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

Hiroshi Yamatani, Kaori Kohzuma, Michiharu Nakano, Tsuneaki Takami, Yusuke Kato, Yoriko Hayashi, Yuki Monden, Yutaka Okumoto, Tomoko Abe, Toshihiro Kumamaru, Ayumi Tanaka, Wataru Sakamoto, Makoto Kusaba

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)1027-1035
Number of pages9
JournalJournal of Experimental Botany
Volume69
Issue number5
DOIs
Publication statusPublished - Feb 23 2018

Fingerprint

light harvesting complex
Chlorophyll
Phenotype
chlorophyll
Light
phenotype
rice
mutants
leaves
Chlorophyll Binding Proteins
Native Polyacrylamide Gel Electrophoresis
Photosynthesis
amino acid substitution
Amino Acid Substitution
Biomass
Organism Cloning
molecular cloning
Carbon
pigments
Oryza

Keywords

  • Chlorophyll
  • Lhca4
  • light-harvesting complex
  • long-term acclimation
  • rice
  • state transition
  • stay-green

ASJC Scopus subject areas

  • Physiology
  • Plant Science

Cite this

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

In: Journal of Experimental Botany, Vol. 69, No. 5, 23.02.2018, p. 1027-1035.

Research output: Contribution to journalArticle

Yamatani, H, Kohzuma, K, Nakano, M, Takami, T, Kato, Y, Hayashi, Y, Monden, Y, Okumoto, Y, Abe, T, Kumamaru, T, Tanaka, A, Sakamoto, W & Kusaba, M 2018, 'Impairment of Lhca4, a subunit of LHCI, causes high accumulation of chlorophyll and the stay-green phenotype in rice', Journal of Experimental Botany, vol. 69, no. 5, pp. 1027-1035. https://doi.org/10.1093/jxb/erx468
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. / Impairment of Lhca4, a subunit of LHCI, causes high accumulation of chlorophyll and the stay-green phenotype in rice. In: Journal of Experimental Botany. 2018 ; Vol. 69, No. 5. pp. 1027-1035.
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AU - Kohzuma, Kaori

AU - Nakano, Michiharu

AU - Takami, Tsuneaki

AU - Kato, Yusuke

AU - Hayashi, Yoriko

AU - Monden, Yuki

AU - Okumoto, Yutaka

AU - Abe, Tomoko

AU - Kumamaru, Toshihiro

AU - Tanaka, Ayumi

AU - Sakamoto, Wataru

AU - Kusaba, Makoto

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N2 - 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.

AB - 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.

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