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Title of Journal: Acta Physiol Plant

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Abbravation: Acta Physiologiae Plantarum

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Springer-Verlag

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DOI

10.1016/j.actamat.2008.04.058

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1861-1664

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Molecular characterization of a cysteine proteinas

Authors: DaeYoung Jung Ok Ran Lee YuJin Kim JungHye Lee Rama Krishna Pulla Gayathri Sathiyaraj JuSun Shim DeokChun Yang
Publish Date: 2010/03/10
Volume: 32, Issue: 5, Pages: 961-970
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Abstract

Phytocystatins are plantderived cysteine proteinase inhibitors implicated in the endogenous regulation of protein turnover and defense mechanisms against insects and pathogens A cysteine proteinase inhibitor PgCPI was isolated and characterized from Panax ginseng Sequence analysis revealed that the coding cDNA sequence of PgCPI is 609 base pairs in length with a predicted molecular mass of 225 kDa A GenBank BlastX search revealed that the deduced amino acid sequence of PgCPI shares a highdegree homology with cysteine proteinase inhibitors from other plants In this present study we analyzed the expression patterns of PgCPI against various abiotic and biotic stresses at different time points using quantitative real timePCR Enzymatic activity of PgCPI was also determined against cysteine proteinase Our results reveal that PgCPI is moderately induced by NaCl chilling CuSO4 ABA and jasmonic acid However high light UV MeJA and wounding triggered a significant induction more than fourfold of PgCPI within 12h posttreatment especially PgCPI prominently accumulated by wounding 24fold In addition increased transcripts of PgCPI were investigated in fungal and nematodeinfected roots These results suggest that PgCPI is involved in defense responses to biotic and abiotic stresses

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