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...
Saved in:
Published in | Plant physiology (Bethesda) Vol. 93; no. 1; pp. 105 - 109 |
---|---|
Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Rockville, MD
American Society of Plant Physiologists
01.05.1990
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
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 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0032-0889 1532-2548 |
DOI: | 10.1104/pp.93.1.105 |