Methyl jasmonate changes the levels of rubisco and other leaf proteins in Ricinus communis |
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Authors: | Ana Paula Rodrigues Cavalcante Tânia Jacinto Olga Lima Tavares Machado |
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Affiliation: | 1. Laboratório de Química e Fun??o de Proteínas e Peptídeos, Centro de Biociências e Biotecnologia, Universidade Federal do Norte Fluminense (LQFPP/CBB/UENF), Brazil 2. Laboratório de Biotecnologia (LBT/CBB/UENF), Brazil 3. Departamento de Bioquímica, Instituto de Biologia, Universidade Estadual do Rio de Janeiro (IB/UERJ), Brazil
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Abstract: | The effect of methyl jasmonate (MJ) on the water-soluble protein pattern of Ricinus communis leaves was analyzed. Several dynamic changes occurred after a period of 24 and 48h including six proteins (Mr 13,000, 15,000, 16,000, 27,000, 29,000 and 60,000) whose levels increased by 48h and seven others (Mr 11,000, 18,000, 20,000 30,000, 37,000, 40,000 and 58,000) whose levels decreased. Four proteins (Mr 24,000, 34,000, 64,000 and 66,000) were induced after 24h of treatment, but returned to control levels by 48h. On the other hand, the levels of three proteins (Mr 74,000, 84,000 and 88,000) decreased after 24h, but returned to control levels after 48h. One of the proteins that accumulated after 48 h had the 13 first residues sequenced. This polypeptide named MJRC-15, was identical to the C-terminal sequence of Rubisco-large chain polypeptide (position 337–350) from tobacco chloroplast. Western-blot analysis using polyclonal antibodies against Rubisco supports the hypothesis that MJRC-15 is a degradation product of Rubisco. |
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Keywords: | castor bean methyl jasmonate Ricinus communis Rubisco |
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