| Autor: |
Levin, Guy, Yasmin, Michael, Pieńko, Tomasz, Yehishalom, Nitsan, Hanna, Rawad, Kleifeld, Oded, Glaser, Fabian, Schuster, Gadi |
| Předmět: |
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| Zdroj: |
New Phytologist; Apr2024, Vol. 242 Issue 2, p544-557, 14p |
| Abstrakt: |
Summary: The phosphorylation of photosystem II (PSII) and its antenna (LHCII) proteins has been studied, and its involvement in state transitions and PSII repair is known. Yet, little is known about the phosphorylation of photosystem I (PSI) and its antenna (LHCI) proteins.Here, we applied proteomics analysis to generate a map of the phosphorylation sites of the PSI–LHCI proteins in Chlorella ohadii cells that were grown under low or extreme high‐light intensities (LL and HL). Furthermore, we analyzed the content of oxidized tryptophans and PSI–LHCI protein degradation products in these cells, to estimate the light‐induced damage to PSI–LHCI.Our work revealed the phosphorylation of 17 of 22 PSI–LHCI subunits. The analyses detected the extensive phosphorylation of the LHCI subunits Lhca6 and Lhca7, which is modulated by growth light intensity. Other PSI–LHCI subunits were phosphorylated to a lesser extent, including PsaE, where molecular dynamic simulation proposed that a phosphoserine stabilizes ferredoxin binding. Additionally, we show that HL‐grown cells accumulate less oxidative damage and degradation products of PSI–LHCI proteins, compared with LL‐grown cells.The significant phosphorylation of Lhca6 and Lhca7 at the interface with other LHCI subunits suggests a physiological role during photosynthesis, possibly by altering light‐harvesting characteristics and binding of other subunits. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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