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Lil3 assembles as chlorophyll‐binding protein complex during deetiolation
Author(s) -
Reisinger Veronika,
Plöscher Matthias,
Eichacker Lutz A.
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.03.042
Subject(s) - chlorophyll , etiolation , chlorophyll a , protochlorophyllide , photosynthesis , pigment , chemistry , protein subunit , fluorescence , chlorophyll fluorescence , photosynthetic pigment , chlorophyll c , binding protein , biophysics , biochemistry , botany , chloroplast , biology , gene , enzyme , physics , organic chemistry , quantum mechanics
Dark‐grown angiosperm seedlings are etiolated and devoid of chlorophyll. Deetiolation is triggered by light leading to chlorophyll dependent accumulation of the photosynthetic machinery. The transfer of chlorophyll to the chlorophyll‐binding proteins is still unclear. We demonstrate here that upon illumination of dark‐grown barley seedlings, two new pigment‐binding protein complexes are de novo accumulated. Pigments bound to both complexes are identified as chlorophyll a and protochlorophyll a . By auto‐fluorescence tracking and mass spectrometry, we show that exclusively Lil3 is the pigment‐binding complex subunit in both complexes.