2005
DOI: 10.1007/bf02703672
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Expression of a ribosome inactivating protein (curcin 2) inJatropha curcas is induced by stress

Abstract: The open reading frame (ORF) encoding curcin 2 was cloned from total genomic and cDNA of Jatropha 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 Weste… Show more

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Cited by 51 publications
(21 citation statements)
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“…Transcripts for curcin 2 [20] were not present. Unlike ricin from castor, the type-I RIPs of J. curcas lack a lectin cell binding domain and are thus thought to be only mildly cytotoxic upon ingestion [21,22].…”
Section: Ribosome-inactivating Proteins Of J Curcasmentioning
confidence: 86%
“…Transcripts for curcin 2 [20] were not present. Unlike ricin from castor, the type-I RIPs of J. curcas lack a lectin cell binding domain and are thus thought to be only mildly cytotoxic upon ingestion [21,22].…”
Section: Ribosome-inactivating Proteins Of J Curcasmentioning
confidence: 86%
“…Nonetheless, the hypothesis of a defensive role is supported by several lines of experimental evidence. The expression of RIP genes can be regulated by biotic stress, including viral [10] or fungal [11,12] infections, and during plant senescence [13]. The proposed mechanisms for the RIP antimicrobial activity are quite controversial in literature; some authors identified the host ribosomes as the main target of endogenous RIPs, while others claimed that the defense mechanism may be exerted by direct interaction of RIP with invading pathogens (reviewed in [9]).…”
Section: Introductionmentioning
confidence: 99%
“…Jatropha curcas is a well-known and mass cultivated multipurpose plant with immense medicinal value [22][23][24] . Felke 25 isolated the toxic principle curcin, from the seeds of this plant which is a type 1 RIP possessing strong inhibitory activity on protein synthesis 1 along with N-glycosidase and antitumor activities 4,[26][27][28] . Recent works have demonstrated the cancer directed therapeutic potential of this RIP in conjunction with peptides and nanoparticles 29,30 , additionally emphasizing the compatibility of curcin to collaborate with various delivery strategies without compromising on its activity.…”
mentioning
confidence: 99%