Dissection of a rice OsMac1 mRNA 5' UTR to uncover regulatory elements that are responsible for its efficient translation.

The untranslated regions (UTRs) of mRNAs are involved in many posttranscriptional regulatory pathways. The rice OsMac1 mRNA has three splicing variants of the 5' UTR (UTRa, UTRb, and UTRc), which include a CU-rich region and three upstream open reading frames (uORFs). UTRc contains an additiona...

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Autores principales:	Hiromi Mutsuro-Aoki, Hiroshi Teramura, Ryoko Tamukai, Miho Fukui, Hiroaki Kusano, Mikhail Schepetilnikov, Lyubov A Ryabova, Hiroaki Shimada
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/f89c787da8a448079695596c0ae0a1c6
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spelling	oai:doaj.org-article:f89c787da8a448079695596c0ae0a1c62021-12-02T20:09:26ZDissection of a rice OsMac1 mRNA 5' UTR to uncover regulatory elements that are responsible for its efficient translation.1932-620310.1371/journal.pone.0253488https://doaj.org/article/f89c787da8a448079695596c0ae0a1c62021-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0253488https://doaj.org/toc/1932-6203The untranslated regions (UTRs) of mRNAs are involved in many posttranscriptional regulatory pathways. The rice OsMac1 mRNA has three splicing variants of the 5' UTR (UTRa, UTRb, and UTRc), which include a CU-rich region and three upstream open reading frames (uORFs). UTRc contains an additional 38-nt sequence, termed sp38, which acts as a strong translational enhancer of the downstream ORF; reporter analysis revealed translational efficiencies >15-fold higher with UTRc than with the other splice variants. Mutation analysis of UTRc demonstrated that an optimal sequence length of sp38, rather than its nucleotide sequence is essential for UTRc to promote efficient translation. In addition, the 5' 100 nucleotides of CU-rich region contribute to UTRc translational enhancement. Strikingly, three uORFs did not reveal their inhibitory potential within the full-length leader, whereas deletion of the 5' leader fragment preceding the leader region with uORFs nearly abolished translation. Computational prediction of UTRc structural motifs revealed stem-loop structures, termed SL1-SL4, and two regions, A and B, involved in putative intramolecular interactions. Our data suggest that SL4 binding to Region-A and base pairing between Region-B and the UTRc 3'end are critically required for translational enhancement. Since UTRc is not capable of internal initiation, we presume that the three-dimensional leader structures can allow translation of the leader downstream ORF, likely allowing the bypass of uORFs.Hiromi Mutsuro-AokiHiroshi TeramuraRyoko TamukaiMiho FukuiHiroaki KusanoMikhail SchepetilnikovLyubov A RyabovaHiroaki ShimadaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 16, Iss 7, p e0253488 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Hiromi Mutsuro-Aoki Hiroshi Teramura Ryoko Tamukai Miho Fukui Hiroaki Kusano Mikhail Schepetilnikov Lyubov A Ryabova Hiroaki Shimada Dissection of a rice OsMac1 mRNA 5' UTR to uncover regulatory elements that are responsible for its efficient translation.
description	The untranslated regions (UTRs) of mRNAs are involved in many posttranscriptional regulatory pathways. The rice OsMac1 mRNA has three splicing variants of the 5' UTR (UTRa, UTRb, and UTRc), which include a CU-rich region and three upstream open reading frames (uORFs). UTRc contains an additional 38-nt sequence, termed sp38, which acts as a strong translational enhancer of the downstream ORF; reporter analysis revealed translational efficiencies >15-fold higher with UTRc than with the other splice variants. Mutation analysis of UTRc demonstrated that an optimal sequence length of sp38, rather than its nucleotide sequence is essential for UTRc to promote efficient translation. In addition, the 5' 100 nucleotides of CU-rich region contribute to UTRc translational enhancement. Strikingly, three uORFs did not reveal their inhibitory potential within the full-length leader, whereas deletion of the 5' leader fragment preceding the leader region with uORFs nearly abolished translation. Computational prediction of UTRc structural motifs revealed stem-loop structures, termed SL1-SL4, and two regions, A and B, involved in putative intramolecular interactions. Our data suggest that SL4 binding to Region-A and base pairing between Region-B and the UTRc 3'end are critically required for translational enhancement. Since UTRc is not capable of internal initiation, we presume that the three-dimensional leader structures can allow translation of the leader downstream ORF, likely allowing the bypass of uORFs.
format	article
author	Hiromi Mutsuro-Aoki Hiroshi Teramura Ryoko Tamukai Miho Fukui Hiroaki Kusano Mikhail Schepetilnikov Lyubov A Ryabova Hiroaki Shimada
author_facet	Hiromi Mutsuro-Aoki Hiroshi Teramura Ryoko Tamukai Miho Fukui Hiroaki Kusano Mikhail Schepetilnikov Lyubov A Ryabova Hiroaki Shimada
author_sort	Hiromi Mutsuro-Aoki
title	Dissection of a rice OsMac1 mRNA 5' UTR to uncover regulatory elements that are responsible for its efficient translation.
title_short	Dissection of a rice OsMac1 mRNA 5' UTR to uncover regulatory elements that are responsible for its efficient translation.
title_full	Dissection of a rice OsMac1 mRNA 5' UTR to uncover regulatory elements that are responsible for its efficient translation.
title_fullStr	Dissection of a rice OsMac1 mRNA 5' UTR to uncover regulatory elements that are responsible for its efficient translation.
title_full_unstemmed	Dissection of a rice OsMac1 mRNA 5' UTR to uncover regulatory elements that are responsible for its efficient translation.
title_sort	dissection of a rice osmac1 mrna 5' utr to uncover regulatory elements that are responsible for its efficient translation.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/f89c787da8a448079695596c0ae0a1c6
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Dissection of a rice OsMac1 mRNA 5' UTR to uncover regulatory elements that are responsible for its efficient translation.

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