TY  - JOUR
A1  - Juhas, Matthias
A1  - Büchel, Claudia
T1  - Properties of photosystem I antenna protein complexes of the diatom Cyclotella meneghiniana
T2  - Journal of Experimental Botany
N2  - Analysis of photosystem I (PSI) complexes from Cyclotella meneghiniana cultured under different growth conditions led to the identification of three groups of antenna proteins, having molecular weights of around 19, 18, and 17 kDa. The 19-kDa proteins have earlier been demonstrated to be more peripherally bound to PSI, and their amount in the PSI complexes was significantly reduced when the iron supply in the growth medium was lowered. This polypeptide was almost missing, and thus the total amount of fucoxanthin-chlorophyll proteins (Fcps) bound to PSI was reduced as well. When treating cells with high light in addition, no further changes in antenna polypeptide composition were detected. Xanthophyll cycle pigments were found to be bound to all Fcps of PSI. However, PSI of high light cultures had a significantly higher diatoxanthin to diadinoxanthin ratio, which is assumed to protect against a surplus of excitation energy. PSI complexes from the double-stressed cultures (high light plus reduced iron supply) were slightly more sensitive against destruction by the detergent treatment. This could be seen as a higher 674-nm emission at 77 K in comparison to the PSI complexes isolated from other growth conditions. Two major emission bands of the Fcps bound to PSI at 77 K could be identified, whereby chlorophyll a fluorescing at 697 nm was more strongly coupled to the PSI core than those fluorescing at 685 nm. Thus, the build up of the PSI antenna of several Fcp components enables variable reactions to several stress factors commonly experienced by the diatoms in vivo, in particular diatoxanthin enrichment under high light and reduction of antenna size under reduced iron conditions.
KW  - diatoxanthin
KW  - Fcp4
KW  - fucoxanthin-chlorophyll-proteins
KW  - high light adaptation
KW  - iron
KW  - Lhcr
Y1  - 2012
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/25946
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-259460
SN  - 0022-0957
SN  - 1460-2431
VL  - 63
IS  - 10
SP  - 3673
EP  - 3681
PB  - Univ. Press
CY  - Oxford
ER  -