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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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