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RNA Chaperone Function of a Universal Stress Protein in Arabidopsis Confers Enhanced Cold Stress Tolerance in Plants

The physiological function of Arabidopsis thaliana universal stress protein (AtUSP) in plant has remained unclear. Thus, we report here the functional role of the Arabidopsis universal stress protein, AtUSP (At3g53990). To determine how AtUSP affects physiological responses towards cold stress, AtUS...

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Autores principales: Melencion, Sarah Mae Boyles, Chi, Yong Hun, Pham, Thuy Thi, Paeng, Seol Ki, Wi, Seong Dong, Lee, Changyu, Ryu, Seoung Woo, Koo, Sung Sun, Lee, Sang Yeol
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5751149/
https://www.ncbi.nlm.nih.gov/pubmed/29186920
http://dx.doi.org/10.3390/ijms18122546
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author Melencion, Sarah Mae Boyles
Chi, Yong Hun
Pham, Thuy Thi
Paeng, Seol Ki
Wi, Seong Dong
Lee, Changyu
Ryu, Seoung Woo
Koo, Sung Sun
Lee, Sang Yeol
author_facet Melencion, Sarah Mae Boyles
Chi, Yong Hun
Pham, Thuy Thi
Paeng, Seol Ki
Wi, Seong Dong
Lee, Changyu
Ryu, Seoung Woo
Koo, Sung Sun
Lee, Sang Yeol
author_sort Melencion, Sarah Mae Boyles
collection PubMed
description The physiological function of Arabidopsis thaliana universal stress protein (AtUSP) in plant has remained unclear. Thus, we report here the functional role of the Arabidopsis universal stress protein, AtUSP (At3g53990). To determine how AtUSP affects physiological responses towards cold stress, AtUSP overexpression (AtUSP OE) and T-DNA insertion knock-out (atusp, SALK_146059) mutant lines were used. The results indicated that AtUSP OE enhanced plant tolerance to cold stress, whereas atusp did not. AtUSP is localized in the nucleus and cytoplasm, and cold stress significantly affects RNA metabolism such as by misfolding and secondary structure changes of RNA. Therefore, we investigated the relationship of AtUSP with RNA metabolism. We found that AtUSP can bind nucleic acids, including single- and double-stranded DNA and luciferase mRNA. AtUSP also displayed strong nucleic acid-melting activity. We expressed AtUSP in RL211 Escherichia coli, which contains a hairpin-loop RNA structure upstream of chloramphenicol acetyltransferase (CAT), and observed that AtUSP exhibited anti-termination activity that enabled CAT gene expression. AtUSP expression in the cold-sensitive Escherichia coli (E. coli) mutant BX04 complemented the cold sensitivity of the mutant cells. As these properties are typical characteristics of RNA chaperones, we conclude that AtUSP functions as a RNA chaperone under cold-shock conditions. Thus, the enhanced tolerance of AtUSP OE lines to cold stress is mediated by the RNA chaperone function of AtUSP.
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spelling pubmed-57511492018-01-08 RNA Chaperone Function of a Universal Stress Protein in Arabidopsis Confers Enhanced Cold Stress Tolerance in Plants Melencion, Sarah Mae Boyles Chi, Yong Hun Pham, Thuy Thi Paeng, Seol Ki Wi, Seong Dong Lee, Changyu Ryu, Seoung Woo Koo, Sung Sun Lee, Sang Yeol Int J Mol Sci Article The physiological function of Arabidopsis thaliana universal stress protein (AtUSP) in plant has remained unclear. Thus, we report here the functional role of the Arabidopsis universal stress protein, AtUSP (At3g53990). To determine how AtUSP affects physiological responses towards cold stress, AtUSP overexpression (AtUSP OE) and T-DNA insertion knock-out (atusp, SALK_146059) mutant lines were used. The results indicated that AtUSP OE enhanced plant tolerance to cold stress, whereas atusp did not. AtUSP is localized in the nucleus and cytoplasm, and cold stress significantly affects RNA metabolism such as by misfolding and secondary structure changes of RNA. Therefore, we investigated the relationship of AtUSP with RNA metabolism. We found that AtUSP can bind nucleic acids, including single- and double-stranded DNA and luciferase mRNA. AtUSP also displayed strong nucleic acid-melting activity. We expressed AtUSP in RL211 Escherichia coli, which contains a hairpin-loop RNA structure upstream of chloramphenicol acetyltransferase (CAT), and observed that AtUSP exhibited anti-termination activity that enabled CAT gene expression. AtUSP expression in the cold-sensitive Escherichia coli (E. coli) mutant BX04 complemented the cold sensitivity of the mutant cells. As these properties are typical characteristics of RNA chaperones, we conclude that AtUSP functions as a RNA chaperone under cold-shock conditions. Thus, the enhanced tolerance of AtUSP OE lines to cold stress is mediated by the RNA chaperone function of AtUSP. MDPI 2017-11-27 /pmc/articles/PMC5751149/ /pubmed/29186920 http://dx.doi.org/10.3390/ijms18122546 Text en © 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Melencion, Sarah Mae Boyles
Chi, Yong Hun
Pham, Thuy Thi
Paeng, Seol Ki
Wi, Seong Dong
Lee, Changyu
Ryu, Seoung Woo
Koo, Sung Sun
Lee, Sang Yeol
RNA Chaperone Function of a Universal Stress Protein in Arabidopsis Confers Enhanced Cold Stress Tolerance in Plants
title RNA Chaperone Function of a Universal Stress Protein in Arabidopsis Confers Enhanced Cold Stress Tolerance in Plants
title_full RNA Chaperone Function of a Universal Stress Protein in Arabidopsis Confers Enhanced Cold Stress Tolerance in Plants
title_fullStr RNA Chaperone Function of a Universal Stress Protein in Arabidopsis Confers Enhanced Cold Stress Tolerance in Plants
title_full_unstemmed RNA Chaperone Function of a Universal Stress Protein in Arabidopsis Confers Enhanced Cold Stress Tolerance in Plants
title_short RNA Chaperone Function of a Universal Stress Protein in Arabidopsis Confers Enhanced Cold Stress Tolerance in Plants
title_sort rna chaperone function of a universal stress protein in arabidopsis confers enhanced cold stress tolerance in plants
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5751149/
https://www.ncbi.nlm.nih.gov/pubmed/29186920
http://dx.doi.org/10.3390/ijms18122546
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