* Present addresses:
D.S: Institute of Microbiology, Academy of Science of the Czech Republic, CZ-379 01 TREBON, CZECH REPUBLIC;
M.D.S: ALK Labs , Böge Allé 10-12 DK-2970 Hörsholm, DENMARK
¤Corresponding author, Phone: +46-46 2227788; Fax: +46-46 2223684; email: john.allen@plantcell.lu.se
Running title: Phosphorylation controls LHC II structure
Keywords: Light harvesting complex; protein phosphorylation; photosynthesis; CD; NMR; FTIR
The most abundant chlorophyll-binding complex in plants is the intrinsic membrane protein Light-Harvesting Complex II. LHC II acts as a light-harvesting antenna and has an important role in the distribution of absorbed energy between the two photosystems of photosynthesis. We used spectroscopic techniques to study a synthetic peptide with identical sequence to the LHC IIb N-terminus found in pea, with and without the phosphorylated Thr at the 5th amino acid residue, and to study both forms of the native full-length protein. Our results show that the N-terminus of LHC II changes structure upon phosphorylation, and that the structural change resembles that of rabbit glycogen phosphorylase, one of the few phosphoproteins where both phosphorylated and non-phosphorylated structures have been solved. Our results indicate that phosphorylation of membrane proteins may regulate their function through structural protein-protein interactions in surface-exposed domains.
A kinemage demonstration of a three-dimensional structure that could give rise to such results can be downloaded from here.
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