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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Summary: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
Bibliography:F60
9040041
F30
ObjectType-Article-1
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ISSN:0032-0889
1532-2548
DOI:10.1104/pp.93.1.105