Light-induced dephosphorylation of a 65-kDa protein in the cyanobacterium Synechocystis sp. PCC 6803

We found that a 65-kDa protein (p65) of Synechocystis sp. PCC 6803 is dephosphorylated in a light-dependent manner. In darkness, p65 was specifically phosphorylated and then completely dephosphorylated within 2 min upon exposure to high-intensity light. The phosphorylation of p65 recurred after 8 ho...

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Bibliographic Details
Published in:Journal of plant physiology 2003, Vol.160 (10), p.1259-1261
Main Authors: Choi, Jong-Soon, Ahn, Mi-Chung, Chung, Young-Ho, Kwon, Ohoak, Suh, Kyong Hoon, Park, Young Mok
Format: Article
Language:English
Subjects:
bacterial proteins
Bacteriology
Biological and medical sciences
Cell biochemistry
Cell physiology
dephosphorylation
Fundamental and applied biological sciences. Psychology
light
light-dependent dephosphorylation
Metabolism. Enzymes
Microbiology
phosphorylation
Plant physiology and development
plant proteins
Synechocystis sp. PCC 6803
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Summary:We found that a 65-kDa protein (p65) of Synechocystis sp. PCC 6803 is dephosphorylated in a light-dependent manner. In darkness, p65 was specifically phosphorylated and then completely dephosphorylated within 2 min upon exposure to high-intensity light. The phosphorylation of p65 recurred after 8 hours incubated in the dark following light exposure. Green (540-560 nm) and red (660 nm) light dephosphorylated p65 efficiently, with the efficiency being greater with green light. These results suggest that p65 is a novel substrate involved in the quantity and quality of light-dependent dephosphorylation in cyanobacteria.
ISSN:0176-1617
1618-1328
DOI:10.1078/0176-1617-01155