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@ARTICLE{Alboresi:16490,
author = {Alboresi, A. and Gerotto, D. and Cazzaniga, S. and Bassi,
R. and Morosinotto, T.},
title = {{A} red-shifted antenna protein associated with
{P}hotosystem {II} in {P}hyscomitrella patens},
journal = {The journal of biological chemistry},
volume = {286},
issn = {0021-9258},
address = {Bethesda, Md.},
publisher = {Soc.},
reportid = {PreJuSER-16490},
pages = {28978 - 28987},
year = {2011},
note = {This 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.},
abstract = {Antenna 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.},
keywords = {Bryopsida: chemistry / Bryopsida: genetics / Bryopsida:
metabolism / Genome, Plant: physiology / Photosystem II
Protein Complex: chemistry / Photosystem II Protein Complex:
genetics / Photosystem II Protein Complex: metabolism /
Plant Proteins: chemistry / Plant Proteins: genetics / Plant
Proteins: metabolism / Photosystem II Protein Complex (NLM
Chemicals) / Plant Proteins (NLM Chemicals) / J (WoSType)},
cin = {IBG-2},
ddc = {570},
cid = {I:(DE-Juel1)IBG-2-20101118},
pnm = {Terrestrische Umwelt},
pid = {G:(DE-Juel1)FUEK407},
shelfmark = {Biochemistry $\&$ Molecular Biology},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:21705318},
pmc = {pmc:PMC3190705},
UT = {WOS:000293837000034},
doi = {10.1074/jbc.M111.226126},
url = {https://juser.fz-juelich.de/record/16490},
}