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Comparative proteomics analysis of the root apoplasts of rice seedlings in response to hydrogen peroxide.

Zhou L, Bokhari SA, Dong CJ, Liu JY - PLoS ONE (2011)

Bottom Line: Of these, 54 were successfully identified by PMF or MS/MS as matches to 35 different proteins including known and novel H(2)O(2)-responsive proteins.Almost all of these identities (98%) were indeed apoplast proteins confirmed either by previous experiments or through publicly available prediction programs.Based on the abundant changes in these proteins, together with their putative functions, we proposed a possible protein network that provides new insights into oxidative stress response in the rice root apoplast and clues for the further functional research of target proteins associated with H(2)O(2) response.

View Article: PubMed Central - PubMed

Affiliation: Laboratory of Molecular Biology, School of Life Sciences, Tsinghua University, Beijing, People's Republic of China.

ABSTRACT

Background: Plant apoplast is the prime site for signal perception and defense response, and of great importance in responding to environmental stresses. Hydrogen peroxide (H(2)O(2)) plays a pivotal role in determining the responsiveness of cells to stress. However, how the apoplast proteome changes under oxidative condition is largely unknown. In this study, we initiated a comparative proteomic analysis to explore H(2)O(2)-responsive proteins in the apoplast of rice seedling roots.

Methodology/principal findings: 14-day-old rice seedlings were treated with low concentrations (300 and 600 µM) of H(2)O(2) for 6 h and the levels of relative electrolyte leakage, malondialdehyde and H(2)O(2) were assayed in roots. The modified vacuum infiltration method was used to extract apoplast proteins of rice seedling roots, and then two-dimensional electrophoresis gel analysis revealed 58 differentially expressed protein spots under low H(2)O(2) conditions. Of these, 54 were successfully identified by PMF or MS/MS as matches to 35 different proteins including known and novel H(2)O(2)-responsive proteins. Almost all of these identities (98%) were indeed apoplast proteins confirmed either by previous experiments or through publicly available prediction programs. These proteins identified are involved in a variety of processes, including redox homeostasis, cell wall modification, signal transduction, cell defense and carbohydrate metabolism, indicating a complex regulative network in the apoplast of seedling roots under H(2)O(2) stress.

Conclusions/significance: The present study is the first apoplast proteome investigation of plant seedlings in response to H(2)O(2) and may be of paramount importance for the understanding of the plant network to environmental stresses. Based on the abundant changes in these proteins, together with their putative functions, we proposed a possible protein network that provides new insights into oxidative stress response in the rice root apoplast and clues for the further functional research of target proteins associated with H(2)O(2) response.

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Functional classification and distribution of the 54 identified protein spots.The number represents the number of protein spots identified in each functional catalog.
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pone-0016723-g005: Functional classification and distribution of the 54 identified protein spots.The number represents the number of protein spots identified in each functional catalog.

Mentions: To characterize the apoplast proteome response to H2O2, all 54 identified protein sequences were functionally classified by GoFigure (http//www.geneontology.org). All H2O2 responsive proteins were grouped into 8 major categories as shown in Figure 5 and Table S1. An impressive 45% of these identities belonged to functional categories including redox homeostasis, cell rescue/defense and signal transduction, suggesting the functional importance of these processes in the apoplastic response to H2O2 treatments.


Comparative proteomics analysis of the root apoplasts of rice seedlings in response to hydrogen peroxide.

Zhou L, Bokhari SA, Dong CJ, Liu JY - PLoS ONE (2011)

Functional classification and distribution of the 54 identified protein spots.The number represents the number of protein spots identified in each functional catalog.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3037377&req=5

pone-0016723-g005: Functional classification and distribution of the 54 identified protein spots.The number represents the number of protein spots identified in each functional catalog.
Mentions: To characterize the apoplast proteome response to H2O2, all 54 identified protein sequences were functionally classified by GoFigure (http//www.geneontology.org). All H2O2 responsive proteins were grouped into 8 major categories as shown in Figure 5 and Table S1. An impressive 45% of these identities belonged to functional categories including redox homeostasis, cell rescue/defense and signal transduction, suggesting the functional importance of these processes in the apoplastic response to H2O2 treatments.

Bottom Line: Of these, 54 were successfully identified by PMF or MS/MS as matches to 35 different proteins including known and novel H(2)O(2)-responsive proteins.Almost all of these identities (98%) were indeed apoplast proteins confirmed either by previous experiments or through publicly available prediction programs.Based on the abundant changes in these proteins, together with their putative functions, we proposed a possible protein network that provides new insights into oxidative stress response in the rice root apoplast and clues for the further functional research of target proteins associated with H(2)O(2) response.

View Article: PubMed Central - PubMed

Affiliation: Laboratory of Molecular Biology, School of Life Sciences, Tsinghua University, Beijing, People's Republic of China.

ABSTRACT

Background: Plant apoplast is the prime site for signal perception and defense response, and of great importance in responding to environmental stresses. Hydrogen peroxide (H(2)O(2)) plays a pivotal role in determining the responsiveness of cells to stress. However, how the apoplast proteome changes under oxidative condition is largely unknown. In this study, we initiated a comparative proteomic analysis to explore H(2)O(2)-responsive proteins in the apoplast of rice seedling roots.

Methodology/principal findings: 14-day-old rice seedlings were treated with low concentrations (300 and 600 µM) of H(2)O(2) for 6 h and the levels of relative electrolyte leakage, malondialdehyde and H(2)O(2) were assayed in roots. The modified vacuum infiltration method was used to extract apoplast proteins of rice seedling roots, and then two-dimensional electrophoresis gel analysis revealed 58 differentially expressed protein spots under low H(2)O(2) conditions. Of these, 54 were successfully identified by PMF or MS/MS as matches to 35 different proteins including known and novel H(2)O(2)-responsive proteins. Almost all of these identities (98%) were indeed apoplast proteins confirmed either by previous experiments or through publicly available prediction programs. These proteins identified are involved in a variety of processes, including redox homeostasis, cell wall modification, signal transduction, cell defense and carbohydrate metabolism, indicating a complex regulative network in the apoplast of seedling roots under H(2)O(2) stress.

Conclusions/significance: The present study is the first apoplast proteome investigation of plant seedlings in response to H(2)O(2) and may be of paramount importance for the understanding of the plant network to environmental stresses. Based on the abundant changes in these proteins, together with their putative functions, we proposed a possible protein network that provides new insights into oxidative stress response in the rice root apoplast and clues for the further functional research of target proteins associated with H(2)O(2) response.

Show MeSH
Related in: MedlinePlus