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Differential Control of Xanthophylls and Light-Induced Stress
Proteins, as Opposed to Light-Harvesting Chlorophyll a/b
Proteins, during Photosynthetic Acclimation of Barley Leaves to Light
Irradiance
Marie-Hélène Montané,
Florence Tardy1,
Klaus Kloppstech, and
Michel Havaux*
Commissariat à l'Energie Atomique/Cadarache,
Département d'Ecophysiologie Végétale et de
Microbiologie, Laboratoire de Radiobiologie Végétale
(M.-H.M.), and Laboratoire d'Ecophysiologie de la
Photosynthèse (F.T., M.H.), F-13108 Saint-Paul-lez-Durance,
France; and F-13108 Saint-Paul-lez-Durance,
FranceInstitute of Botany, Hannover University,
Herrenhäuser Strasse 2, D-30419 Hannover, Germany (K.K.)
Barley (Hordeum
vulgare L.) plants were grown at different photon flux
densities ranging from 100 to 1800 µmol m 2
s 1 in air and/or in atmospheres with reduced levels of
O2 and CO2. Low O2 and
CO2 partial pressures allowed plants to grow under high
photosystem II (PSII) excitation pressure, estimated in vivo by
chlorophyll fluorescence measurements, at moderate photon flux densities. The xanthophyll-cycle pigments, the early light-inducible proteins, and their mRNA accumulated with increasing PSII excitation pressure irrespective of the way high excitation pressure was obtained
(high-light irradiance or decreased CO2 and O2
availability). These findings indicate that the reduction state of
electron transport chain components could be involved in light sensing
for the regulation of nuclear-encoded chloroplast gene expression. In
contrast, no correlation was found between the reduction state of PSII
and various indicators of the PSII light-harvesting system, such as the
chlorophyll a-to-b ratio, the abundance of the
major pigment-protein complex of PSII (LHCII), the mRNA level of LHCII,
the light-saturation curve of O2 evolution, and the induced
chlorophyll-fluorescence rise. We conclude that the chlorophyll antenna
size of PSII is not governed by the redox state of PSII in higher
plants and, consequently, regulation of early light-inducible protein
synthesis is different from that of LHCII.
1
Present address: Laboratoire de Chimie Physique
des Macromolécules aux Interfaces, Université Libre de
Bruxelles, B-1050 Bruxelles, Belgium.
*
Corresponding author; e-mail michel.havaux{at}cea.fr; fax
33-4-4225-6265.
Plant Physiol. (1998) 118: 227-235
Copyright Clearance Center: 0032-0889/98/118//09
© 1998 American Society of Plant Physiologists
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