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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.


Functional classifications of the differential latex proteins upon ethylene treatment.All differentially expressed latex proteins after ethylene-treated for 3 and/or 5 days that identified by different methods, including D1-D143, P1-P59 and the 404 ERLPs from iTRAQ, are illustrated in a Venn diagram as differential proteins (a), up-regulated (b) and down-regulated (c) proteins. Proteins are clustered into 4 overlapping areas with numbers in different colors. Then, GO classification of all differential proteins (d,g,j), up-regulated (e,h,k), and down-regulated (f,i,l) proteins on cellular component (d–f), biological process (g–i) and molecular function (j–l) are presented. The abbreviations are listed in Supplemental Fig. S2.
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f6: Functional classifications of the differential latex proteins upon ethylene treatment.All differentially expressed latex proteins after ethylene-treated for 3 and/or 5 days that identified by different methods, including D1-D143, P1-P59 and the 404 ERLPs from iTRAQ, are illustrated in a Venn diagram as differential proteins (a), up-regulated (b) and down-regulated (c) proteins. Proteins are clustered into 4 overlapping areas with numbers in different colors. Then, GO classification of all differential proteins (d,g,j), up-regulated (e,h,k), and down-regulated (f,i,l) proteins on cellular component (d–f), biological process (g–i) and molecular function (j–l) are presented. The abbreviations are listed in Supplemental Fig. S2.

Mentions: ERLPs identified by DIGE (143 proteins, D1-D143) and iTRAQ (404 proteins) from E-3 and/or E-5 treatments, as well as the 59 differential phosphoproteins (P1-P59), were plotted in a Venn diagram, which revealed 92 shared protein spots representing 11 unique proteins (Fig. 6a–c; Fig. S5; Tables S2–S4): REF; SRPP; hevein; 14-3-3 protein; HSP70; glucanase; latex abundant protein; ELRP; Hev b7.02; phosphoglycerate kinase; and nucleoredoxin. Moreover, 135 protein species were shared between DIGE and iTRAQ (Fig. 6a). Of the up-regulated proteins, 38 were presented in all experiments and represented 4 unique proteins (REF, SRPP, Gluc and HSP70; Fig. 6b). In DIGE and iTRAQ, we identified 33 shared up-regulated protein species, including ETIF, ubiquitin, V-ATPase, glutathione-S-transferase, proteasome, aminopeptidase, esterase, HSP18 and RNA helicase. In addition, 9 unique proteins were down-regulated in all three experiments. In both DIGE and iTRAQ, 14 unique down-regulated proteins were identified, including chitinase, HMGR or HMGS, ubiquitin, proteasome, enolase, G3PD, and a 50-kDa protein (Fig. 6c; Fig. S5; Tables S3 and S4).


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)

Functional classifications of the differential latex proteins upon ethylene treatment.All differentially expressed latex proteins after ethylene-treated for 3 and/or 5 days that identified by different methods, including D1-D143, P1-P59 and the 404 ERLPs from iTRAQ, are illustrated in a Venn diagram as differential proteins (a), up-regulated (b) and down-regulated (c) proteins. Proteins are clustered into 4 overlapping areas with numbers in different colors. Then, GO classification of all differential proteins (d,g,j), up-regulated (e,h,k), and down-regulated (f,i,l) proteins on cellular component (d–f), biological process (g–i) and molecular function (j–l) are presented. The 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

f6: Functional classifications of the differential latex proteins upon ethylene treatment.All differentially expressed latex proteins after ethylene-treated for 3 and/or 5 days that identified by different methods, including D1-D143, P1-P59 and the 404 ERLPs from iTRAQ, are illustrated in a Venn diagram as differential proteins (a), up-regulated (b) and down-regulated (c) proteins. Proteins are clustered into 4 overlapping areas with numbers in different colors. Then, GO classification of all differential proteins (d,g,j), up-regulated (e,h,k), and down-regulated (f,i,l) proteins on cellular component (d–f), biological process (g–i) and molecular function (j–l) are presented. The abbreviations are listed in Supplemental Fig. S2.
Mentions: ERLPs identified by DIGE (143 proteins, D1-D143) and iTRAQ (404 proteins) from E-3 and/or E-5 treatments, as well as the 59 differential phosphoproteins (P1-P59), were plotted in a Venn diagram, which revealed 92 shared protein spots representing 11 unique proteins (Fig. 6a–c; Fig. S5; Tables S2–S4): REF; SRPP; hevein; 14-3-3 protein; HSP70; glucanase; latex abundant protein; ELRP; Hev b7.02; phosphoglycerate kinase; and nucleoredoxin. Moreover, 135 protein species were shared between DIGE and iTRAQ (Fig. 6a). Of the up-regulated proteins, 38 were presented in all experiments and represented 4 unique proteins (REF, SRPP, Gluc and HSP70; Fig. 6b). In DIGE and iTRAQ, we identified 33 shared up-regulated protein species, including ETIF, ubiquitin, V-ATPase, glutathione-S-transferase, proteasome, aminopeptidase, esterase, HSP18 and RNA helicase. In addition, 9 unique proteins were down-regulated in all three experiments. In both DIGE and iTRAQ, 14 unique down-regulated proteins were identified, including chitinase, HMGR or HMGS, ubiquitin, proteasome, enolase, G3PD, and a 50-kDa protein (Fig. 6c; Fig. S5; Tables S3 and S4).

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.