Publikation: Deg/HtrA proteases as components of a network for photosystem II quality control in chloroplasts and cyanobacteria
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2009
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Research in Microbiology. 2009, 160(9), pp. 726-732. ISSN 0923-2508. eISSN 1769-7123. Available under: doi: 10.1016/j.resmic.2009.08.005
Zusammenfassung
Organisms that perform oxygenic photosynthesis are subjected to photoinhibition of their photosynthetic function when exposed to excessive illumination. The main target of photoinhibition is the D1 protein in the reaction center of the photosystem II complex. Rapid degradation of photodamaged D1 protein and its replacement by a de novo synthesized functional copy represent an important repair mechanism crucial for cell survival under light stress conditions. This review summarizes the literature on the ATP-independent Deg/HtrA family of serine endopeptidases in cyanobacteria and chloroplasts of higher plants, and discusses their role in D1 protein degradation. We propose that Deg/HtrA proteases are part of a larger network of enzymes that ensure protein quality control, including photosystem II, in plants and cyanobacteria.
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570 Biowissenschaften, Biologie
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Deg/HtrA protease, Chloroplast, Photosystem II, Synechocystis 6803
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HUESGEN, Pitter Florian, Holger SCHUHMANN, Iwona ADAMSKA, 2009. Deg/HtrA proteases as components of a network for photosystem II quality control in chloroplasts and cyanobacteria. In: Research in Microbiology. 2009, 160(9), pp. 726-732. ISSN 0923-2508. eISSN 1769-7123. Available under: doi: 10.1016/j.resmic.2009.08.005BibTex
@article{Huesgen2009DegHt-1128,
year={2009},
doi={10.1016/j.resmic.2009.08.005},
title={Deg/HtrA proteases as components of a network for photosystem II quality control in chloroplasts and cyanobacteria},
number={9},
volume={160},
issn={0923-2508},
journal={Research in Microbiology},
pages={726--732},
author={Huesgen, Pitter Florian and Schuhmann, Holger and Adamska, Iwona}
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<dcterms:abstract xml:lang="eng">Organisms that perform oxygenic photosynthesis are subjected to photoinhibition of their photosynthetic function when exposed to excessive illumination. The main target of photoinhibition is the D1 protein in the reaction center of the photosystem II complex. Rapid degradation of photodamaged D1 protein and its replacement by a de novo synthesized functional copy represent an important repair mechanism crucial for cell survival under light stress conditions. This review summarizes the literature on the ATP-independent Deg/HtrA family of serine endopeptidases in cyanobacteria and chloroplasts of higher plants, and discusses their role in D1 protein degradation. We propose that Deg/HtrA proteases are part of a larger network of enzymes that ensure protein quality control, including photosystem II, in plants and cyanobacteria.</dcterms:abstract>
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