DISCONTINUED Cyt f | Cytochrome f protein (PetA) of thylakoid Cyt b6/f-complex (higher plants)

Silver staining and Western blot analyses of protein extracts from the isolated dimorphic chloroplasts. Two micrograms of proteins from total chloroplasts (lane 1), peripheral chloroplasts (lane 2) and central chloroplasts (lane 3) were separated on SDS/12% PAGE. Molecular weights are shown on the left in kilodaltons. (A) Total proteins were visualized by silver staining. Polypeptides of the highly abundant pyruvate orthophosphate dikinase (PPDK), Rubisco large-subunit (LSU) and small-subunit (SSU) are indicated. Other bands of significantly different intensities between the dimorphic chloroplasts are indicated by arrowheads. (B) Resolved proteins were electroblotted onto nitrocellulose membranes and probed with antibodies against PPDK, LSU, Photosystem II manganese-stabilizing protein (PsbO), cytochrome f (Cyt-f), or Photosystem I subunit II (PsaD). (C) The immunoblots were analyzed by densitometric quantification. The abundance of each protein in peripheral (P-Chls) and central (C-Chls) chloroplasts was calculated relative to that of total chloroplasts and shown with standard errors, after three (PsbO) or four (others) independent experiments.

Stepwise detachment of photosynthetic protein complexes from the thylakoid membrane of WT, stn7, stn8, stn7stn8, and tap38/pph1. Thylakoid membranes of WT, stn7, stn8, stn7stn8, and tap38/pph1 plants harvested from moderate growth light (GL, 120 ?mol photons m?2 s?1) or after high light illumination (HL, 600 ?mol photons m?2 s?1 for 2 hr) were isolated and solubilized with 0%, 0.25%, 0.5%, 1%, and 2% DIG. Equal volumes of the soluble supernatant (S) and insoluble pellet (P) fractions were loaded and separated in SDS?PAGE followed by immunodetection of (a) proteins D1, PSAB, CYTF, and ATPF representing the protein complexes PSII, PSI, LHCII, Cyt b6f, and ATP synthase, respectively, as well as (b) proteins LHCB1, P?LHCB1, LHCB2, P?LHCB2, and LHCB3, representing the different subunits of the LHCII complexes. The differences in mutants with respect to WT as well as the differences in WT in response to Hl are marked with white boxes. Representative data from three different biological replicates are shown

Western Blot analyses (a) and densitometric analyses of PsbS (b), VDE (c), PGRL1 (d), and cytf (e) proteins in leaves of tomato plants (Solanum lycopersicum L. cv. Malinowy Ozarowski) grown under different light conditions (see Material and Methods for details). The bands were normalized to the appropriate ? subunit of ATP synthase (ATPB) band (loading control, Figure S4) (a). The bar diagrams (b–e) represent pixel volumes (densitometric analyses) of proteins in samples. Each value represents the mean ± SD (n = 3) considering the control sample (WL) value as 1 (100%). Different letters indicate significant differences between treatments (p = 0.05) with a Tukey’s HSD test. MW—molecular weight.