Journal
PLANT AND CELL PHYSIOLOGY
Volume 58, Issue 11, Pages 2026-2039Publisher
OXFORD UNIV PRESS
DOI: 10.1093/pcp/pcx124
Keywords
Arabidopsis; Light harvesting; Thylakoids
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Funding
- Japan Science and Technology Agency [the CREST] [JPMJCR11B2]
- Japan Society for the Promotion of Science [KAKENHI] [16H06554, 17K07431, 16H06553]
- Grants-in-Aid for Scientific Research [17K07431, 17K19420, 16H06554, 15H04381, 17K07691] Funding Source: KAKEN
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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.
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