Proteomic and phosphoproteomic analysis of polyethylene glycol-induced osmotic stress in root tips of common bean (Phaseolus vulgaris L.)


Autoria(s): Yang, Zhong-Bao; Eticha, Dejene; Fuehrs, Hendrik; Heintz, Dimitri; Ayoub, Daniel; Van Dorsselaer, Alain; Schlingmann, Barbara; Rao, Idupulapati Madhusudana; Braun, Hans-Peter; Horst, Walter Johannes
Data(s)

01/12/2013

Resumo

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.

Identificador

http://dx.doi.org/10.15488/453

http://www.repo.uni-hannover.de/handle/123456789/476

Idioma(s)

eng

Publicador

Oxford : Oxford Univ. Press

Relação

http://dx.doi.org/10.1093/jxb/ert328

ISSN:0022-0957

ESSN:1460-2431

Direitos

CC-BY 3.0

https://creativecommons.org/licenses/by/3.0/

frei zugänglich

Fonte

Journal of experimental botany 64 (2013), Nr. 18

Palavras-Chave #apoplast #cell wall #common bean #dehydrin #phosphoproteomics #proteomics #root tips #low water potentials #cell-wall proteome #maize primary root #nadp(+)-dependent isocitrate dehydrogenase #s-adenosylmethionine synthetase #ionically bound proteins #salt-responsive proteins #dehydrin-like proteins #arabidopsis-thaliana #elongation zone #ddc:500
Tipo

status-type:publishedVersion

doc-type:article

doc-type:Text