Details
| Original language | English |
|---|---|
| Pages (from-to) | 5569-5586 |
| Number of pages | 18 |
| Journal | Journal of experimental botany |
| Volume | 64 |
| Issue number | 18 |
| Publication status | Published - 11 Oct 2013 |
Abstract
Previous studies have shown that polyethylene glycol (PEG)-induced osmotic stress (OS) reduces cell-wall (CW) porosity and limits aluminium (Al) uptake by root tips of common bean (Phaseolus vulgaris L.). A subsequent transcriptomic study suggested that genes related to CW processes are involved in adjustment to OS. In this study, a proteomic and phosphoproteomic approach was applied to identify OS-induced protein regulation to further improve our understanding of how OS affects Al accumulation. Analysis of total soluble proteins in root tips indicated that, in total, 22 proteins were differentially regulated by OS; these proteins were functionally categorized. Seventy-seven per- cent of the total expressed proteins were involved in metabolic pathways, particularly of carbohydrate and amino acid metabolism. An analysis of the apoplastic proteome revealed that OS reduced the level of five proteins and increased that of seven proteins. Investigation of the total soluble phosphoproteome suggested that dehydrin responded to OS with an enhanced phosphorylation state without a change in abundance. A cellular immunolocalization analysis indicated that dehydrin was localized mainly in the CW. This suggests that dehydrin may play a major protective role in the OS-induced physical breakdown of the CW structure and thus maintenance of the reversibility of CW extensibility during recovery from OS. The proteomic and phosphoproteomic analyses provided novel insights into the complex mechanisms of OS-induced reduction of Al accumulation in the root tips of common bean and highlight a key role for modification of CW structure.
Keywords
- Apoplast, cell wall, common bean, dehydrin, phosphoproteomics, proteomics, root tips
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Physiology
- Agricultural and Biological Sciences(all)
- Plant Science
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In: Journal of experimental botany, Vol. 64, No. 18, 11.10.2013, p. 5569-5586.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Proteomic and phosphoproteomic analysis of polyethylene glycol-induced osmotic stress in root tips of common bean (Phaseolus vulgaris L.)
AU - Yang, Zhong Bao
AU - Eticha, Dejene
AU - Führs, Hendrik
AU - Heintz, Dimitri
AU - Ayoub, Daniel
AU - Van Dorsselaer, Alain
AU - Schlingmann, Barbara
AU - Rao, Idupulapati Madhusudana
AU - Braun, Hans Peter
AU - Horst, Walter Johannes
N1 - Funding information: This research was supported by a restricted core project from the Bundesministerium für Wirtschaftliche Zusammenarbeit/ Gesellschaft für Technische Zusammenarbeit (BMZ/GTZ) (no. 05.7860.9-001.00) granted to the International Center for Tropical Agriculture (CIAT). We thank Dr Steve Beebe, Leader of the Bean Program of CIAT, for the supply of seeds of the common bean genotype.
PY - 2013/10/11
Y1 - 2013/10/11
N2 - Previous studies have shown that polyethylene glycol (PEG)-induced osmotic stress (OS) reduces cell-wall (CW) porosity and limits aluminium (Al) uptake by root tips of common bean (Phaseolus vulgaris L.). A subsequent transcriptomic study suggested that genes related to CW processes are involved in adjustment to OS. In this study, a proteomic and phosphoproteomic approach was applied to identify OS-induced protein regulation to further improve our understanding of how OS affects Al accumulation. Analysis of total soluble proteins in root tips indicated that, in total, 22 proteins were differentially regulated by OS; these proteins were functionally categorized. Seventy-seven per- cent of the total expressed proteins were involved in metabolic pathways, particularly of carbohydrate and amino acid metabolism. An analysis of the apoplastic proteome revealed that OS reduced the level of five proteins and increased that of seven proteins. Investigation of the total soluble phosphoproteome suggested that dehydrin responded to OS with an enhanced phosphorylation state without a change in abundance. A cellular immunolocalization analysis indicated that dehydrin was localized mainly in the CW. This suggests that dehydrin may play a major protective role in the OS-induced physical breakdown of the CW structure and thus maintenance of the reversibility of CW extensibility during recovery from OS. The proteomic and phosphoproteomic analyses provided novel insights into the complex mechanisms of OS-induced reduction of Al accumulation in the root tips of common bean and highlight a key role for modification of CW structure.
AB - Previous studies have shown that polyethylene glycol (PEG)-induced osmotic stress (OS) reduces cell-wall (CW) porosity and limits aluminium (Al) uptake by root tips of common bean (Phaseolus vulgaris L.). A subsequent transcriptomic study suggested that genes related to CW processes are involved in adjustment to OS. In this study, a proteomic and phosphoproteomic approach was applied to identify OS-induced protein regulation to further improve our understanding of how OS affects Al accumulation. Analysis of total soluble proteins in root tips indicated that, in total, 22 proteins were differentially regulated by OS; these proteins were functionally categorized. Seventy-seven per- cent of the total expressed proteins were involved in metabolic pathways, particularly of carbohydrate and amino acid metabolism. An analysis of the apoplastic proteome revealed that OS reduced the level of five proteins and increased that of seven proteins. Investigation of the total soluble phosphoproteome suggested that dehydrin responded to OS with an enhanced phosphorylation state without a change in abundance. A cellular immunolocalization analysis indicated that dehydrin was localized mainly in the CW. This suggests that dehydrin may play a major protective role in the OS-induced physical breakdown of the CW structure and thus maintenance of the reversibility of CW extensibility during recovery from OS. The proteomic and phosphoproteomic analyses provided novel insights into the complex mechanisms of OS-induced reduction of Al accumulation in the root tips of common bean and highlight a key role for modification of CW structure.
KW - Apoplast
KW - cell wall
KW - common bean
KW - dehydrin
KW - phosphoproteomics
KW - proteomics
KW - root tips
UR - http://www.scopus.com/inward/record.url?scp=84891525422&partnerID=8YFLogxK
U2 - 10.1093/jxb/ert328
DO - 10.1093/jxb/ert328
M3 - Article
C2 - 24123251
AN - SCOPUS:84891525422
VL - 64
SP - 5569
EP - 5586
JO - Journal of experimental botany
JF - Journal of experimental botany
SN - 0022-0957
IS - 18
ER -