Structural adaptation of the plant protease Deg1 to repair photosystem II during light exposure
Deg1 is a chloroplastic protease involved in maintaining the photosynthetic machinery. Structural and biochemical analyses reveal that the inactive Deg1 monomer is transformed into the proteolytically active hexamer at acidic pH. The change in pH is sensed by His244, which upon protonation, repositi...
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Published in | Nature structural & molecular biology Vol. 18; no. 6; pp. 728 - 731 |
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Main Authors | , , , , , , , , , |
Format | Journal Article |
Language | English |
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01.06.2011
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Abstract | Deg1 is a chloroplastic protease involved in maintaining the photosynthetic machinery. Structural and biochemical analyses reveal that the inactive Deg1 monomer is transformed into the proteolytically active hexamer at acidic pH. The change in pH is sensed by His244, which upon protonation, repositions a specific helix to trigger oligomerization. This system ensures selective activation of Deg1 during daylight, when acidification of the thylakoid lumen occurs and photosynthetic proteins are damaged. |
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AbstractList | Deg1 is a chloroplastic protease involved in maintaining the photosynthetic machinery. Structural and biochemical analyses reveal that the inactive Deg1 monomer is transformed into the proteolytically active hexamer at acidic pH. The change in pH is sensed by His244, which upon protonation, repositions a specific helix to trigger oligomerization. This system ensures selective activation of Deg1 during daylight, when acidification of the thylakoid lumen occurs and photosynthetic proteins are damaged. Deg1 is an HtrA protease that participates in the turnover of the photosynthetic proteins in chloroplasts. Now the crystal structure of Deg1, along with functional work, reveals that Deg1 oligomerization and activation occur in response to acidic pH, which should be encountered in the thylakoid lumen when exposed to light. Deg1 is a chloroplastic protease involved in maintaining the photosynthetic machinery. Structural and biochemical analyses reveal that the inactive Deg1 monomer is transformed into the proteolytically active hexamer at acidic pH. The change in pH is sensed by His244, which upon protonation, repositions a specific helix to trigger oligomerization. This system ensures selective activation of Deg1 during daylight, when acidification of the thylakoid lumen occurs and photosynthetic proteins are damaged. Deg1 is a chloroplastic protease involved in maintaining the photosynthetic machinery. Structural and biochemical analyses reveal that the inactive Deg1 monomer is transformed into the proteolytically active hexamer at acidic pH. The change in pH is sensed by His244, which upon protonation, repositions a specific helix to trigger oligomerization. This system ensures selective activation of Deg1 during daylight, when acidification of the thylakoid lumen occurs and photosynthetic proteins are damaged. [PUBLICATION ABSTRACT] |
Author | Boyanov, Boril Kley, Juliane Naveh, Leah Adam, Zach Clausen, Tim Knopf, Ronit R Schmidt, Bastian Stolt-Bergner, Peggy C Ehrmann, Michael Kirk, Rebecca |
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BackLink | https://www.ncbi.nlm.nih.gov/pubmed/21532594$$D View this record in MEDLINE/PubMed |
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Snippet | Deg1 is a chloroplastic protease involved in maintaining the photosynthetic machinery. Structural and biochemical analyses reveal that the inactive Deg1... Deg1 is an HtrA protease that participates in the turnover of the photosynthetic proteins in chloroplasts. Now the crystal structure of Deg1, along with... |
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SubjectTerms | 631/337/474 631/449/2675 631/45/535 Acidification Arabidopsis - enzymology Arabidopsis - radiation effects Arabidopsis Proteins - chemistry Arabidopsis Proteins - metabolism Biochemistry Biological Microscopy Biomedical and Life Sciences brief-communication Crystal structure Crystallography, X-Ray Hydrogen-Ion Concentration Life Sciences Light Membrane Biology Models, Biological Models, Molecular Molecular biology Photosynthesis Photosystem II Protein Complex - metabolism Plant biology Proteases Protein Conformation Protein Multimerization Protein Structure Protein Structure, Quaternary Protein Structure, Tertiary Serine Endopeptidases - chemistry Serine Endopeptidases - metabolism |
Title | Structural adaptation of the plant protease Deg1 to repair photosystem II during light exposure |
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