Identification of the 64 kilodalton chloroplast stromal phosphoprotein as phosphoglucomutase |
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| Authors: | Salvucci M E Drake R R Broadbent K P Haley B E Hanson K R McHale N A |
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| Affiliation: | U.S. Department of Agriculture, Agricultural Research Service, University of Kentucky, Lexington, Kentucky 40546. |
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| Abstract: | Phosphorylation of the 64 kilodalton stromal phosphoprotein by incubation of pea (Pisum sativum) chloroplast extracts with γ-32P]ATP decreased in the presence of Glc-6-P and Glc-1,6-P2, but was stimulated by glucose. Two-dimensional gel electrophoresis following incubation of intact chloroplasts and stromal extracts with γ-32P]ATP, or incubation of stromal extracts and partially purified phosphoglucomutase (EC 2.7.5.1) with 32P]Glc-1-P showed that the identical 64 kilodalton polypeptide was labeled. A 62 kilodalton polypeptide was phosphorylated by incubation of tobacco (Nicotiana sylvestris) stromal extracts with either γ-32P]ATP or 32P]Glc-1-P. In contrast, an analogous polypeptide was not phosphorylated in extracts from a tobacco mutant deficient in plastid phosphoglucomutase activity. The results indicate that the 64 (or 62) kilodalton chloroplast stromal phosphoprotein is phosphoglucomutase. |
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