mimicry by the fap7 adenylate kinase in ribosome biogenesis.
title_fullStr	RNA mimicry by the fap7 adenylate kinase in ribosome biogenesis.
title_full_unstemmed	RNA mimicry by the fap7 adenylate kinase in ribosome biogenesis.
title_sort	rna mimicry by the fap7 adenylate kinase in ribosome biogenesis.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/b5bc28e3f7a5415191a558049d3855ae
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RNA mimicry by the fap7 adenylate kinase in ribosome biogenesis.

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