Phosphorylation of photosystem II components, CP43 apoprotein, D1, D2, and 10 to 11 kilodalton protein in chloroplast thylakoids of higher plants
Abstract
Phosphorylated thylakoid proteins of spinach (Spinacia oleracea L.) and pea (Pisum sativum L.) were solubilized, fractionated by sucrose density gradient centrifugation, and analyzed by gel electrophoresis and crossed immunoelectrophoresis to identify the phosphoproteins. It was found that in addition to intense phosphorylation of light-harvesting chlorophyll complex II, four photosystem II components, CP43 apoprotein, D1, D2, and a 10 to 11 kilodalton protein, are substantially phosphorylated in the light. Furthermore, the CP43 apoprotein, D1 and D2 can be resolved into two electrophoretic subspecies, only one of which is phosphorylated. This indicates that only a fraction of the PSII polypeptides is phosphorylated. Finally, analysis of detergent procedures suggests that the 10 to 11 kilodalton phosphoprotein is a peripheral component of the O/sub 2/-evolving PSII reaction center complex.
- Authors:
- Publication Date:
- Research Org.:
- Institute of Physical and Chemical Research (RIKEN), Saitama, Japan
- OSTI Identifier:
- 5563213
- DOE Contract Number:
- FG09-84ER13188
- Resource Type:
- Journal Article
- Journal Name:
- Plant Physiol.; (United States)
- Additional Journal Information:
- Journal Volume: 85:3
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; PHOTOSYNTHETIC REACTION CENTERS; BIOCHEMICAL REACTION KINETICS; PROTEINS; FRACTIONATION; PHOSPHORYLATION; CHLOROPLASTS; ELECTROPHORESIS; PISUM; SPINACH; ULTRACENTRIFUGATION; BACTERIA; CELL CONSTITUENTS; CENTRIFUGATION; CHEMICAL REACTIONS; FOOD; KINETICS; LEGUMINOSAE; MICROORGANISMS; ORGANIC COMPOUNDS; PLANTS; REACTION KINETICS; RHIZOBIUM; SEPARATION PROCESSES; VEGETABLES; 550200* - Biochemistry
Citation Formats
Ikeuchi, M, Plumley, F G, Inoue, Y, and Schmidt, G W. Phosphorylation of photosystem II components, CP43 apoprotein, D1, D2, and 10 to 11 kilodalton protein in chloroplast thylakoids of higher plants. United States: N. p., 1987.
Web. doi:10.1104/pp.85.3.638.
Ikeuchi, M, Plumley, F G, Inoue, Y, & Schmidt, G W. Phosphorylation of photosystem II components, CP43 apoprotein, D1, D2, and 10 to 11 kilodalton protein in chloroplast thylakoids of higher plants. United States. https://doi.org/10.1104/pp.85.3.638
Ikeuchi, M, Plumley, F G, Inoue, Y, and Schmidt, G W. 1987.
"Phosphorylation of photosystem II components, CP43 apoprotein, D1, D2, and 10 to 11 kilodalton protein in chloroplast thylakoids of higher plants". United States. https://doi.org/10.1104/pp.85.3.638.
@article{osti_5563213,
title = {Phosphorylation of photosystem II components, CP43 apoprotein, D1, D2, and 10 to 11 kilodalton protein in chloroplast thylakoids of higher plants},
author = {Ikeuchi, M and Plumley, F G and Inoue, Y and Schmidt, G W},
abstractNote = {Phosphorylated thylakoid proteins of spinach (Spinacia oleracea L.) and pea (Pisum sativum L.) were solubilized, fractionated by sucrose density gradient centrifugation, and analyzed by gel electrophoresis and crossed immunoelectrophoresis to identify the phosphoproteins. It was found that in addition to intense phosphorylation of light-harvesting chlorophyll complex II, four photosystem II components, CP43 apoprotein, D1, D2, and a 10 to 11 kilodalton protein, are substantially phosphorylated in the light. Furthermore, the CP43 apoprotein, D1 and D2 can be resolved into two electrophoretic subspecies, only one of which is phosphorylated. This indicates that only a fraction of the PSII polypeptides is phosphorylated. Finally, analysis of detergent procedures suggests that the 10 to 11 kilodalton phosphoprotein is a peripheral component of the O/sub 2/-evolving PSII reaction center complex.},
doi = {10.1104/pp.85.3.638},
url = {https://www.osti.gov/biblio/5563213},
journal = {Plant Physiol.; (United States)},
number = ,
volume = 85:3,
place = {United States},
year = {Sun Nov 01 00:00:00 EST 1987},
month = {Sun Nov 01 00:00:00 EST 1987}
}