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000016490 0247_ $$2DOI$$a10.1074/jbc.M111.226126
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000016490 084__ $$2WoS$$aBiochemistry & Molecular Biology
000016490 1001_ $$0P:(DE-HGF)0$$aAlboresi, A.$$b0
000016490 245__ $$aA red-shifted antenna protein associated with Photosystem II in Physcomitrella patens
000016490 260__ $$aBethesda, Md.$$bSoc.$$c2011
000016490 300__ $$a28978 - 28987
000016490 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000016490 440_0 $$03091$$aJournal of Biological Chemistry$$v286$$x0021-9258$$y33
000016490 500__ $$aThis work was supported by the Cassa di Risparmio di Padova e Rovigo (CaRiPaRo) Foundation, Universita di Padova Grant CPDA089403, EEC Project Harvest and Fondo per gli Investimenti della Ricerca di Base-Parallelomics Grant RBIP06CTBR.
000016490 520__ $$aAntenna systems of plants and green algae are made up of pigment-protein complexes belonging to the light-harvesting complex (LHC) multigene family. LHCs increase the light-harvesting cross-section of photosystems I and II and catalyze photoprotective reactions that prevent light-induced damage in an oxygenic environment. The genome of the moss Physcomitrella patens contains two genes encoding LHCb9, a new antenna protein that bears an overall sequence similarity to photosystem II antenna proteins but carries a specific motif typical of photosystem I antenna proteins. This consists of the presence of an asparagine residue as a ligand for Chl 603 (A5) chromophore rather than a histidine, the common ligand in all other LHCbs. Asparagine as a Chl 603 (A5) ligand generates red-shifted spectral forms associated with photosystem I rather than with photosystem II, suggesting that in P. patens, the energy landscape of photosystem II might be different with respect to that of most green algae and plants. In this work, we show that the in vitro refolded LHCb9-pigment complexes carry a red-shifted fluorescence emission peak, different from all other known photosystem II antenna proteins. By using a specific antibody, we localized LHCb9 within PSII supercomplexes in the thylakoid membranes. This is the first report of red-shifted spectral forms in a PSII antenna system, suggesting that this biophysical feature might have a special role either in optimization of light use efficiency or in photoprotection in the specific environmental conditions experienced by this moss.
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000016490 650_2 $$2MeSH$$aBryopsida: chemistry
000016490 650_2 $$2MeSH$$aBryopsida: genetics
000016490 650_2 $$2MeSH$$aBryopsida: metabolism
000016490 650_2 $$2MeSH$$aGenome, Plant: physiology
000016490 650_2 $$2MeSH$$aPhotosystem II Protein Complex: chemistry
000016490 650_2 $$2MeSH$$aPhotosystem II Protein Complex: genetics
000016490 650_2 $$2MeSH$$aPhotosystem II Protein Complex: metabolism
000016490 650_2 $$2MeSH$$aPlant Proteins: chemistry
000016490 650_2 $$2MeSH$$aPlant Proteins: genetics
000016490 650_2 $$2MeSH$$aPlant Proteins: metabolism
000016490 650_7 $$00$$2NLM Chemicals$$aPhotosystem II Protein Complex
000016490 650_7 $$00$$2NLM Chemicals$$aPlant Proteins
000016490 650_7 $$2WoSType$$aJ
000016490 7001_ $$0P:(DE-HGF)0$$aGerotto, D.$$b1
000016490 7001_ $$0P:(DE-HGF)0$$aCazzaniga, S.$$b2
000016490 7001_ $$0P:(DE-Juel1)VDB38860$$aBassi, R.$$b3$$uFZJ
000016490 7001_ $$0P:(DE-HGF)0$$aMorosinotto, T.$$b4
000016490 773__ $$0PERI:(DE-600)1474604-9$$a10.1074/jbc.M111.226126$$gVol. 286, p. 28978 - 28987$$p28978 - 28987$$q286<28978 - 28987$$tThe @journal of biological chemistry$$v286$$x0021-9258$$y2011
000016490 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3190705
000016490 8564_ $$uhttps://juser.fz-juelich.de/record/16490/files/FZJ-16490.pdf$$yRestricted$$zPublished final document.
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000016490 9141_ $$y2011
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