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Supermolecular organization of photosystem II and its associated light‐harvesting antenna in Arabidopsis thaliana
Author(s) -
Yakushevska Alevtyna E.,
Jensen Poul E.,
Keegstra Wilko,
van Roon Henny,
Scheller Henrik V.,
Boekema Egbert J.,
Dekker Jan P.
Publication year - 2001
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.0014-2956.2001.02505.x
Subject(s) - spinach , photosystem ii , crystallography , arabidopsis thaliana , arabidopsis , chemistry , light harvesting complex , single particle analysis , photosystem , biophysics , biology , photosynthesis , biochemistry , aerosol , organic chemistry , mutant , gene
The organization of Arabidopsis thaliana photosystem II (PSII) and its associated light‐harvesting antenna (LHCII) was studied in isolated PSII–LHCII supercomplexes and native membrane‐bound crystals by transmission electron microscopy and image analysis. Over 4000 single‐particle projections of PSII–LHCII supercomplexes were analyzed. In comparison to spinach supercomplexes [Boekema, E.J., van Roon, H., van Breemen, J.F.L. & Dekker, J.P. (1999) Eur. J. Biochem . 266 , 444–452] some striking differences were revealed: a much larger number of supercomplexes from Arabidopsis contain copies of M‐type LHCII trimers. M‐type trimers can also bind in the absence of the more common S‐type trimers. No binding of l ‐type trimers could be detected. Analysis of native membrane‐bound PSII crystals revealed a novel type of crystal with a unit cell of 25.6 × 21.4 nm (angle 77°), which is larger than any of the PSII lattices observed before. The data show that the unit cell is built up from C 2 S 2 M 2 supercomplexes, rather than from C 2 S 2 M supercomplexes observed in native membrane crystals from spinach [Boekema, E.J., Van Breemen, J.F.L., Van Roon, H. & Dekker, J.P. (2000) J. Mol. Biol. 301 , 1123–1133]. It is concluded from both the single particle analysis and the crystal analysis that the M‐type trimers bind more strongly to PSII core complexes in Arabidopsis than in spinach.

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