Cargando…

Changes in the Arabidopsis RNA-binding proteome reveal novel stress response mechanisms

BACKGROUND: RNA-binding proteins (RBPs) are increasingly recognized as regulatory component of post-transcriptional gene expression. RBPs interact with mRNAs via RNA-binding domains and these interactions affect RNA availability for translation, RNA stability and turn-over thus affecting both RNA an...

Descripción completa

Detalles Bibliográficos
Autores principales: Marondedze, Claudius, Thomas, Ludivine, Gehring, Chris, Lilley, Kathryn S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6460520/
https://www.ncbi.nlm.nih.gov/pubmed/30975080
http://dx.doi.org/10.1186/s12870-019-1750-x
_version_ 1783410337794490368
author Marondedze, Claudius
Thomas, Ludivine
Gehring, Chris
Lilley, Kathryn S.
author_facet Marondedze, Claudius
Thomas, Ludivine
Gehring, Chris
Lilley, Kathryn S.
author_sort Marondedze, Claudius
collection PubMed
description BACKGROUND: RNA-binding proteins (RBPs) are increasingly recognized as regulatory component of post-transcriptional gene expression. RBPs interact with mRNAs via RNA-binding domains and these interactions affect RNA availability for translation, RNA stability and turn-over thus affecting both RNA and protein expression essential for developmental and stimulus specific responses. Here we investigate the effect of severe drought stress on the RNA-binding proteome to gain insights into the mechanisms that govern drought stress responses at the systems level. RESULTS: Label-free mass spectrometry enabled the identification 567 proteins of which 150 significantly responded to the drought-induced treatment. A gene ontology analysis revealed enrichment in the “RNA binding” and “RNA processing” categories as well as biological processes such as “response to abscisic acid” and “response to water deprivation”. Importantly, a large number of the stress responsive proteins have not previously been identified as RBPs and include proteins in carbohydrate metabolism and in the glycolytic and citric acid pathways in particular. This suggests that RBPs have hitherto unknown roles in processes that govern metabolic changes during stress responses. Furthermore, a comparative analysis of RBP domain architectures shows both, plant specific and common domain architectures between plants and animals. The latter could be an indication that RBPs are part of an ancient stress response. CONCLUSION: This study establishes mRNA interactome capture technique as an approach to study stress signal responses implicated in environmental changes. Our findings denote RBP changes in the proteome as critical components in plant adaptation to changing environments and in particular drought stress protein-dependent changes in RNA metabolism. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12870-019-1750-x) contains supplementary material, which is available to authorized users.
format Online
Article
Text
id pubmed-6460520
institution National Center for Biotechnology Information
language English
publishDate 2019
publisher BioMed Central
record_format MEDLINE/PubMed
spelling pubmed-64605202019-04-22 Changes in the Arabidopsis RNA-binding proteome reveal novel stress response mechanisms Marondedze, Claudius Thomas, Ludivine Gehring, Chris Lilley, Kathryn S. BMC Plant Biol Research Article BACKGROUND: RNA-binding proteins (RBPs) are increasingly recognized as regulatory component of post-transcriptional gene expression. RBPs interact with mRNAs via RNA-binding domains and these interactions affect RNA availability for translation, RNA stability and turn-over thus affecting both RNA and protein expression essential for developmental and stimulus specific responses. Here we investigate the effect of severe drought stress on the RNA-binding proteome to gain insights into the mechanisms that govern drought stress responses at the systems level. RESULTS: Label-free mass spectrometry enabled the identification 567 proteins of which 150 significantly responded to the drought-induced treatment. A gene ontology analysis revealed enrichment in the “RNA binding” and “RNA processing” categories as well as biological processes such as “response to abscisic acid” and “response to water deprivation”. Importantly, a large number of the stress responsive proteins have not previously been identified as RBPs and include proteins in carbohydrate metabolism and in the glycolytic and citric acid pathways in particular. This suggests that RBPs have hitherto unknown roles in processes that govern metabolic changes during stress responses. Furthermore, a comparative analysis of RBP domain architectures shows both, plant specific and common domain architectures between plants and animals. The latter could be an indication that RBPs are part of an ancient stress response. CONCLUSION: This study establishes mRNA interactome capture technique as an approach to study stress signal responses implicated in environmental changes. Our findings denote RBP changes in the proteome as critical components in plant adaptation to changing environments and in particular drought stress protein-dependent changes in RNA metabolism. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12870-019-1750-x) contains supplementary material, which is available to authorized users. BioMed Central 2019-04-11 /pmc/articles/PMC6460520/ /pubmed/30975080 http://dx.doi.org/10.1186/s12870-019-1750-x Text en © The Author(s). 2019 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Research Article
Marondedze, Claudius
Thomas, Ludivine
Gehring, Chris
Lilley, Kathryn S.
Changes in the Arabidopsis RNA-binding proteome reveal novel stress response mechanisms
title Changes in the Arabidopsis RNA-binding proteome reveal novel stress response mechanisms
title_full Changes in the Arabidopsis RNA-binding proteome reveal novel stress response mechanisms
title_fullStr Changes in the Arabidopsis RNA-binding proteome reveal novel stress response mechanisms
title_full_unstemmed Changes in the Arabidopsis RNA-binding proteome reveal novel stress response mechanisms
title_short Changes in the Arabidopsis RNA-binding proteome reveal novel stress response mechanisms
title_sort changes in the arabidopsis rna-binding proteome reveal novel stress response mechanisms
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6460520/
https://www.ncbi.nlm.nih.gov/pubmed/30975080
http://dx.doi.org/10.1186/s12870-019-1750-x
work_keys_str_mv AT marondedzeclaudius changesinthearabidopsisrnabindingproteomerevealnovelstressresponsemechanisms
AT thomasludivine changesinthearabidopsisrnabindingproteomerevealnovelstressresponsemechanisms
AT gehringchris changesinthearabidopsisrnabindingproteomerevealnovelstressresponsemechanisms
AT lilleykathryns changesinthearabidopsisrnabindingproteomerevealnovelstressresponsemechanisms