Welcome to Chinese Journal of Tropical Crops,

Chinese Journal of Tropical Crops ›› 2022, Vol. 43 ›› Issue (5): 904-914.DOI: 10.3969/j.issn.1000-2561.2022.05.004

• Omics & Biotechnology • Previous Articles     Next Articles

Comparative Proteomics Analysis and Identification of Phosphorylated Protein in Latex of Rubber Tree Clones PR107 and CATAS8-79

WANG Dan1, XU Bingqiang2,*(), SUN Yong3, PENG Cunzhi1, CHANG Lili1, TONG Zheng1,*()   

  1. 1. Institute of Tropical Bioscience and Biotechnology, Chinese Academy of Tropical Agricultural Sciences, Haikou, Hainan 571101, China
    2. Haikou Experimental Station (Institute of Tropical Fruit Tree Research), Chinese Academy of Tropical Agricultural Sciences, Haikou, Hainan 571101, China
    3. Rubber Research Institute, Chinese Academy of Tropical Agricultural Sciences, Danzhou, Hainan 571737, China
  • Received:2021-07-27 Revised:2022-01-11 Online:2022-05-25 Published:2022-05-30
  • Contact: XU Bingqiang,TONG Zheng


Hevea brasiliensis is an important plant for producing natural rubber. RP107 and CATAS8-79 are two clones of H. brasiliensis with different properties of rubber production and expulsion. The study of protein function in the latex may help understand the regulatory mechanism related to the properties of rubber production and expulsion. This study aimed to compare and analyze the difference in latex protein between RP107 and CATAS8-79 at the level of protein accumulation and post-translational modification. Through the two-dimensional gel electrophoresis (2-DE) analysis, 65 proteins derived from 88 spots were found to be accumulated differently in the latex between the 2 clones. Among the proteins, 44 proteins had high accumulation in the latex of PR107 and 21 had high accumulation in the latex of CATAS8-79. The high-accumulation proteins (HAPs) in the latex of CATAS8-79 were involved in intracellular organelles, external encapsulating structure, and membrane-bound organelles in terms of cellular component, and most of them had drug-binding activity and hydrolase activity. Different from CATAS8-79, the HAPs in the latex of PR107 participated in a catalytic complex, nonmembrane-bound organelles, and apoplasts. Most of them had protein-binding and transferase activities. Furthermore, some proteins related to natural rubber synthesis and latex agglutination were found in DAPs. The rubber elongation factors (REFs) and small rubber particle proteins (SRPPs) were identified. The two classes of proteins played an important role in natural rubber biosynthesis in rubber trees. Some proteins mediating rubber particle aggregation (RPA) and participating in response to tapping were found in DAPs too. To determinate the phosphorylated proteins and amino acids in the latex of the two clones, the phosphopeptides were enriched using a Fe-NTA Phosphopeptide Enrichment Kit and shotgun analysis was performed through the high-throughput Tandem Mass Spectrometer (MS/MS). 74 phosphorylated amino acid residues derived from 31 phosphorylated proteins, as well as 166 phosphorylated amino acid residues derived from 80 phosphorylated proteins, were identified in PR107 and CATAS8-79, respectively. Among the phosphorylated proteins, 25 proteins of PR107 and 74 proteins of CATAS8-79 were specific in terms of the phosphorylation amino acids. Between the two clones, the members of REF/SRPP protein family, which regulate the synthesis of nature rubber (NR) in the latex, have high differentiation capacity at both protein accumulation and phosphorylation modification levels. The pro-hevein and hevamine proteins, which influence the process of rubber expulsion, also showed diversity at the phosphorylation modification level. The phosphorylation and dephosphorylation of an serine/threonine protein phosphatase kinase might play a regulatory role in NR synthesis. The results could provide a new theoretical basis for the study of the regulatory mechanism of NR biosynthesis.

Key words: Hevea brasiliensis, natural rubber biosynthesis, phosphoproteome, two-dimensional gel electrophoresis (2-DE)

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