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Phosphorylation Controls the Three-dimensional Structure of Plant Light Harvesting Complex II*
 

Summary: Phosphorylation Controls the Three-dimensional Structure of Plant
Light Harvesting Complex II*
(Received for publication, February 25, 1997, and in revised form, April 30, 1997)
Anders Nilsson, Dalibor Stys§, Torbjo¨rn Drakenberg¶, Michael D. Spangfort§ , Sture Forse´n¶,
and John F. Allen**
From Plant Cell Biology, Box 7007, Lund University, S-220 07 Lund, ¶Physical Chemistry 2, Box 124, Lund University,
S-221 00 Lund, and Biochemistry, Box 124, Lund University, S-221 00 Lund, Sweden
The most abundant chlorophyll-binding complex in
plants is the intrinsic membrane protein light-harvest-
ing complex II (LHC 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 pho-
tosynthesis. 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 phos-
phorylated 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 phosphoryl-

  

Source: Allen, John F. - School of Biological and Chemical Sciences, Queen Mary, University of London

 

Collections: Renewable Energy; Biology and Medicine