Conversion of photosystem II dimer to monomers during photoinhibition is tightly coupled with decrease in oxygen-evolving activity in the diatom Chaetoceros gracilis

The rapid turnover of photosystem II (PSII) in diatoms is thought to be at an exceptionally high rate compared with other oxyphototrophs; however, its molecular mechanisms are largely unknown. In this study, we examined the photodamage and repair processes of PSII in the marine centric diatom Chaeto...

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Veröffentlicht in:Photosynthesis research 2016-12, Vol.130 (1-3), p.83-91
Hauptverfasser: Nagao, Ryo, Tomo, Tatsuya, Narikawa, Rei, Enami, Isao, Ikeuchi, Masahiko
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container_issue 1-3
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container_title Photosynthesis research
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creator Nagao, Ryo
Tomo, Tatsuya
Narikawa, Rei
Enami, Isao
Ikeuchi, Masahiko
description The rapid turnover of photosystem II (PSII) in diatoms is thought to be at an exceptionally high rate compared with other oxyphototrophs; however, its molecular mechanisms are largely unknown. In this study, we examined the photodamage and repair processes of PSII in the marine centric diatom Chaetoceros gracilis incubated at 30 or 300 μmol photons m −2  s −1 in the presence of a de novo protein-synthesis inhibitor. When de novo protein synthesis was blocked by chloramphenicol (Cm), oxygen-evolving activity gradually decreased even at 30 μmol photons m −2  s −1 and could not be detected at 12 h. PSII inactivation was enhanced by higher illumination. Using Cm-treated cells, the conversion of PSII dimer to monomers was observed by blue native PAGE. The rate of PSII monomerization was very similar to that of the decrease in oxygen-evolving activity under both light conditions. Immunological detection of D1 protein in the Cm-treated cells showed that the rate of D1 degradation was slower than that of the former two events, although it was more rapid than that observed in other oxyphototrophs. Thus, the three accelerated events, especially PSII monomerization, appear to cause the unusually high rate of PSII turnover in diatoms.
doi_str_mv 10.1007/s11120-016-0226-1
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however, its molecular mechanisms are largely unknown. In this study, we examined the photodamage and repair processes of PSII in the marine centric diatom Chaetoceros gracilis incubated at 30 or 300 μmol photons m −2  s −1 in the presence of a de novo protein-synthesis inhibitor. When de novo protein synthesis was blocked by chloramphenicol (Cm), oxygen-evolving activity gradually decreased even at 30 μmol photons m −2  s −1 and could not be detected at 12 h. PSII inactivation was enhanced by higher illumination. Using Cm-treated cells, the conversion of PSII dimer to monomers was observed by blue native PAGE. The rate of PSII monomerization was very similar to that of the decrease in oxygen-evolving activity under both light conditions. Immunological detection of D1 protein in the Cm-treated cells showed that the rate of D1 degradation was slower than that of the former two events, although it was more rapid than that observed in other oxyphototrophs. Thus, the three accelerated events, especially PSII monomerization, appear to cause the unusually high rate of PSII turnover in diatoms.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>26846772</pmid><doi>10.1007/s11120-016-0226-1</doi><tpages>9</tpages></addata></record>
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subjects Algae
Bacillariophyceae
Biochemistry
Biomedical and Life Sciences
Chaetoceros gracilis
Chloramphenicol - pharmacology
Diatoms - drug effects
Diatoms - metabolism
Diatoms - radiation effects
Electrophoresis, Polyacrylamide Gel
Life Sciences
Light
Original Article
Oxygen - metabolism
Photodegradation
Photons
Photosystem II Protein Complex - drug effects
Photosystem II Protein Complex - metabolism
Photosystem II Protein Complex - radiation effects
Plant Genetics and Genomics
Plant Physiology
Plant Sciences
Protein synthesis
title Conversion of photosystem II dimer to monomers during photoinhibition is tightly coupled with decrease in oxygen-evolving activity in the diatom Chaetoceros gracilis
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