TY - JOUR
T1 - Supermolecular organization of photosystem II and its associated light-harvesting antenna in Arabidopsis thaliana.
AU - Yakushevska, A.E.
AU - Jensen, P.E.
AU - Keegstra, W.
AU - van Roon, H.
AU - Scheller, H.V.
AU - Boekema, E.J.
AU - Dekker, J.P.
PY - 2001
Y1 - 2001
N2 - 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
AB - 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
U2 - 10.1046/j.0014-2956.2001.02505.x
DO - 10.1046/j.0014-2956.2001.02505.x
M3 - Article
SN - 0014-2956
VL - 268
SP - 6020
EP - 6028
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
ER -