Light-induced dephosphorylation of a 65-kDa protein in the cyanobacterium Synechocystis sp. PCC6803.
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.
Choi
Jong-Soon
JS
Proteome Analysis Team, Korea Basic Science Institute, Daejeon 305-333, Korea.
Ahn
Mi-Chung
MC
Chung
Young-Ho
YH
Kwon
Ohoak
O
Suh
Kyong Hoon
KH
Park
Young Mok
YM
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism* / Q000528:radiation effects; D000458:Cyanobacteria / Q000378:metabolism* / Q000528:radiation effects*; D008027:Light; D008970:Molecular Weight; D010766:Phosphorylation; D018462:Photobiology; D020283:Photoreceptors, Microbial / Q000737:chemistry / Q000378:metabolism / Q000528:radiation effects
D001426:Bacterial Proteins; D020283:Photoreceptors, Microbial