Journal of Biosciences

, Volume 30, Issue 3, pp 351–357

Expression of a ribosome inactivating protein (curcin 2) inJatropha curcas is induced by stress

  • Wei Qin
  • Huang Ming-Xing
  • Xu Ying
  • Zhang Xin-Shen
  • Chen Fang
Article

Abstract

The open reading frame (ORF) encoding curcin 2 was cloned from total genomic and cDNA ofJatropha curcas leaves, which were treated by drought, temperature stress and fungal infection, by polymerase chain reaction (PCR) and reverse transcriptase (RT)-PCR amplification. The ORF has 927 bp that encodes a precursor protein of 309 amino acid residues. There are high similarities with curcin and the conserved domain of ribosome inactivating proteins (RIPs). Antiserum to curcin recognized one band of 32 kDa on Western blot of the leaves treated by temperature stresses at 4°C and 50°C and by fungal infections ofPestalotia funerea, Curvularia lunata (Walk) Boed,Gibberelle zeae (Schw.) Petch. Two bands of 32 kDa and 65 kDa were recognized on Western blot of the leaves treated by 10%-40% polyethylene glycol (PEG). In addition, the 32 kDa band is nearly the molecular weight of curcin 2. This finding suggests that the protein of 32 kDa should be related to curcin 2. The presence of this protein molecular marker under stresses may provide an experimental foundation to study the stress proteins inJ. curcas.

Keywords

Curcin 2 Jatropha curcas protein induction stress 

Abbreviations used

ORF

open reading frame

PEG

polyethylene glycol

RIPs

ribosome inactivating proteins

RT-PCR

reverse transcriptase-polymerase chain reaction

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Copyright information

© Indian Academy of Sciences 2005

Authors and Affiliations

  • Wei Qin
    • 2
    • 3
  • Huang Ming-Xing
    • 1
  • Xu Ying
    • 1
  • Zhang Xin-Shen
    • 3
  • Chen Fang
    • 1
  1. 1.College of Life SciencesSichuan UniversityChengduPR China
  2. 2.Department of Biological EngineeringYibin UniversityYinbinPR China
  3. 3.College of Light Industry and Food Engineering SciencesSichuan UniversityChengduPR China

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