Evidence of protein-tyrosine kinase activity in Catharanthus roseus roots transformed by Agrobacterium rhizogenes |
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Authors: | Luis Carlos Rodríguez-Zapata S M Teresa Hernández-Sotomayor |
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Institution: | (1) Unidad de Biología Experimental, Centro de Investigación Científica de Yucatán Apdo., Postal 87 Cordemex, Yucatán 97310, México, |
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Abstract: | Homogenate fractions (soluble and particulate) from transformed roots of Catharanthus roseus (L.) G. Don showed several phosphorylated proteins when incubated with γ-32P]ATP. The phosphorylation in the proteins of 55, 40, 25, 18 and 10 kDa in the particulate fraction and 63 kDa in the soluble
fraction was resistant to alkali treatment. Several proteins in both fractions gave a positive signal with monoclonal antiphosphotyrosine
antibodies. In-situ phosphorylation in both fractions showed several proteins that cross-reacted with the antiphosphotyrosine
antibodies. Tyrosine kinase activity was detected using an exogenous substrate RR-SRC, a synthetic peptide derived from the
amino acid sequence surrounding the phosphorylation site in pp60src. This activity was inhibited by genistein, a tyrosine kinase inhibitor. These results indicate, for the first time, the presence
of protein-tyrosine kinase (EC 2.7.1.112) activity in transformed plant tissues.
Received: 29 March 1997 / Accepted: 21 May 1997 |
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Keywords: | :Catharanthus (transformed) Protein phos-phorylation Signal transduction Tyrosine kinase |
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