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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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Published in: | Journal of plant physiology 2003, Vol.160 (10), p.1259-1261 |
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creator | Choi, Jong-Soon Ahn, Mi-Chung Chung, Young-Ho Kwon, Ohoak Suh, Kyong Hoon Park, Young Mok |
description | 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. |
doi_str_mv | 10.1078/0176-1617-01155 |
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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.</description><identifier>ISSN: 0176-1617</identifier><identifier>EISSN: 1618-1328</identifier><identifier>DOI: 10.1078/0176-1617-01155</identifier><identifier>CODEN: JPPHEY</identifier><language>eng</language><publisher>Jena: Elsevier GmbH</publisher><subject>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</subject><ispartof>Journal of plant physiology, 2003, Vol.160 (10), p.1259-1261</ispartof><rights>2003 Urban & Fischer Verlag</rights><rights>2004 INIST-CNRS</rights><rights>Copyright Urban & Fischer Verlag Oct 2003</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c324t-5d8146cae0ab468a3885404978e5ac368c6e320bc971d7886a041719fb9ffac33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,4024,27923,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15193779$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Choi, Jong-Soon</creatorcontrib><creatorcontrib>Ahn, Mi-Chung</creatorcontrib><creatorcontrib>Chung, Young-Ho</creatorcontrib><creatorcontrib>Kwon, Ohoak</creatorcontrib><creatorcontrib>Suh, Kyong Hoon</creatorcontrib><creatorcontrib>Park, Young Mok</creatorcontrib><title>Light-induced dephosphorylation of a 65-kDa protein in the cyanobacterium Synechocystis sp. PCC 6803</title><title>Journal of plant physiology</title><description>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.</description><subject>bacterial proteins</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Cell biochemistry</subject><subject>Cell physiology</subject><subject>dephosphorylation</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>light</subject><subject>light-dependent dephosphorylation</subject><subject>Metabolism. Enzymes</subject><subject>Microbiology</subject><subject>phosphorylation</subject><subject>Plant physiology and development</subject><subject>plant proteins</subject><subject>Synechocystis sp. 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PCC 6803</atitle><jtitle>Journal of plant physiology</jtitle><date>2003</date><risdate>2003</risdate><volume>160</volume><issue>10</issue><spage>1259</spage><epage>1261</epage><pages>1259-1261</pages><issn>0176-1617</issn><eissn>1618-1328</eissn><coden>JPPHEY</coden><abstract>We found that a 65-kDa protein (p65) of
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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 |
title | Light-induced dephosphorylation of a 65-kDa protein in the cyanobacterium Synechocystis sp. PCC 6803 |
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