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 inPlant physiology (Bethesda) Vol. 93; no. 1; pp. 105 - 109
Main Authors Salvucci, M.E. (USDA, ARS, Lexington, KY), Drake, R.R, Broadbent, K.P, Haley, B.E, Hanson, K.R, McHale, N.A
Format Journal Article
LanguageEnglish
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
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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Issue 1
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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StartPage 105
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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