% IMPORTANT: The following is UTF-8 encoded. This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.
@ARTICLE{Ferrante:22169,
author = {Ferrante, P. and Ballottari, M. and Bonente, G. and
Giuliano, G. and Bassi, R.},
title = {{LHCBM}1 and {LHCBM}2/7 polypeptides, components of the
major {LHCII} complex, have distinct functional roles in the
photosynthetic antenna system of {C}hlamydomonas
reinhardtii},
journal = {The journal of biological chemistry},
volume = {287},
issn = {0021-9258},
address = {Bethesda, Md.},
publisher = {Soc.},
reportid = {PreJuSER-22169},
pages = {16276 - 16288},
year = {2012},
note = {This work was supported by the Italian Ministry of
Agriculture, Hydrobio project, and by Euopean Union Project
245070 FP7-KBBE-2009-3 SUNBIOPATH.},
abstract = {The photosystem II antenna of Chlamydomonas reinhardtii is
composed of monomeric and trimeric complexes, the latter
encoded by LHCBM genes. We employed artificial microRNA
technology to specifically silence the LHCBM2 and LHCBM7
genes, encoding identical mature polypeptides, and the
LHCBM1 gene. As a control, we studied the npq5 mutant,
deficient in the LHCBM1 protein. The organization of LHCII
complexes, functional antenna size, capacity for
photoprotection, thermal energy dissipation and state
transitions, and resistance to reactive oxygen species was
studied in the various genotypes. Silencing of the LHCBM2/7
genes resulted in a decrease of an LHCII protein with an
apparent molecular mass of 22 kDa, whereas silencing/lack of
LHCBM1 caused the decrease/disappearance of a 23-kDa
protein. A decrease in the abundance of trimeric LHCII
complexes and in functional antenna size was observed in
both LHCBM2/7 and LHCBM1 knockouts. In agreement with
previous data, depletion of LHCBM1 decreased the capacity
for excess energy dissipation but not the ability to perform
state transitions. The opposite was true for LHCBM2/7,
implying that this polypeptide has a different functional
role from LHCBM1. The abundance of LHCBM1 and LHCBM2/7 is in
both cases correlated with resistance to superoxide anion,
whereas only LHCBM1 is also involved in singlet oxygen
scavenging. These results suggest that different LHCBM
components have well defined, non-redundant functions
despite their high homology, implying that engineering of
LHCBM proteins can be an effective strategy for manipulating
the light harvesting system of Chlamydomonas reinhardtii.},
keywords = {Chlamydomonas reinhardtii: enzymology / Chlamydomonas
reinhardtii: genetics / Gene Silencing / MicroRNAs: genetics
/ MicroRNAs: metabolism / Photosystem II Protein Complex:
genetics / Photosystem II Protein Complex: metabolism /
Plant Proteins: genetics / Plant Proteins: metabolism /
MicroRNAs (NLM Chemicals) / 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 / SUNBIOPATH - Towards a better
sunlight to biomass conversion efficiency in microalgae
(245070)},
pid = {G:(DE-Juel1)FUEK407 / G:(EU-Grant)245070},
shelfmark = {Biochemistry $\&$ Molecular Biology},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:22431727},
pmc = {pmc:PMC3351333},
UT = {WOS:000304030900020},
doi = {10.1074/jbc.M111.316729},
url = {https://juser.fz-juelich.de/record/22169},
}