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Photo- and Metabolite Regulation of the Synthesis of Ribulose Bisphosphate Carboxylase/Oxygenase and the Phycobiliproteins in the Alga Cyanidium caldarium
Author(s) -
Klaus Steinmüller,
Klaus Zetsche
Publication year - 1984
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.76.4.935
Subject(s) - phycobiliprotein , ribulose 1,5 bisphosphate , oxygenase , metabolite , pyruvate carboxylase , biochemistry , chemistry , rubisco , biology , cyanobacteria , photosynthesis , enzyme , bacteria , genetics
In the eukaryotic and unicellular alga Cyanidium caldarium the synthesis of the plastid enzyme ribulose bisphosphate carboxylase/oxygenase (RuBPCase) and the light gathering proteins phycocyanin (PC) and allophycocyanin (APC) is under the control of light and glucose, which is a metabolizable carbon source for this organism. Light promotes the synthesis of these proteins while glucose has a strong inhibitory effect on this process. All subunits of the proteins mentioned above are in vitro translation products of poly (A)(-)-RNA (Steinmüller, Kaling, Zetsche 1983 Planta 159: 308-313). Both factors-light and glucose-exert their effects mainly by modulation of the level of translatable messenger RNA for these proteins. Under autotrophic growth conditions the level of translatable RuBPCase-, PC-, and APC-messenger RNA is high, whereas in the presence of glucose the level of these mRNAs is low or not detectable at all.

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