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Impairment of Lhca4, a subunit of LHCI, causes high accumulation of chlorophyll and the stay-green phenotype in rice

Chlorophyll is an essential molecule for acquiring light energy during photosynthesis. Mutations that result in chlorophyll retention during leaf senescence are called ‘stay-green’ mutants. One of the several types of stay-green mutants, Type E, accumulates high levels of chlorophyll in the pre-sene...

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Detalles Bibliográficos
Autores principales: Yamatani, Hiroshi, Kohzuma, Kaori, Nakano, Michiharu, Takami, Tsuneaki, Kato, Yusuke, Hayashi, Yoriko, Monden, Yuki, Okumoto, Yutaka, Abe, Tomoko, Kumamaru, Toshihiro, Tanaka, Ayumi, Sakamoto, Wataru, Kusaba, Makoto
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6019047/
https://www.ncbi.nlm.nih.gov/pubmed/29304198
http://dx.doi.org/10.1093/jxb/erx468
Descripción
Sumario:Chlorophyll is an essential molecule for acquiring light energy during photosynthesis. Mutations that result in chlorophyll retention during leaf senescence are called ‘stay-green’ mutants. One of the several types of stay-green mutants, Type E, accumulates high levels of chlorophyll in the pre-senescent leaves, resulting in delayed yellowing. We isolated delayed yellowing1-1 (dye1-1), a rice mutant whose yellowing is delayed in the field. dye1-1 accumulated more chlorophyll than the wild-type in the pre-senescent and senescent leaves, but did not retain leaf functionality in the ‘senescent green leaves’, suggesting that dye1-1 is a Type E stay-green mutant. Positional cloning revealed that DYE1 encodes Lhca4, a subunit of the light-harvesting complex I (LHCI). In dye1-1, amino acid substitution occurs at the location of a highly conserved amino acid residue involved in pigment binding; indeed, a severely impaired structure of the PSI-LHCI super-complex in dye1-1 was observed in a blue native PAGE analysis. Nevertheless, the biomass and carbon assimilation rate of dye1-1 were comparable to those in the wild-type. Interestingly, Lhcb1, a trimeric LHCII protein, was highly accumulated in dye1-1, in the chlorophyll–protein complexes. The high accumulation of LHCII in the LHCI mutant dye1 suggests a novel functional interaction between LHCI and LHCII.