Co-Authors:
Ferguson, I.B., The Horticulture and Food Research Institute, Mt. Albert, Auckland, New Zealand
Lay Yee, M., The Horticulture and Food Research Institute, Mt. Albert, Auckland, New Zealand
Watkins, C.B., Department of Fruit and Vegetable Science, Cornell University, Ithaca, NY, United States
Lurie, S., Department of Postharvest Science, Volcani Center, ARO, Bet Dagon, 50250, Israel
Abstract:
Phosphorylation of membrane proteins was studied in suspension cultured pear (Pyrus communis L. cv. Passe Crassane) cells in response to a heat shock of 38°C for 2 h. Protein kinase activity was assayed in the membrane preparation, and was significantly reduced by heat treatment of the cells. The presence of EGTA in the assay medium reduced kinase activity about 60% in membranes from unheated cells and 40% in membranes of heated cells. In vitro labelling of membrane preparations with [32P]ATP for 60 s resulted in some bands more heavily labelled in heated membranes than in unheated ones. When in vivo labelling of proteins with 32P was done during the second hour of heating, there were differences in labelled membrane proteins, compared with membrane proteins from unheated cells. Incorporation of [35S]methionine during the second hour of treatment resulted in the synthesis of a number of heat shock proteins, two of which had the same Mr as phosphorylated proteins. These results indicate that membrane protein phosphorylation may be involved in the response of cells to heat shock. © 1994.
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