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Low threshold levels of ultraviolet-B in a background of photosynthetically active radiation trigger rapid degradation of the D2 protein of photosystem-II
Year:
1996
Source of publication :
Plant Journal
Authors :
Gaba, Victor
;
.
Volume :
9
Co-Authors:
Jansen, M.A.K., Department of Plant Genetics, Weizmann Institute of Science, Rehovot 76100, Israel, Department of Plant Physiology, Wageningen Agricultural University, Arboretumlaan 4, 6703 BD Wageningen, Netherlands
Gaba, V., Department of Virology, ARO Volcani Centre, P.O.B. 6, Beit Dagan 50250, Israel
Greenberg, B.M., Department of Biology, University of Waterloo, Waterloo, Ont. N2L-3G1, Canada
Mattoo, A.K., Plant Molecular Biology Laboratory, USDA/ARS, Beltsville Agric. Research Centre, Beltsville, MD 20705, United States
Edelman, M., Department of Plant Genetics, Weizmann Institute of Science, Rehovot 76100, Israel
Facilitators :
From page:
693
To page:
699
(
Total pages:
7
)
Abstract:
The photosystem II reaction centre has at its core a heterodimer made up of two proteins, D1 and D2. The D1 protein is known to be rapidly degraded by photosynthetically active radiation while the D2 protein is relatively stable. This paper reports that when the aquatic higher plant, Spirodela was exposed to ultraviolet-B radiation, D2 degradation accelerated markedly and half life times approached those of the D1 protein. Moreover, in the presence of an environmentally relevant background of photosynthetically active radiation, low fluxes of ultraviolet-B (but not ultraviolet-A) radiation synergistically stimulated degradation of the D2 protein within functional reaction centres. Thus, above a critical threshold, ultraviolet-B specifically targets the D1-D2 heterodimer for accelerated degradation.
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DOI :
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
28756
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:41
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Low threshold levels of ultraviolet-B in a background of photosynthetically active radiation trigger rapid degradation of the D2 protein of photosystem-II
9
Jansen, M.A.K., Department of Plant Genetics, Weizmann Institute of Science, Rehovot 76100, Israel, Department of Plant Physiology, Wageningen Agricultural University, Arboretumlaan 4, 6703 BD Wageningen, Netherlands
Gaba, V., Department of Virology, ARO Volcani Centre, P.O.B. 6, Beit Dagan 50250, Israel
Greenberg, B.M., Department of Biology, University of Waterloo, Waterloo, Ont. N2L-3G1, Canada
Mattoo, A.K., Plant Molecular Biology Laboratory, USDA/ARS, Beltsville Agric. Research Centre, Beltsville, MD 20705, United States
Edelman, M., Department of Plant Genetics, Weizmann Institute of Science, Rehovot 76100, Israel
Low threshold levels of ultraviolet-B in a background of photosynthetically active radiation trigger rapid degradation of the D2 protein of photosystem-II
The photosystem II reaction centre has at its core a heterodimer made up of two proteins, D1 and D2. The D1 protein is known to be rapidly degraded by photosynthetically active radiation while the D2 protein is relatively stable. This paper reports that when the aquatic higher plant, Spirodela was exposed to ultraviolet-B radiation, D2 degradation accelerated markedly and half life times approached those of the D1 protein. Moreover, in the presence of an environmentally relevant background of photosynthetically active radiation, low fluxes of ultraviolet-B (but not ultraviolet-A) radiation synergistically stimulated degradation of the D2 protein within functional reaction centres. Thus, above a critical threshold, ultraviolet-B specifically targets the D1-D2 heterodimer for accelerated degradation.
Scientific Publication
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