Long-term acclimation of the cyanobacterium Synechocystis sp. PCC 6803 to high light is accompanied by an enhanced production of chlorophyll that is preferentially channeled to trimeric photosystem I
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
23037506
PubMed Central
PMC3510144
DOI
10.1104/pp.112.207274
PII: pp.112.207274
Knihovny.cz E-zdroje
- MeSH
- aklimatizace účinky záření MeSH
- bakteriální proteiny metabolismus MeSH
- biosyntetické dráhy účinky záření MeSH
- časové faktory MeSH
- chlorofyl biosyntéza MeSH
- fotosystém I (proteinový komplex) metabolismus MeSH
- fotosystém II (proteinový komplex) metabolismus MeSH
- izotopy uhlíku MeSH
- spektrální analýza MeSH
- světlo * MeSH
- Synechocystis cytologie fyziologie účinky záření ultrastruktura MeSH
- up regulace genetika účinky záření MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- bakteriální proteiny MeSH
- chlorofyl MeSH
- fotosystém I (proteinový komplex) MeSH
- fotosystém II (proteinový komplex) MeSH
- izotopy uhlíku MeSH
Cyanobacteria acclimate to high-light conditions by adjusting photosystem stoichiometry through a decrease of photosystem I (PSI) abundance in thylakoid membranes. As PSI complexes bind the majority of chlorophyll (Chl) in cyanobacterial cells, it is accepted that the mechanism controlling PSI level/synthesis is tightly associated with the Chl biosynthetic pathway. However, how Chl is distributed to photosystems under different light conditions remains unknown. Using radioactive labeling by (35)S and by (14)C combined with native/two-dimensional electrophoresis, we assessed the synthesis and accumulation of photosynthetic complexes in parallel with the synthesis of Chl in Synechocystis sp. PCC 6803 cells acclimated to different light intensities. Although cells acclimated to higher irradiances (150 and 300 μE m(-2)s(-1)) exhibited markedly reduced PSI content when compared with cells grown at lower irradiances (10 and 40 μE m(-2) s(-1)), they grew much faster and synthesized significantly more Chl, as well as both photosystems. Interestingly, even under high irradiance, almost all labeled de novo Chl was localized in the trimeric PSI, whereas only a weak Chl labeling in photosystem II (PSII) was accompanied by the intensive (35)S protein labeling, which was much stronger than in PSI. These results suggest that PSII subunits are mostly synthesized using recycled Chl molecules previously released during PSII repair-driven protein degradation. In contrast, most of the fresh Chl is utilized for synthesis of PSI complexes likely to maintain a constant level of PSI during cell proliferation.
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