Details
| Original language | English |
|---|---|
| Pages (from-to) | 732-45 |
| Number of pages | 14 |
| Journal | Plant physiology |
| Volume | 163 |
| Issue number | 2 |
| Publication status | Published - Oct 2013 |
Abstract
Excess light can have a negative impact on photosynthesis; thus, plants have evolved many different ways to adapt to different light conditions to both optimize energy use and avoid damage caused by excess light. Analysis of the Arabidopsis (Arabidopsis thaliana) mutant snowy cotyledon4 (sco4) revealed a mutation in a chloroplast-targeted protein that shares limited homology with CaaX-type endopeptidases. The SCO4 protein possesses an important function in photosynthesis and development, with point mutations rendering the seedlings and adult plants susceptible to photooxidative stress. The sco4 mutation impairs the acclimation of chloroplasts and their photosystems to excess light, evidenced in a reduction in photosystem I function, decreased linear electron transfer, yet increased nonphotochemical quenching. SCO4 is localized to the chloroplasts, which suggests the existence of an unreported type of protein modification within this organelle. Phylogenetic and yeast complementation analyses of SCO4-like proteins reveal that SCO4 is a member of an unknown group of higher plant-specific proteinases quite distinct from the well-described CaaX-type endopeptidases RAS Converting Enzyme1 (RCE1) and zinc metallopeptidase STE24 and lacks canonical CaaX activity. Therefore, we hypothesize that SCO4 is a novel endopeptidase required for critical protein modifications within chloroplasts, influencing the function of proteins involved in photosynthesis required for tolerance to excess light.
Keywords
- Acclimatization/radiation effects, Amino Acid Motifs, Arabidopsis/enzymology, Arabidopsis Proteins/metabolism, Chloroplasts/enzymology, Conserved Sequence, Ecotype, Electron Transport/radiation effects, Hydrogen Peroxide/metabolism, Light, Metalloendopeptidases/metabolism, Mutation/genetics, Peptide Hydrolases/metabolism, Phenotype, Photobleaching/radiation effects, Photosynthesis/radiation effects, Photosystem I Protein Complex/metabolism, Photosystem II Protein Complex/metabolism, Phylogeny, Plant Leaves/physiology, Protein Transport/radiation effects, Seedlings/growth & development, Spectrometry, Fluorescence, Time Factors
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In: Plant physiology, Vol. 163, No. 2, 10.2013, p. 732-45.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - A novel proteinase, SNOWY COTYLEDON4, is required for photosynthetic acclimation to higher light intensities in Arabidopsis
AU - Albrecht-Borth, Verónica
AU - Kauss, Dominika
AU - Fan, Dayong
AU - Hu, Yuanyuan
AU - Collinge, Derek
AU - Marri, Shashikanth
AU - Liebers, Monique
AU - Apel, Klaus
AU - Pfannschmidt, Thomas
AU - Chow, Wah S
AU - Pogson, Barry J
PY - 2013/10
Y1 - 2013/10
N2 - Excess light can have a negative impact on photosynthesis; thus, plants have evolved many different ways to adapt to different light conditions to both optimize energy use and avoid damage caused by excess light. Analysis of the Arabidopsis (Arabidopsis thaliana) mutant snowy cotyledon4 (sco4) revealed a mutation in a chloroplast-targeted protein that shares limited homology with CaaX-type endopeptidases. The SCO4 protein possesses an important function in photosynthesis and development, with point mutations rendering the seedlings and adult plants susceptible to photooxidative stress. The sco4 mutation impairs the acclimation of chloroplasts and their photosystems to excess light, evidenced in a reduction in photosystem I function, decreased linear electron transfer, yet increased nonphotochemical quenching. SCO4 is localized to the chloroplasts, which suggests the existence of an unreported type of protein modification within this organelle. Phylogenetic and yeast complementation analyses of SCO4-like proteins reveal that SCO4 is a member of an unknown group of higher plant-specific proteinases quite distinct from the well-described CaaX-type endopeptidases RAS Converting Enzyme1 (RCE1) and zinc metallopeptidase STE24 and lacks canonical CaaX activity. Therefore, we hypothesize that SCO4 is a novel endopeptidase required for critical protein modifications within chloroplasts, influencing the function of proteins involved in photosynthesis required for tolerance to excess light.
AB - Excess light can have a negative impact on photosynthesis; thus, plants have evolved many different ways to adapt to different light conditions to both optimize energy use and avoid damage caused by excess light. Analysis of the Arabidopsis (Arabidopsis thaliana) mutant snowy cotyledon4 (sco4) revealed a mutation in a chloroplast-targeted protein that shares limited homology with CaaX-type endopeptidases. The SCO4 protein possesses an important function in photosynthesis and development, with point mutations rendering the seedlings and adult plants susceptible to photooxidative stress. The sco4 mutation impairs the acclimation of chloroplasts and their photosystems to excess light, evidenced in a reduction in photosystem I function, decreased linear electron transfer, yet increased nonphotochemical quenching. SCO4 is localized to the chloroplasts, which suggests the existence of an unreported type of protein modification within this organelle. Phylogenetic and yeast complementation analyses of SCO4-like proteins reveal that SCO4 is a member of an unknown group of higher plant-specific proteinases quite distinct from the well-described CaaX-type endopeptidases RAS Converting Enzyme1 (RCE1) and zinc metallopeptidase STE24 and lacks canonical CaaX activity. Therefore, we hypothesize that SCO4 is a novel endopeptidase required for critical protein modifications within chloroplasts, influencing the function of proteins involved in photosynthesis required for tolerance to excess light.
KW - Acclimatization/radiation effects
KW - Amino Acid Motifs
KW - Arabidopsis/enzymology
KW - Arabidopsis Proteins/metabolism
KW - Chloroplasts/enzymology
KW - Conserved Sequence
KW - Ecotype
KW - Electron Transport/radiation effects
KW - Hydrogen Peroxide/metabolism
KW - Light
KW - Metalloendopeptidases/metabolism
KW - Mutation/genetics
KW - Peptide Hydrolases/metabolism
KW - Phenotype
KW - Photobleaching/radiation effects
KW - Photosynthesis/radiation effects
KW - Photosystem I Protein Complex/metabolism
KW - Photosystem II Protein Complex/metabolism
KW - Phylogeny
KW - Plant Leaves/physiology
KW - Protein Transport/radiation effects
KW - Seedlings/growth & development
KW - Spectrometry, Fluorescence
KW - Time Factors
U2 - 10.1104/pp.113.216036
DO - 10.1104/pp.113.216036
M3 - Article
C2 - 23940253
VL - 163
SP - 732
EP - 745
JO - Plant physiology
JF - Plant physiology
SN - 0032-0889
IS - 2
ER -