Dynamic interactions within sub-complexes of the H/ACA pseudouridylation guide RNP

H/ACA RNP complexes change uridines to pseudouridines in target non-coding RNAs in eukaryotes and archaea. H/ACA RNPs are comprised of a guide RNA and four essential proteins: Cbf5 (pseudouridine synthase), L7Ae, Gar1 and Nop10 in archaea. The guide RNA captures the target RNA via two antisense elem...

Full description

Bibliographic Details
Main Authors:	Youssef, Osama A., Terns, Rebecca M., Terns, Michael P.
Format:	Online
Language:	English
Published:	Oxford University Press 2007
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2094053/

id	pubmed-2094053
recordtype	oai_dc
spelling	pubmed-20940532007-12-03 Dynamic interactions within sub-complexes of the H/ACA pseudouridylation guide RNP Youssef, Osama A. Terns, Rebecca M. Terns, Michael P. Molecular Biology H/ACA RNP complexes change uridines to pseudouridines in target non-coding RNAs in eukaryotes and archaea. H/ACA RNPs are comprised of a guide RNA and four essential proteins: Cbf5 (pseudouridine synthase), L7Ae, Gar1 and Nop10 in archaea. The guide RNA captures the target RNA via two antisense elements brought together to form a contiguous binding site within the pseudouridylation pocket (internal loop) of the guide RNA. Cbf5 and L7Ae interact independently with the guide RNA, and here we have examined the impacts of these proteins on the RNA in nucleotide protection assays. The results indicate that the interactions observed in a fully assembled H/ACA RNP are established in the sub-complexes, but also reveal a unique Cbf5–guide RNA interaction that is displaced by L7Ae. In addition, the results indicate that L7Ae binding at the kink (k)-turn of the guide RNA induces the formation of the upper stem, and thus also the pseudouridylation pocket. Our findings indicate that L7Ae is essential for formation of the substrate RNA binding site in the archaeal H/ACA RNP, and suggest that k-turn-binding proteins may remodel partner RNAs with important effects distant from the protein-binding site. Oxford University Press 2007-09 2007-09-12 /pmc/articles/PMC2094053/ /pubmed/17855403 http://dx.doi.org/10.1093/nar/gkm673 Text en © 2007 The Author(s) http://creativecommons.org/licenses/by-nc/2.0/uk/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Youssef, Osama A. Terns, Rebecca M. Terns, Michael P.
spellingShingle	Youssef, Osama A. Terns, Rebecca M. Terns, Michael P. Dynamic interactions within sub-complexes of the H/ACA pseudouridylation guide RNP
author_facet	Youssef, Osama A. Terns, Rebecca M. Terns, Michael P.
author_sort	Youssef, Osama A.
title	Dynamic interactions within sub-complexes of the H/ACA pseudouridylation guide RNP
title_short	Dynamic interactions within sub-complexes of the H/ACA pseudouridylation guide RNP
title_full	Dynamic interactions within sub-complexes of the H/ACA pseudouridylation guide RNP
title_fullStr	Dynamic interactions within sub-complexes of the H/ACA pseudouridylation guide RNP
title_full_unstemmed	Dynamic interactions within sub-complexes of the H/ACA pseudouridylation guide RNP
title_sort	dynamic interactions within sub-complexes of the h/aca pseudouridylation guide rnp
description	H/ACA RNP complexes change uridines to pseudouridines in target non-coding RNAs in eukaryotes and archaea. H/ACA RNPs are comprised of a guide RNA and four essential proteins: Cbf5 (pseudouridine synthase), L7Ae, Gar1 and Nop10 in archaea. The guide RNA captures the target RNA via two antisense elements brought together to form a contiguous binding site within the pseudouridylation pocket (internal loop) of the guide RNA. Cbf5 and L7Ae interact independently with the guide RNA, and here we have examined the impacts of these proteins on the RNA in nucleotide protection assays. The results indicate that the interactions observed in a fully assembled H/ACA RNP are established in the sub-complexes, but also reveal a unique Cbf5–guide RNA interaction that is displaced by L7Ae. In addition, the results indicate that L7Ae binding at the kink (k)-turn of the guide RNA induces the formation of the upper stem, and thus also the pseudouridylation pocket. Our findings indicate that L7Ae is essential for formation of the substrate RNA binding site in the archaeal H/ACA RNP, and suggest that k-turn-binding proteins may remodel partner RNAs with important effects distant from the protein-binding site.
publisher	Oxford University Press
publishDate	2007
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2094053/
_version_	1611408306411143168

Dynamic interactions within sub-complexes of the H/ACA pseudouridylation guide RNP

Similar Items