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Shi M.-J.,Chinese Academy of Sciences | Shi M.-J.,Key Laboratory of Biology and Genetic Resources of Rubber Tree | Cai F.-G.,Key Laboratory of Biology and Genetic Resources of Rubber Tree | Tian W.-M.,Chinese Academy of Sciences | Tian W.-M.,Key Laboratory of Biology and Genetic Resources of Rubber Tree
Journal of Biochemistry | Year: 2015

Ethrel is the most effective stimuli in prolonging the latex flow that consequently increases yield per tapping. This effect is largely ascribed to the enhanced lutoid stability, which is associated with the decreased release of initiators of rubber particle (RP) aggregation from lutoid bursting. However, the increase in both the bursting index of lutoids and the duration of latex flow after applying ethrel or ethylene gas in high concentrations suggests that a new mechanism needs to be introduced. In this study, a latex allergen Hev b 7-like protein in C-serum was identified by matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI TOF MS). In vitro analysis showed that the protein acted as a universal antagonist of RP aggregating factors from lutoids and C-serum. Ethrel treatment obviously weakened the effect of C-serum on RP aggregation, which was closely associated with the increase in the level of the Hev b 7-like protein and the decrease in the level of the 37 kDa protein, as revealed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), western blotting analysis and antibody neutralization. Thus, the increase of the Hev b 7-like protein level or the ratio of the Hev b 7-like protein to the 37 kDa protein in C-serum should be primarily ascribed to the ethrel-stimulated prolongation of latex flow duration. © 2015 The Authors. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved. Source


Dai L.,Key Laboratory of Biology and Genetic Resources of Rubber Tree | Dai L.,Rubber Research Institute of China | Kang G.,Key Laboratory of Biology and Genetic Resources of Rubber Tree | Kang G.,Rubber Research Institute of China | And 6 more authors.
Journal of Proteomics | Year: 2016

Ethrel (ET) is an effective and widely used latex yield stimulant of Hevea brasiliensis (Pará rubber tree), and jasmonate (JA) is a key inducer of laticifer differentiation in this plant. To examine variations in the latex proteome caused by these phytohormones, ET and methyl jasmonate (MeJA) were applied to Reyan 7-33-97 rubber tree clones, and comparative proteomic analyses were conducted. On the basis of a transcriptome shotgun assembly (TSA) sequence database and an iTRAQ-coupled two-dimensional LC-MS/MS approach, 1499 latex proteins belonging to 1078 clusters were identified. With a 1.5-fold cut-off value to determine up- and down-regulated proteins, a total of 101 latex proteins were determined to be regulated by ET and/or MeJA via pairwise comparisons among the three exposure durations (0. h, 6 h, and 48 h). Proteins associated with latex regeneration, including phosphoenolpyruvate carboxylase and acetyl-CoA C-acetyltransferase, and those associated with latex flow, such as chitinase and a sieve element occlusion protein, were affected by the application of ET. Chitinase and polyphenol oxidase were also found to be regulated by MeJA. The findings of this study may provide new insight into the roles of phytohormones in latex yield and the causative mechanisms of laticifer differentiation in rubber trees. Significance: On the basis of a transcriptome shotgun assembly (TSA) sequence database and an iTRAQ-coupled two-dimensional LC-MS/MS approach, the most comprehensive proteome of the latex was profiled, and the ethylene-/jasmonate-responsive proteins were identified in the latex of H. brasiliensis. The findings of this study may provide new insight into the role of phytohormones in latex yield and the causative mechanisms of laticifer differentiation in rubber trees. © 2015 Elsevier B.V. Source


Dai L.,Key Laboratory of Biology and Genetic Resources of Rubber Tree | Dai L.,Rubber Research Institute of China | Kang G.,Key Laboratory of Biology and Genetic Resources of Rubber Tree | Kang G.,Rubber Research Institute of China | And 8 more authors.
Plant Molecular Biology | Year: 2013

The rubber particle is a special organelle in which natural rubber is synthesised and stored in the laticifers of Hevea brasiliensis. To better understand the biological functions of rubber particles and to identify the candidate rubber biosynthesis-related proteins, a comprehensive proteome analysis was performed on H. brasiliensis rubber particles using shotgun tandem mass spectrometry profiling approaches-resulting in a thorough report on the rubber particle proteins. A total of 186 rubber particle proteins were identified, with a range in relative molecular mass of 3.9-194.2 kDa and in isoelectric point values of 4.0-11.2. The rubber particle proteins were analysed for gene ontology and could be categorised into eight major groups according to their functions: including rubber biosynthesis, stress- or defence-related responses, protein processing and folding, signal transduction and cellular transport. In addition to well-known rubber biosynthesis-related proteins such as rubber elongation factor (REF), small rubber particle protein (SRPP) and cis-prenyl transferase (CPT), many proteins were firstly identified to be on the rubber particles, including cyclophilin, phospholipase D, cytochrome P450, small GTP-binding protein, clathrin, eukaryotic translation initiation factor, annexin, ABC transporter, translationally controlled tumour protein, ubiquitin-conjugating enzymes, and several homologues of REF, SRPP and CPT. A procedure of multiple reaction monitoring was established for further protein validation. This comprehensive proteome data of rubber particles would facilitate investigation into molecular mechanisms of biogenesis, self-homeostasis and rubber biosynthesis of the rubber particle, and might serve as valuable biomarkers in molecular breeding studies of H. brasiliensis and other alternative rubber-producing species. © 2013 Springer Science+Business Media Dordrecht. Source


Xiang Q.,Key Laboratory of Biology and Genetic Resources of Rubber Tree | Xiang Q.,State Key Laboratory Incubation Base | Xia K.,Key Laboratory of Biology and Genetic Resources of Rubber Tree | Xia K.,State Key Laboratory Incubation Base | And 12 more authors.
Plant Physiology and Biochemistry | Year: 2012

The rubber particle is a specialized organelle in which natural rubber is synthesised and stored in the laticifers of Hevea brasiliensis (para rubber tree). It has been demonstrated that the small rubber particles (SRPs) has higher rubber biosynthesis ratio than the large rubber particles (LRPs), but the underlying molecular mechanism still remains unknown. In this study, LRPs and SRPs were firstly separated from the fresh latex using differential centrifugation, and two-dimensional difference in-gel electrophoresis (2D-DIGE) combined with MALDI-TOF/TOF was then applied to investigate the proteomic alterations associated with the changed rubber biosynthesis capacity between LRPs and SRPs. A total of 53 spots corresponding to 22 gene products, were significantly altered with the |ratio|. ≥. 2.0 and T value ≤0.05, among which 15 proteins were up-regulated and 7 were down-regulated in the SRPs compared with the LRPs. The 15 up-regulated proteins in the SRPs included small rubber particle protein (SRPP), 3-hydroxy-3-methylglutaryl-CoA synthase (HMGCS), phospholipase D alpha (PLD α), ethylene response factor 2, eukaryotic translation initiation factor 5A isoform IV (eIF 5A-4), 70-kDa heat shock cognate protein (HSC 70), several unknown proteins, etc., whereas the 7 up-regulated proteins in the LRPs were rubber elongation factor (REF, 19.6. kDa), ASR-like protein 1, REF-like stress-related protein 1, a putative phosphoglyceride transfer family protein, β-1,3-glucanase, a putative retroelement, and a hypothetical protein. Since several proteins related to rubber biosynthesis were differentially expressed between LRPs and SRPs, the comparative proteome data may provide useful insights into understanding the mechanism involved in rubber biosynthesis and latex coagulation in H. brasiliensis. © 2012 Elsevier Masson SAS. Source

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