PJB-2013-376
BACTERIAL EXPRESSION, PURIFICATION AND PARTIAL CHARACTERIZATION OF NEW RECOMBINANT CYSTEINE PROTEASE FROM MAIZE LEAVES: POST-TRANSCRIPTIONAL CHANGES UNDER OZONE STRESS
RAFIQ AHMAD1*,2, 3, YASMINE ZUILY-FODIL3, CHANTAL PASSAQUET3 AND JAM NAZEER AHMAD4
Abstract
Cysteine proteases are implicated in senescence, defense signaling pathways and cellular responses to biotic and abiotic stresses. In this context, we have cloned a novel cDNA encoding for papain family of cysteine protease from maize leaves. Mature part of papain-like protease was expressed in Escherichia coli using T7 promoter system. The recombinant protein was purified from inclusion bodies, refolded, characterized and used to produce corresponding antibodies in order to study post-transcriptional level of this specific protease under ozone stress. The results showed that ozone enhanced significantly papain-like cysteine protease at post-transcriptional level in 12th and 10th leaves of field grown maize plants. Simultaneously, senescence induced a rise in cysteine protease activity in both leaves. All together, these results suggest that ozone stress stimulates senescence processes, such as those related to proteolysis.
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