Phosphorylation of photosystem II components, CP43 apoprotein, D1, D2, and 10 to 11 kilodalton protein in chloroplast thylakoids of higher plants

Journal Article · Sun Nov 01 04:00:00 EST 1987 · Plant Physiol.; (United States)

DOI:https://doi.org/10.1104/pp.85.3.638· OSTI ID:5563213

Ikeuchi, M; Plumley, F G; Inoue, Y; Schmidt, G W

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.

• Research Organization: Institute of Physical and Chemical Research (RIKEN), Saitama, Japan
• DOE Contract Number: FG09-84ER13188
• OSTI ID: 5563213
• Journal Information: Plant Physiol.; (United States), Journal Name: Plant Physiol.; (United States) Vol. 85:3; ISSN PLPHA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
BACTERIA
BIOCHEMICAL REACTION KINETICS
CELL CONSTITUENTS
CENTRIFUGATION
CHEMICAL REACTIONS
CHLOROPLASTS
ELECTROPHORESIS
FOOD
FRACTIONATION
KINETICS
LEGUMINOSAE
MICROORGANISMS
ORGANIC COMPOUNDS
PHOSPHORYLATION
PHOTOSYNTHETIC REACTION CENTERS
PISUM
PLANTS
PROTEINS
REACTION KINETICS
RHIZOBIUM
SEPARATION PROCESSES
SPINACH
ULTRACENTRIFUGATION
VEGETABLES