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 inNature structural & molecular biology Vol. 18; no. 6; pp. 728 - 731
Main Authors Adam, Zach, Clausen, Tim, Kley, Juliane, Schmidt, Bastian, Boyanov, Boril, Stolt-Bergner, Peggy C, Kirk, Rebecca, Ehrmann, Michael, Knopf, Ronit R, Naveh, Leah
Format Journal Article
LanguageEnglish
Published New York Nature Publishing Group US 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.
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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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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pubmed
springer
nature
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Index Database
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StartPage 728
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
URI http://dx.doi.org/10.1038/nsmb.2055
https://link.springer.com/article/10.1038/nsmb.2055
https://www.ncbi.nlm.nih.gov/pubmed/21532594
https://www.proquest.com/docview/871563764
https://search.proquest.com/docview/870552816
Volume 18
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