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Comprehensive Proteomics Analysis of Laticifer Latex Reveals New Insights into Ethylene Stimulation of Natural Rubber Production.

Wang X, Wang D, Sun Y, Yang Q, Chang L, Wang L, Meng X, Huang Q, Jin X, Tong Z - Sci Rep (2015)

Bottom Line: Moreover, we found that ethylene improves the generation of small rubber particles.Functional classification of ERLPs revealed that enzymes involved in post-translational modification, carbohydrate metabolism, hydrolase activity, and kinase activity were overrepresented.Phosphoproteomics analysis identified 59 differential phosphoproteins; notably, specific isoforms of rubber elongation factor and small rubber particle protein that were phosphorylated mainly at serine residues.

View Article: PubMed Central - PubMed

Affiliation: Key Laboratory of Biology and Genetic Resources for Tropical Crops, Institute of Tropical Biosciences and Biotechnology, Chinese Academy of Tropical Agricultural Sciences, Haikou Hainan 571101, China.

ABSTRACT
Ethylene is a stimulant to increase natural rubber latex. After ethylene application, both fresh yield and dry matter of latex are substantially improved. Moreover, we found that ethylene improves the generation of small rubber particles. However, most genes involved in rubber biosynthesis are inhibited by exogenous ethylene. Therefore, we conducted a proteomics analysis of ethylene-stimulated rubber latex, and identified 287 abundant proteins as well as 143 ethylene responsive latex proteins (ERLPs) with mass spectrometry from the 2-DE and DIGE gels, respectively. In addition, more than 1,600 proteins, including 404 ERLPs, were identified by iTRAQ. Functional classification of ERLPs revealed that enzymes involved in post-translational modification, carbohydrate metabolism, hydrolase activity, and kinase activity were overrepresented. Some enzymes for rubber particle aggregation were inhibited to prolong latex flow, and thus finally improved latex production. Phosphoproteomics analysis identified 59 differential phosphoproteins; notably, specific isoforms of rubber elongation factor and small rubber particle protein that were phosphorylated mainly at serine residues. This post-translational modification and isoform-specific phosphorylation might be important for ethylene-stimulated latex production. These results not only deepen our understanding of the rubber latex proteome but also provide new insights into the use of ethylene to stimulate rubber latex production.

No MeSH data available.


Schematic of enzyme localization and regulation of ethylene-induced pathways at the proteomic level in rubber latex cells.The ethylene-responsive proteins in rubber latex were localized in the C-serum, nucleus, lutoid and rubber particle based on GO analysis and their reported functions. The main biochemical processes and ethylene-responsive pathways are highlighted in different colors. Proteins activated (up) or inhibited (down) by ethylene are marked with arrows in different colors (pink, from DIGE; blue, from iTRAQ and/or Western blotting). Abbreviations are listed in Supplemental Fig. S2.
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f8: Schematic of enzyme localization and regulation of ethylene-induced pathways at the proteomic level in rubber latex cells.The ethylene-responsive proteins in rubber latex were localized in the C-serum, nucleus, lutoid and rubber particle based on GO analysis and their reported functions. The main biochemical processes and ethylene-responsive pathways are highlighted in different colors. Proteins activated (up) or inhibited (down) by ethylene are marked with arrows in different colors (pink, from DIGE; blue, from iTRAQ and/or Western blotting). Abbreviations are listed in Supplemental Fig. S2.

Mentions: Given our in-depth proteomics analysis of rubber latex following ethylene treatment and the recent findings reported in the literatures, we have summarized the putative subcellular localization and main function of the identified proteins and have proposed a schematic for their regulation (Fig. 8). These results revealed that ethylene stimulation of rubber latex production might act neither at the level of gene expression nor on general protein accumulation. Our data point to the post-translational modification of several key enzymes and the involvement of carbohydrate metabolic process-related proteins as playing crucial roles in controlling natural rubber biosynthesis and latex production.


