Phosphorylation and nitration levels of photosynthetic proteins are conversely regulated by light stress

Dmitry Galetskiy, Jens N. Lohscheider, Alexey S. Kononikhin, Igor A. Popov, Eugene N. Nikolaev, Iwona Adamska

Research output: Contribution to journalArticlepeer-review

33 Citations (Scopus)

Abstract

Using a label-free mass spectrometric approach, we investigated light-induced changes in the distribution of phosphorylated and nitrated proteins within subpopulations of native photosynthetic complexes in the thylakoid membrane of Arabidopsis thaliana leaves adapted to growth light (GL) and subsequently exposed to high light (HL). Eight protein phosphorylation sites were identified in photosystem II (PSII) and the phosphorylation level of seven was regulated by HL as determined based on peak areas from ion chromatograms of phosphorylated and non-phosphorylated peptides. Although the phosphorylation of PSII proteins was reported in the past, we demonstrated for the first time that two minor antenna LHCB4 isoforms are alternately phosphorylated under GL and HL conditions in PSII monomers, dimers and supercomplexes. A role of LHCB4 phosphorylation in state transition and monomerization of PSII under HL conditions is proposed. We determined changes in the nitration level of 23 tyrosine residues in five photosystem I (PSI) and nine PSII proteins and demonstrated for the majority of them a lower nitration level in PSI and PSII complexes and supercomplexes under HL conditions, as compared to GL. In contrast, the nitration level significantly increased in assembled/disassembled PSI and PSII subcomplexes under HL conditions. A possible role of nitration in (1) monomerization of LHCB1-3 trimers under HL conditions (2) binding properties of ferredoxin-NADP+ oxidoreductase to photosystem I, and (3) PSII photodamage and repair cycle, is discussed. Based on these data, we propose that the conversely regulated phosphorylation and nitration levels regulate the stability and turnover of photosynthetic complexes under HL conditions.

Original languageEnglish
Pages (from-to)461-473
Number of pages13
JournalPlant Molecular Biology
Volume77
Issue number4-5
DOIs
Publication statusPublished - Nov 2011
Externally publishedYes

Keywords

  • Light stress
  • Mass spectrometry
  • Photosystem II complex
  • Post-translational protein modification

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