Identification of the 64 kilodalton chloroplast stromal phosphoprotein as phosphoglucomutase
Phosphorylation of the 64 kilodalton stromal phosphoprotein by incubation of pea (Pisum sativum) chloroplast extracts with [gamma-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 chloroplast...
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Published in | Plant physiology (Bethesda) Vol. 93; no. 1; pp. 105 - 109 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Rockville, MD
American Society of Plant Physiologists
01.05.1990
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Abstract | Phosphorylation of the 64 kilodalton stromal phosphoprotein by incubation of pea (Pisum sativum) chloroplast extracts with [gamma-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 [gamma-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 [gamma-32P]ATP or [32P]Glc-l-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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AbstractList | Phosphorylation of the 64 kilodalton stromal phosphoprotein by incubation of pea (Pisum sativum) chloroplast extracts with ({gamma}-{sup 32}P)ATP decreased in the presence of Glc-6-P and Glc-1,6-P{sub 2}, but was stimulated by glucose. Two-dimensional gel electrophoresis following incubation of intact chloroplasts and stromal extracts with ({gamma}-{sup 32}P)ATP, or incubation of stromal extracts and partially purified phosphoglucomutase (EC 2.7.5.1) with ({sup 32}P)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 ({gamma}-{sup 32}P)ATP or ({sup 32}P)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. 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. Phosphorylation of the 64 kilodalton stromal phosphoprotein by incubation of pea (Pisum sativum) chloroplast extracts with [gamma-(32)P]ATP decreased in the presence of Glc-6-P and Glc-1,6-P(2), but was stimulated by glucose. Two-dimensional gel electrophoresis following incubation of intact chloroplasts and stromal extracts with [gamma-(32)P]ATP, or incubation of stromal extracts and partially purified phosphoglucomutase (EC 2.7.5.1) with [(32)P]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 [gamma-(32)P]ATP or [(32)P]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. Phosphorylation of the 64 kilodalton stromal phosphoprotein by incubation of pea (Pisum sativum) chloroplast extracts with [gamma-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 [gamma-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 [gamma-32P]ATP or [32P]Glc-l-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 |
Author | Drake, R.R McHale, N.A Broadbent, K.P Salvucci, M.E. (USDA, ARS, Lexington, KY) Haley, B.E Hanson, K.R |
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Keywords | Phosphorylation Radiolabelling Enzyme Phosphate sugar Phosphoglucomutase Leguminosae Phosphoproteins Dicotyledones Pisum sativum Angiospermae Spermatophyta Solanaceae ATP Chloroplast |
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Snippet | Phosphorylation of the 64 kilodalton stromal phosphoprotein by incubation of pea (Pisum sativum) chloroplast extracts with [gamma-32P]ATP decreased in the... Phosphorylation of the 64 kilodalton stromal phosphoprotein by incubation of pea (Pisum sativum) chloroplast extracts with [γ-32P]ATP decreased in the presence... Phosphorylation of the 64 kilodalton stromal phosphoprotein by incubation of pea (Pisum sativum) chloroplast extracts with [gamma-(32)P]ATP decreased in the... Phosphorylation of the 64 kilodalton stromal phosphoprotein by incubation of pea (Pisum sativum) chloroplast extracts with ({gamma}-{sup 32}P)ATP decreased in... |
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SubjectTerms | 550201 - Biochemistry- Tracer Techniques ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE Agriculture BASIC BIOLOGICAL SCIENCES BETA DECAY RADIOISOTOPES BETA-MINUS DECAY RADIOISOTOPES Biological and medical sciences Cell biochemistry CELL CONSTITUENTS Cell physiology CHEMICAL REACTIONS CHLOROPLASTS DAYS LIVING RADIOISOTOPES Electrophoresis ENZYME ACTIVITY ENZYMES FOSFORILACION Fundamental and applied biological sciences. Psychology Gels ISOTOPE APPLICATIONS ISOTOPES LEGUMINOSAE LIGHT NUCLEI MAGNOLIOPHYTA MAGNOLIOPSIDA METABOLITES MUTANT MUTANTES NICOTIANA NUCLEI ODD-ODD NUCLEI Peas PEPTIDE PEPTIDOS Phosphoproteins PHOSPHORUS 32 PHOSPHORUS ISOTOPES PHOSPHORUS-GROUP TRANSFERASES PHOSPHORYLATION PHOSPHOTRANSFERASES PISUM PISUM SATIVUM Plant physiology and development PLANTS PLASTE PLASTIDIOS Plastids RADIOISOTOPES Spinach TRACER TECHNIQUES TRANSFERASAS TRANSFERASE TRANSFERASES |
Title | Identification of the 64 kilodalton chloroplast stromal phosphoprotein as phosphoglucomutase |
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