Degradation of the main Photosystem II light-harvesting complex. García-Lorenzo, M., Żelisko, A., Jackowski, G., & Funk, C. Photochemical & Photobiological Sciences, 4(12):1065–1071, November, 2005. Publisher: The Royal Society of Chemistry![Degradation of the main Photosystem II light-harvesting complex [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex Many factors trigger the degradation of proteins, including changes in environmental conditions, genetic mutations, and limitations in the availability of cofactors. Despite the importance for viability, still very little is known about protein degradation and its regulation. The degradation of the most abundant membrane protein on Earth, the light-harvesting complex of Photosystem II (LHC II), is highly regulated under different environmental conditions, e.g. light stress, to prevent photochemical damage of the reaction center. However, despite major effort to identify the protease/proteases involved in the degradation of the apoproteins of LHC II the molecular details of this important process remain obscure. LHC II belongs to the family of chlorophyll a/b binding proteins (CAB proteins) and is located in the thylakoid membrane of the plant chloroplast. The results of biochemical experiments to isolate and characterize the protease degrading LHC II are summarized here and compared to our own recent finding indicating that a metalloprotease of the FtsH family is involved in this process.
@article{garcia-lorenzo_degradation_2005,
title = {Degradation of the main {Photosystem} {II} light-harvesting complex},
volume = {4},
issn = {1474-9092},
url = {https://pubs.rsc.org/en/content/articlelanding/2005/pp/b506625e},
doi = {10.1039/B506625E},
abstract = {Many factors trigger the degradation of proteins, including changes in environmental conditions, genetic mutations, and limitations in the availability of cofactors. Despite the importance for viability, still very little is known about protein degradation and its regulation. The degradation of the most abundant membrane protein on Earth, the light-harvesting complex of Photosystem II (LHC II), is highly regulated under different environmental conditions, e.g. light stress, to prevent photochemical damage of the reaction center. However, despite major effort to identify the protease/proteases involved in the degradation of the apoproteins of LHC II the molecular details of this important process remain obscure. LHC II belongs to the family of chlorophyll a/b binding proteins (CAB proteins) and is located in the thylakoid membrane of the plant chloroplast. The results of biochemical experiments to isolate and characterize the protease degrading LHC II are summarized here and compared to our own recent finding indicating that a metalloprotease of the FtsH family is involved in this process.},
language = {en},
number = {12},
urldate = {2021-06-11},
journal = {Photochemical \& Photobiological Sciences},
author = {García-Lorenzo, Maribel and Żelisko, Agnieszka and Jackowski, Grzegorz and Funk, Christiane},
month = nov,
year = {2005},
note = {Publisher: The Royal Society of Chemistry},
pages = {1065--1071},
}
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