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<p>The Para rubber tree (<i>Hevea brasiliensis</i>) is one of the most economically important latex-producing plants in the industrial sectors worldwide. The RRIT 251 clone is well recognized for its high latex yield and tolerance to diverse environmental conditions. Although considerable efforts have been made to enhance the latex production of RRIT 251, a comprehensive analysis of the functional and structural properties of its proteins remains limited. In this study, an in-depth proteomic analysis was conducted on C-serum (CS) and rubber particles (RPs) to gain insights into the molecular mechanisms and biological processes involved in latex production in the RRIT 251 clone. A total of 3028 proteins were identified in CS and 1854 proteins in RPs. Based on the evolutionary genealogy of genes: Non-supervised Orthologous Groups (eggNOG), many of proteins were preliminary classified into three groups: posttranslational modification, protein turnover and chaperones. A comprehensive analysis of protein domain family (Pfam) revealed that the protein kinase and small GTP-binding domains were most frequently detected in CS and RP fractions. In addition, KEGG and Plant Reactome pathway enrichment analyses of CS and RP fractions showed significant association with the Metabolism category. Collectively, these results suggest that proteins from the CS and RP fractions of latex play essential roles in cellular and metabolic processes. These findings not only deepen our understanding of the RRIT 251 latex proteome but also provide further insights into the biological processes underlying latex production and plant defense.</p>

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Proteomics Analysis of C-Serum and Rubber Particles from Hevea brasiliensis (Clone RRIT 251)

  • 期刊论文

  • 发表日期：

    2025年6月28日

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  • Charinrat Saechan,
  • Natakorn Nokchan,
  • Suttida Saewong,
  • Supinya Thanapongpichat,
  • Kanitta Srinoun,
  • Natta Tansila,
  • Worrawit Wanichsuwan,
  • Phanthipha Runsaeng,
  • Juthamard Chantaraamporn,
  • Daranee Chokchaichamnankit,
  • Chantragan Srisomsap,
  • Jisnuson Svasti,
  • Churat Weeraphan,
  • Hansuk Buncherd

摘要

The Para rubber tree (Hevea brasiliensis) is one of the most economically important latex-producing plants in the industrial sectors worldwide. The RRIT 251 clone is well recognized for its high latex yield and tolerance to diverse environmental conditions. Although considerable efforts have been made to enhance the latex production of RRIT 251, a comprehensive analysis of the functional and structural properties of its proteins remains limited. In this study, an in-depth proteomic analysis was conducted on C-serum (CS) and rubber particles (RPs) to gain insights into the molecular mechanisms and biological processes involved in latex production in the RRIT 251 clone. A total of 3028 proteins were identified in CS and 1854 proteins in RPs. Based on the evolutionary genealogy of genes: Non-supervised Orthologous Groups (eggNOG), many of proteins were preliminary classified into three groups: posttranslational modification, protein turnover and chaperones. A comprehensive analysis of protein domain family (Pfam) revealed that the protein kinase and small GTP-binding domains were most frequently detected in CS and RP fractions. In addition, KEGG and Plant Reactome pathway enrichment analyses of CS and RP fractions showed significant association with the Metabolism category. Collectively, these results suggest that proteins from the CS and RP fractions of latex play essential roles in cellular and metabolic processes. These findings not only deepen our understanding of the RRIT 251 latex proteome but also provide further insights into the biological processes underlying latex production and plant defense.