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Acclimation of the Photosynthetic Machinery to High Temperature inChlamydomonas reinhardtiiRequires Synthesis de Novo of Proteins Encoded by the Nuclear and Chloroplast Genomes
Author(s) -
Yuji Tanaka,
Yoshitaka Nishiyama,
Norio Murata
Publication year - 2000
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.124.1.441
Subject(s) - chlamydomonas reinhardtii , chloroplast , heat shock protein , biology , chlamydomonas , microbiology and biotechnology , protein biosynthesis , cycloheximide , hsp70 , photosystem ii , photosynthesis , acclimatization , biochemistry , biophysics , gene , botany , mutant
The mechanism responsible for the enhancement of the thermal stability of the oxygen-evolving machinery of photosystem II during acclimation of Chlamydomonas reinhardtii to high temperatures such as 35 degrees C remains unknown. When cells that had been grown at 20 degrees C were transferred to 35 degrees C, the thermal stability of the oxygen-evolving machinery increased and within 8 h it was equivalent to that in cells grown initially at 35 degrees C. Such enhancement of thermal stability was prevented by cycloheximide and by lincomycin, suggesting that the synthesis de novo of proteins encoded by both the nuclear and the chloroplast genome was required for this process. No increase in thermal stability was observed when cells that had been grown at 35 degrees C were exposed to heat shock at 41 degrees C, optimum conditions for the induction of the synthesis of homologs of three heat shock proteins (Hsps), namely, Hsp60, Hsp70, and Hsp22. Moreover, no synthesis of these homologs of Hsps was induced at 35 degrees C. Thus it appears likely that Hsps are not involved in the enhancement of the thermal stability of the oxygen-evolving machinery.

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