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@ARTICLE{deBianchi:16562,
      author       = {de Bianchi, S. and Betterle, N. and Kouril, R. and
                      Cazzaniga, S. and Boekema, E. and Bassi, R. and Dall'Osto,
                      L.},
      title        = {{A}rabidopsis {M}utants {D}eleted in the
                      {L}ight-{H}arvesting {P}rotein {L}hcb4 {H}ave a {D}isrupted
                      {P}hotosystem {II} {M}acrostructure and {A}re {D}efective in
                      {P}hotoprotection},
      journal      = {The Plant Cell},
      issn         = {1040-4651},
      address      = {Rockville, Md.},
      publisher    = {Soc.},
      reportid     = {PreJuSER-16562},
      pages        = {2659 - 2679},
      year         = {2011},
      note         = {We thank Giovanni Finazzi (Commissariat a l'Energie
                      Atomique, Grenoble, France) for helpful discussion.
                      Financial support for this work was provided by the
                      Programmi di Ricerca di Interesse Nazionale (2008XB774B) and
                      by a grant of the Italian Ministry of Research and Marie
                      Curie Actions Initial Training Networks HARVEST (Grant
                      238017).},
      abstract     = {The role of the light-harvesting complex Lhcb4 (CP29) in
                      photosynthesis was investigated in Arabidopsis thaliana by
                      characterizing knockout lines for each of the three Lhcb4
                      isoforms (Lhcb4.1/4.2/4.3). Plants lacking all isoforms
                      (koLhcb4) showed a compensatory increase of Lhcb1 and a
                      slightly reduced photosystem II/I ratio with respect to the
                      wild type. The absence of Lhcb4 did not result in alteration
                      in electron transport rates. However, the kinetic of state
                      transition was faster in the mutant, and nonphotochemical
                      quenching activity was lower in koLhcb4 plants with respect
                      to either wild type or mutants retaining a single Lhcb4
                      isoform. KoLhcb4 plants were more sensitive to
                      photoinhibition, while this effect was not observed in
                      knockout lines for any other photosystem II antenna subunit.
                      Ultrastructural analysis of thylakoid grana membranes showed
                      a lower density of photosystem II complexes in koLhcb4.
                      Moreover, analysis of isolated supercomplexes showed a
                      different overall shape of the C₂S₂ particles due to a
                      different binding mode of the S-trimer to the core complex.
                      An empty space was observed within the photosystem II
                      supercomplex at the Lhcb4 position, implying that the
                      missing Lhcb4 was not replaced by other Lhc subunits. This
                      suggests that Lhcb4 is unique among photosystem II antenna
                      proteins and determinant for photosystem II
                      macro-organization and photoprotection.},
      keywords     = {Arabidopsis: genetics / Arabidopsis: physiology /
                      Arabidopsis: ultrastructure / Arabidopsis Proteins: genetics
                      / Arabidopsis Proteins: metabolism / Chlorophyll: chemistry
                      / Chlorophyll Binding Proteins: genetics / Chlorophyll
                      Binding Proteins: metabolism / Fluorescence / Gene Knockdown
                      Techniques / Light / Lipid Peroxidation / Membrane Lipids:
                      chemistry / Membrane Lipids: metabolism /
                      Oxidation-Reduction / Oxidative Stress / Oxygen: metabolism
                      / Photosynthesis: physiology / Photosynthetic Reaction
                      Center Complex Proteins: genetics / Photosynthetic Reaction
                      Center Complex Proteins: metabolism / Photosystem I Protein
                      Complex: metabolism / Photosystem II Protein Complex:
                      metabolism / Photosystem II Protein Complex: ultrastructure
                      / Protein Isoforms: genetics / Protein Isoforms: metabolism
                      / Temperature / Thylakoids: chemistry / Thylakoids:
                      metabolism / Thylakoids: ultrastructure / Arabidopsis
                      Proteins (NLM Chemicals) / Chlorophyll Binding Proteins (NLM
                      Chemicals) / LHCB4.1 protein, Arabidopsis (NLM Chemicals) /
                      Membrane Lipids (NLM Chemicals) / Photosynthetic Reaction
                      Center Complex Proteins (NLM Chemicals) / Photosystem I
                      Protein Complex (NLM Chemicals) / Photosystem II Protein
                      Complex (NLM Chemicals) / Protein Isoforms (NLM Chemicals) /
                      Chlorophyll (NLM Chemicals) / Oxygen (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 / Plant Sciences / Cell
                      Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:21803939},
      pmc          = {pmc:PMC3226214},
      UT           = {WOS:000294164300020},
      doi          = {10.1105/tpc.111.087320},
      url          = {https://juser.fz-juelich.de/record/16562},
}