title: Lil3 assembles as chlorophyll-binding protein complex during deetiolation.
abstract: 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.
authors.affiliation: Ludwig-Maximilians-University Munich, Department Biology I, Menzingerstrasse 67, 80638 Munich, Germany.
authors.forename: Veronika
authors.initials: V
authors.lastname: Reisinger
authors.forename: Matthias
authors.initials: M
authors.lastname: Plöscher
authors.forename: Lutz A
authors.initials: LA
authors.lastname: Eichacker
mesh_terms: D002734:Chlorophyll / Q000096:biosynthesis*; D002736:Chloroplasts / Q000201:enzymology / Q000528:radiation effects; D003624:Darkness; D001467:Hordeum / Q000201:enzymology / Q000528:radiation effects*; D008027:Light; D045342:Light-Harvesting Protein Complexes / Q000378:metabolism*; D010940:Plant Proteins / Q000378:metabolism*; D021122:Protein Subunits / Q000378:metabolism; D012639:Seeds / Q000201:enzymology / Q000528:radiation effects
chemical_list: D045342:Light-Harvesting Protein Complexes; D010940:Plant Proteins; D021122:Protein Subunits; D002734:Chlorophyll