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Çѱ¹½Ä¹°ÇÐȸ / v.47, no.4, 2004³â, pp.330-337

( Defects in a Proteolytic Step of Light-Harvesting Complex II in an Arabidopsis Stay-Green Mutant, ore10, during Dark-Induced Leaf Senescence )
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During dark-induced leaf senescence (DIS), the non-functional stay-green mutant ore10 showed delayed chlorophyll (Chl) degradation and increased stability in its light-harvesting complex II (LHCII). These phenomena were closely related to the formation of aggregates that mainly consisted of terminal-truncated LHCII (Oh et al., 2003). The ore10 mutant apparently lacks the protease needed to degrade the truncated LHCII. In wild-type (WT) plants, protease was found in the thylakoid fraction, but not the soluble fraction. A similar experiment using dansylated LHCII revealed that the protease degraded both WT and ore10 LHCII, indicating that its stability in ore10 perhaps did not result from a defect in the LHCII polypeptides themselves. Although protease activity was not present in non-senesced WT leaves, it was induced during DIS. It also was possible to diminish the high level of protease present in the thylakoids through high-salt washing, suggesting that this enzyme is extrinsically bound to the outer surface of the stroma-exposed thylakoid regions.
 
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Arabidopsis thaliana;leaf senescence;light-harvesting complex II;proteolysis;stay-green mutant;
 
Journal of Plant Biology / v.47, no.4, 2004³â, pp.330-337
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ISSN : 1226-9239
UCI : G100:I100-KOI(KISTI1.1003/JNL.JAKO200415875830685)
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