Disturbed excitation energy transfer in Arabidopsis thaliana mutants lacking minor antenna complexes of photosystem II

L. Dall'Osto, C. Ünlü, S. Cazzaniga, H. van Amerongen

Research output: Contribution to journalArticleAcademicpeer-review

23 Citations (Scopus)

Abstract

Minor light-harvesting complexes (Lhcs) CP24, CP26 and CP29 occupy a position in photosystem II (PSII) of plants between the major light-harvesting complexes LHCII and the PSII core subunits. Lack of minor Lhcs in vivo causes impairment of PSII organization, and negatively affects electron transport rates and photoprotection capacity. Here we used picosecond-fluorescence spectroscopy to study excitation-energy transfer (EET) in thylakoid membranes isolated from Arabidopsis thaliana wild-type plants and knockout lines depleted of either two (koCP26/24 and koCP29/24) or all minor Lhcs (NoM). In the absence of all minor Lhcs, the functional connection of LHCII to the PSII cores appears to be seriously impairedwhereas the “disconnected” LHCII is substantially quenched. For both double knock-out mutants, excitation trapping in PSII is faster than in NoM thylakoids but slower than in WT thylakoids. In NoM thylakoids, the loss of all minor Lhcs is accompanied by an over-accumulation of LHCII, suggesting a compensating response to the reduced trapping efficiency in limiting light,which leads to a photosynthetic phenotype resembling that of low-light-acclimated plants. Finally, fluorescence kinetics and biochemical results show that the missing minor complexes are not replaced by other Lhcs, implying that they are unique among the antenna subunits and crucial for the functioning and macroorganization of PSII.
Original languageEnglish
Pages (from-to)1981-1988
JournalBiochimica et Biophysica Acta. B, Bioenergetics
Volume1837
Issue number12
DOIs
Publication statusPublished - 2014

Keywords

  • light-harvesting-complex
  • primary charge separation
  • chlamydomonas-reinhardtii
  • thylakoid membrane
  • electron-transport
  • crystal-structure
  • green plants
  • redox state
  • wild-type
  • proteins

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