Plant and Cell Physiology Advance Access originally published online on December 22, 2005
Plant and Cell Physiology 2006 47(2):270-276; doi:10.1093/pcp/pci245
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In vivo Fragmentation of the Large Subunit of Ribulose-1,5-Bisphosphate Carboxylase by Reactive Oxygen Species in an Intact Leaf of Cucumber under Chilling-light Conditions
Department of Applied Plant Science, Graduate School of Agricultural Science, Tohoku University, Tsutsumidori-Amamiyamachi, Sendai, 981-8555 Japan
* Corresponding author: E-mail, hiroyuki{at}biochem.tohoku.ac.jp; Fax, +81-22-717-8765.
Previous studies have demonstrated that the large subunit (LSU) of ribulose-1,5-bisphosphate carboxylase (Rubisco) is site-specifically cleaved by a hydroxyl radical (·OH) generated in the illuminated chloroplast lysates or by an artificial ·OH-generating system. However, it is not known whether such cleavage of the LSU by reactive oxygen species (ROS) actually occurs in an intact leaf. When leaf discs of chilling-sensitive cucumber (Cucumis sativus L.) were illuminated at 4°C, five major fragments of the LSU were observed. This fragmentation was completely inhibited by ROS scavengers, such as n-propyl gallate (for ·OH) and 1,2-dihydroxybenzene-3,5-disulfonic acid (Tiron) (for superoxide). FeSO4 stimulated this fragmentation, whereas an iron-specific chelator, deferoxamine, suppressed it. Furthermore, such fragments were identical to those generated from the purified Rubisco by an ·OH-generating system in vitro on two-dimensional PAGE. These results indicate that the direct fragmentation of the LSU by reacive oxygen species also occurs in an intact leaf.
(Received June 1, 2005; Accepted December 12, 2005)
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