The N‐terminal domain of the light‐harvesting chlorophyll a/b‐binding protein complex (LHCII) is essential for its acclimative proteolysis

FEBS Letters

Yang, Dan-Hui²  Paulsen, Harald¹  Andersson, Bertil² 

[1] Institut für Allgemeine Botanik, Johannes Gutenberg-Universität Mainz, Müllerweg 6, D-55099 Mainz, Germany;Department of Biochemistry, Arrhenius Laboratories for Natural Sciences, Stockholm University, SE-106 91 Stockholm, Sweden

关键词: Light-harvesting complex II;    Proteolysis;    Acclimative protease;    N-terminal domain;    Recognition site;    Recombinant light-harvesting complex II;    chl;    chlorophyll;    ECL;    enhanced chemiluminescence;    LHCII;    light-harvesting chlorophyll a/b protein complex of photosystem II;    LM;    lauryl maltoside;    OG;    octyl glucoside;    PFD;    photon flux density;    SDS;    sodium dodecyl sulfate;    PAGE;    polyacrylamide gel electrophoresis;   

DOI  :  10.1016/S0014-5793(00)01107-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Variations in the amount of the light-harvesting chlorophyll a/b-binding protein complex (LHCII) is essential for regulation of the uptake of light into photosystem II. An endogenous proteolytic system was found to be involved in the degradation of LHCII in response to elevated light intensities and the proteolysis was shown to be under tight regulation [Yang, D.-H. et al. (1998) Plant Physiol. 118, 827–834]. In this study, the substrate specificity and recognition site towards the protease were examined using reconstituted wild-type and mutant recombinant LHCII. The results show that the LHCII apoprotein and the monomeric form of the holoprotein are targeted for proteolysis while the trimeric form is not. The N-terminal domain of LHCII was found to be essential for recognition by the regulatory protease and the involvement of the N-end rule pathway is discussed.

【 授权许可】

Unknown