Comprehensive Proteomics Analysis of Laticifer Latex Reveals New Insights into Ethylene Stimulation of Natural Rubber Production.

Wang X, Wang D, Sun Y, Yang Q, Chang L, Wang L, Meng X, Huang Q, Jin X, Tong Z - Sci Rep (2015)

Schematic of enzyme localization and regulation of ethylene-induced pathways at the proteomic level in rubber latex cells.The ethylene-responsive proteins in rubber latex were localized in the C-serum, nucleus, lutoid and rubber particle based on GO analysis and their reported functions. The main biochemical processes and ethylene-responsive pathways are highlighted in different colors. Proteins activated (up) or inhibited (down) by ethylene are marked with arrows in different colors (pink, from DIGE; blue, from iTRAQ and/or Western blotting). Abbreviations are listed in Supplemental Fig. S2.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4562231&req=5

f8: Schematic of enzyme localization and regulation of ethylene-induced pathways at the proteomic level in rubber latex cells.The ethylene-responsive proteins in rubber latex were localized in the C-serum, nucleus, lutoid and rubber particle based on GO analysis and their reported functions. The main biochemical processes and ethylene-responsive pathways are highlighted in different colors. Proteins activated (up) or inhibited (down) by ethylene are marked with arrows in different colors (pink, from DIGE; blue, from iTRAQ and/or Western blotting). Abbreviations are listed in Supplemental Fig. S2.
Mentions: Given our in-depth proteomics analysis of rubber latex following ethylene treatment and the recent findings reported in the literatures, we have summarized the putative subcellular localization and main function of the identified proteins and have proposed a schematic for their regulation (Fig. 8). These results revealed that ethylene stimulation of rubber latex production might act neither at the level of gene expression nor on general protein accumulation. Our data point to the post-translational modification of several key enzymes and the involvement of carbohydrate metabolic process-related proteins as playing crucial roles in controlling natural rubber biosynthesis and latex production.

Bottom Line: Moreover, we found that ethylene improves the generation of small rubber particles.Functional classification of ERLPs revealed that enzymes involved in post-translational modification, carbohydrate metabolism, hydrolase activity, and kinase activity were overrepresented.Phosphoproteomics analysis identified 59 differential phosphoproteins; notably, specific isoforms of rubber elongation factor and small rubber particle protein that were phosphorylated mainly at serine residues.

View Article: PubMed Central - PubMed

Affiliation: Key Laboratory of Biology and Genetic Resources for Tropical Crops, Institute of Tropical Biosciences and Biotechnology, Chinese Academy of Tropical Agricultural Sciences, Haikou Hainan 571101, China.

ABSTRACT
Ethylene is a stimulant to increase natural rubber latex. After ethylene application, both fresh yield and dry matter of latex are substantially improved. Moreover, we found that ethylene improves the generation of small rubber particles. However, most genes involved in rubber biosynthesis are inhibited by exogenous ethylene. Therefore, we conducted a proteomics analysis of ethylene-stimulated rubber latex, and identified 287 abundant proteins as well as 143 ethylene responsive latex proteins (ERLPs) with mass spectrometry from the 2-DE and DIGE gels, respectively. In addition, more than 1,600 proteins, including 404 ERLPs, were identified by iTRAQ. Functional classification of ERLPs revealed that enzymes involved in post-translational modification, carbohydrate metabolism, hydrolase activity, and kinase activity were overrepresented. Some enzymes for rubber particle aggregation were inhibited to prolong latex flow, and thus finally improved latex production. Phosphoproteomics analysis identified 59 differential phosphoproteins; notably, specific isoforms of rubber elongation factor and small rubber particle protein that were phosphorylated mainly at serine residues. This post-translational modification and isoform-specific phosphorylation might be important for ethylene-stimulated latex production. These results not only deepen our understanding of the rubber latex proteome but also provide new insights into the use of ethylene to stimulate rubber latex production.

No MeSH data available.