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Association of Proteomics Changes with Al-Sensitive Root Zones in Switchgrass

In this paper, we report on aluminum (Al)-induced root proteomic changes in switchgrass. After growth in a hydroponic culture system supplemented with 400 μM of Al, plants began to show signs of physiological stress such as a reduction in photosynthetic rate. At this time, the basal 2-cm long root t...

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Autores principales: Rangu, Mahesh, Ye, Zhujia, Bhatti, Sarabjit, Zhou, Suping, Yang, Yong, Fish, Tara, Thannhauser, Theodore W.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6027131/
https://www.ncbi.nlm.nih.gov/pubmed/29565292
http://dx.doi.org/10.3390/proteomes6020015
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author Rangu, Mahesh
Ye, Zhujia
Bhatti, Sarabjit
Zhou, Suping
Yang, Yong
Fish, Tara
Thannhauser, Theodore W.
author_facet Rangu, Mahesh
Ye, Zhujia
Bhatti, Sarabjit
Zhou, Suping
Yang, Yong
Fish, Tara
Thannhauser, Theodore W.
author_sort Rangu, Mahesh
collection PubMed
description In this paper, we report on aluminum (Al)-induced root proteomic changes in switchgrass. After growth in a hydroponic culture system supplemented with 400 μM of Al, plants began to show signs of physiological stress such as a reduction in photosynthetic rate. At this time, the basal 2-cm long root tips were harvested and divided into two segments, each of 1-cm in length, for protein extraction. Al-induced changes in proteomes were identified using tandem mass tags mass spectrometry (TMT-MS)-based quantitative proteomics analysis. A total of 216 proteins (approximately 3.6% of total proteins) showed significant differences between non-Al treated control and treated groups with significant fold change (twice the standard deviation; FDR adjusted p-value < 0.05). The apical root tip tissues expressed more dramatic proteome changes (164 significantly changed proteins; 3.9% of total proteins quantified) compared to the elongation/maturation zones (52 significantly changed proteins, 1.1% of total proteins quantified). Significantly changed proteins from the apical 1-cm root apex tissues were clustered into 25 biological pathways; proteins involved in the cell cycle (rotamase FKBP 1 isoforms, and CDC48 protein) were all at a reduced abundance level compared to the non-treated control group. In the root elongation/maturation zone tissues, the identified proteins were placed into 18 pathways, among which proteins involved in secondary metabolism (lignin biosynthesis) were identified. Several STRING protein interaction networks were developed for these Al-induced significantly changed proteins. This study has identified a large number of Al-responsive proteins, including transcription factors, which will be used for exploring new Al tolerance genes and mechanisms. Data are available via ProteomeXchange with identifiers PXD008882 and PXD009125.
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spelling pubmed-60271312018-07-13 Association of Proteomics Changes with Al-Sensitive Root Zones in Switchgrass Rangu, Mahesh Ye, Zhujia Bhatti, Sarabjit Zhou, Suping Yang, Yong Fish, Tara Thannhauser, Theodore W. Proteomes Article In this paper, we report on aluminum (Al)-induced root proteomic changes in switchgrass. After growth in a hydroponic culture system supplemented with 400 μM of Al, plants began to show signs of physiological stress such as a reduction in photosynthetic rate. At this time, the basal 2-cm long root tips were harvested and divided into two segments, each of 1-cm in length, for protein extraction. Al-induced changes in proteomes were identified using tandem mass tags mass spectrometry (TMT-MS)-based quantitative proteomics analysis. A total of 216 proteins (approximately 3.6% of total proteins) showed significant differences between non-Al treated control and treated groups with significant fold change (twice the standard deviation; FDR adjusted p-value < 0.05). The apical root tip tissues expressed more dramatic proteome changes (164 significantly changed proteins; 3.9% of total proteins quantified) compared to the elongation/maturation zones (52 significantly changed proteins, 1.1% of total proteins quantified). Significantly changed proteins from the apical 1-cm root apex tissues were clustered into 25 biological pathways; proteins involved in the cell cycle (rotamase FKBP 1 isoforms, and CDC48 protein) were all at a reduced abundance level compared to the non-treated control group. In the root elongation/maturation zone tissues, the identified proteins were placed into 18 pathways, among which proteins involved in secondary metabolism (lignin biosynthesis) were identified. Several STRING protein interaction networks were developed for these Al-induced significantly changed proteins. This study has identified a large number of Al-responsive proteins, including transcription factors, which will be used for exploring new Al tolerance genes and mechanisms. Data are available via ProteomeXchange with identifiers PXD008882 and PXD009125. MDPI 2018-03-22 /pmc/articles/PMC6027131/ /pubmed/29565292 http://dx.doi.org/10.3390/proteomes6020015 Text en © 2018 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
Rangu, Mahesh
Ye, Zhujia
Bhatti, Sarabjit
Zhou, Suping
Yang, Yong
Fish, Tara
Thannhauser, Theodore W.
Association of Proteomics Changes with Al-Sensitive Root Zones in Switchgrass
title Association of Proteomics Changes with Al-Sensitive Root Zones in Switchgrass
title_full Association of Proteomics Changes with Al-Sensitive Root Zones in Switchgrass
title_fullStr Association of Proteomics Changes with Al-Sensitive Root Zones in Switchgrass
title_full_unstemmed Association of Proteomics Changes with Al-Sensitive Root Zones in Switchgrass
title_short Association of Proteomics Changes with Al-Sensitive Root Zones in Switchgrass
title_sort association of proteomics changes with al-sensitive root zones in switchgrass
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6027131/
https://www.ncbi.nlm.nih.gov/pubmed/29565292
http://dx.doi.org/10.3390/proteomes6020015
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