Deficiency of the Stroma-Lamellar Protein LIL8/PSB33 Affects Energy Transfer Around PSI in Arabidopsis.

Abstract

Light-harvesting-like (LIL) proteins are a group of proteins that share a consensus amino acid sequence with light-harvesting Chl-binding (LHC) proteins. We hypothesized that they might be involved in photosynthesis-related processes. In order to gain a better understanding of a potential role in photosynthesis-related processes, we examined the most recently identified LIL protein, LIL8/PSB33. Recently, it was suggested that this protein is an auxiliary PSII core protein which is involved in organization of the PSII supercomplex. However, we found that the majority of LIL8/PSB33 was localized in stroma lamellae, where PSI is predominant. Moreover, the PSI antenna sizes measured under visible light were slightly increased in the lil8 mutants which lack LIL8/PSB33 protein. Analysis of fluorescence decay kinetics and fluorescence decay-associated spectra indicated that energy transfer to quenching sites within PSI was partially hampered in these mutants. On the other hand, analysis of the steady-state fluorescence spectra in these mutants indicates that a population of LHCII is energetically disconnected from PSII. Taken together, we suggest that LIL8/PSB33 is involved in the fine-tuning of light harvesting and/or energy transfer around both photosystems.