Cell growth defect factor1/CHAPERONE-LIKE PROTEIN OF POR1 plays a role in stabilization of light-dependent protochlorophyllide oxidoreductase in Nicotiana benthamiana and Arabidopsis

Jae Yong Lee, Ho Seok Lee, Ji Young Song, Young Jun Jung, Steffen Reinbothe, Youn Il Park, Sang Yeol Lee, Hyun Sook Pai

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Angiosperms require light for chlorophyll biosynthesis because one reaction in the pathway, the reduction of protochlorophyllide (Pchlide) to chlorophyllide, is catalyzed by the light-dependent protochlorophyllide oxidoreductase (POR). Here, we report that Cell growth defect factor1 (Cdf1), renamed here as CHAPERONE-LIKE PROTEIN OF POR1 (CPP1), an essential protein for chloroplast development, plays a role in the regulation of POR stability and function. Cdf1/CPP1 contains a J-like domain and three transmembrane domains, is localized in the thylakoid and envelope membranes, and interacts with POR isoforms in chloroplasts. CPP1 can stabilize POR proteins with its holdase chaperone activity. CPP1 deficiency results in diminished POR protein accumulation and defective chlorophyll synthesis, leading to photobleaching and growth inhibition of plants under light conditions. CPP1 depletion also causes reduced POR accumulation in etioplasts of dark-grown plants and as a result impairs the formation of prolamellar bodies, which subsequently affects chloroplast biogenesis upon illumination. Furthermore, in cyanobacteria, the CPP1 homolog critically regulates POR accumulation and chlorophyll synthesis under high-light conditions, in which the dark-operative Pchlide oxidoreductase is repressed by its oxygen sensitivity. These findings and the ubiquitous presence of CPP1 in oxygenic photosynthetic organisms suggest the conserved nature of CPP1 function in the regulation of POR.

Original languageEnglish
Pages (from-to)3944-3960
Number of pages17
JournalPlant Cell
Volume25
Issue number10
DOIs
Publication statusPublished - 2013 Oct 1

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Protochlorophyllide
protochlorophyllides
Nicotiana benthamiana
oxidoreductases
Arabidopsis
Tobacco
cell growth
Oxidoreductases
Light
Growth
Proteins
proteins
Chloroplasts
Chlorophyll
chloroplasts
chlorophyll
Chlorophyllides
Chloroplast Proteins
etioplasts
chlorophyllides

All Science Journal Classification (ASJC) codes

  • Plant Science
  • Cell Biology

Cite this

Lee, Jae Yong ; Lee, Ho Seok ; Song, Ji Young ; Jung, Young Jun ; Reinbothe, Steffen ; Park, Youn Il ; Lee, Sang Yeol ; Pai, Hyun Sook. / Cell growth defect factor1/CHAPERONE-LIKE PROTEIN OF POR1 plays a role in stabilization of light-dependent protochlorophyllide oxidoreductase in Nicotiana benthamiana and Arabidopsis. In: Plant Cell. 2013 ; Vol. 25, No. 10. pp. 3944-3960.
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abstract = "Angiosperms require light for chlorophyll biosynthesis because one reaction in the pathway, the reduction of protochlorophyllide (Pchlide) to chlorophyllide, is catalyzed by the light-dependent protochlorophyllide oxidoreductase (POR). Here, we report that Cell growth defect factor1 (Cdf1), renamed here as CHAPERONE-LIKE PROTEIN OF POR1 (CPP1), an essential protein for chloroplast development, plays a role in the regulation of POR stability and function. Cdf1/CPP1 contains a J-like domain and three transmembrane domains, is localized in the thylakoid and envelope membranes, and interacts with POR isoforms in chloroplasts. CPP1 can stabilize POR proteins with its holdase chaperone activity. CPP1 deficiency results in diminished POR protein accumulation and defective chlorophyll synthesis, leading to photobleaching and growth inhibition of plants under light conditions. CPP1 depletion also causes reduced POR accumulation in etioplasts of dark-grown plants and as a result impairs the formation of prolamellar bodies, which subsequently affects chloroplast biogenesis upon illumination. Furthermore, in cyanobacteria, the CPP1 homolog critically regulates POR accumulation and chlorophyll synthesis under high-light conditions, in which the dark-operative Pchlide oxidoreductase is repressed by its oxygen sensitivity. These findings and the ubiquitous presence of CPP1 in oxygenic photosynthetic organisms suggest the conserved nature of CPP1 function in the regulation of POR.",
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Cell growth defect factor1/CHAPERONE-LIKE PROTEIN OF POR1 plays a role in stabilization of light-dependent protochlorophyllide oxidoreductase in Nicotiana benthamiana and Arabidopsis. / Lee, Jae Yong; Lee, Ho Seok; Song, Ji Young; Jung, Young Jun; Reinbothe, Steffen; Park, Youn Il; Lee, Sang Yeol; Pai, Hyun Sook.

In: Plant Cell, Vol. 25, No. 10, 01.10.2013, p. 3944-3960.

Research output: Contribution to journalArticle

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AU - Lee, Jae Yong

AU - Lee, Ho Seok

AU - Song, Ji Young

AU - Jung, Young Jun

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AU - Pai, Hyun Sook

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AB - Angiosperms require light for chlorophyll biosynthesis because one reaction in the pathway, the reduction of protochlorophyllide (Pchlide) to chlorophyllide, is catalyzed by the light-dependent protochlorophyllide oxidoreductase (POR). Here, we report that Cell growth defect factor1 (Cdf1), renamed here as CHAPERONE-LIKE PROTEIN OF POR1 (CPP1), an essential protein for chloroplast development, plays a role in the regulation of POR stability and function. Cdf1/CPP1 contains a J-like domain and three transmembrane domains, is localized in the thylakoid and envelope membranes, and interacts with POR isoforms in chloroplasts. CPP1 can stabilize POR proteins with its holdase chaperone activity. CPP1 deficiency results in diminished POR protein accumulation and defective chlorophyll synthesis, leading to photobleaching and growth inhibition of plants under light conditions. CPP1 depletion also causes reduced POR accumulation in etioplasts of dark-grown plants and as a result impairs the formation of prolamellar bodies, which subsequently affects chloroplast biogenesis upon illumination. Furthermore, in cyanobacteria, the CPP1 homolog critically regulates POR accumulation and chlorophyll synthesis under high-light conditions, in which the dark-operative Pchlide oxidoreductase is repressed by its oxygen sensitivity. These findings and the ubiquitous presence of CPP1 in oxygenic photosynthetic organisms suggest the conserved nature of CPP1 function in the regulation of POR.

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