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Plant Physiology Preview Published on June 28, 2007; 10.1104/pp.107.103341
Received June 4, 2007 Long-term Response Towards Inorganic Carbon Limitation in Wild Type and Glycolate Turnover Mutants of the Cyanobacterium Synechocystis sp. Strain PCC 6803
Universität Rostock, Institut für Biowissenschaften, Abt. Pflanzenphysiologie, und Ökologie, Albert-Einstein-Strasse 3, D-18059 Rostock, Germany; University of Amsterdam, Institute for Biodiversity and Ecosystem Dynamics (IBED), Nieuwe Achtergracht 127, NL-1018WS Amsterdam, The Netherlands; Universität Rostock, Institut für Pathologie, Elektronenmikroskopisches Zentrum, Strempelstrasse 14, D-18055 Rostock, Germany; Netherlands Institute of Ecology (NIOO-KNAW), Centre for Limnology - Department of Foodweb Studies, Rijksstraatweg 6, NL-3631AC Nieuwersluis, The Netherlands and, Eawag, Swiss Federal Institute of Aquatic Sciences and Technology, Centre of Ecology, Evolution and Biogeochemistry, Seestrasse 79 CH-6047 Kastanienbaum, Switzerland * Corresponding author; email: martin.hagemann{at}uni-rostock.de.
Concerted changes in the transcriptional pattern and physiological traits that result from long-term (here defined as up to 24 h) limitation of inorganic carbon (Ci) have been investigated for the cyanobacterium Synechocystis sp. strain PCC6803. Results from RT-PCR and genome-wide DNA-microarray analyses indicated stable up-regulation of genes for inducible CO2 and HCO3- uptake systems and of the rfb cluster that encodes enzymes involved in outer cell wall polysaccharide synthesis. Coordinated up-regulation of photosystem 1 (PS1) genes was further found and supported by a higher PS1 content and activity under low Ci (LC) conditions. Bacterial-type glycerate pathway genes were induced by low Ci (LC) conditions, in contrast to the genes for the plant-like photorespiratory C2-cycle. Down-regulation was observed for nitrate assimilation genes and surprisingly also for almost all carboxysomal proteins. However, for the latter the observed elongation of the half life time of the RbcL protein may render compensation. Mutants defective in glycolate turnover (
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