Fig. 4: Light-dependent accumulation of thylakoid proteins in deip1 mutants.

a Phenotypes of 5-week-old plants grown in vitro under extreme low-light conditions (5  µmol m⁻² s⁻¹). b Accumulation of diagnostic protein subunits of the major thylakoidal protein complexes in the wild type (WT), and the deip1-1, deip1-2, and deip1-3 mutants grown under moderate light (ML; 95 μmol m⁻² s⁻¹) or extreme low light (LL; 5 μmol  m⁻² s⁻¹). Samples of 20 µg total protein were loaded for deip1-1, deip1-2, and deip1-3 (1×), and blots were probed with antibodies against proteins of the PSII complex (PsbA, PsbD, and LHCB2), the PSI complex (PsaB, PSAD and LCHA2), the Cytb₆f complex (PetA, PetB) and the chloroplast ATP synthase (AtpB and AtpE). As a control for equal loading, the Coomassie-stained PAA gel (CBB) is shown below each series of immunoblots. n = 3 independent biological replicates. c Protein accumulation in thylakoids purified from the wild type (WT) and the deip1 mutants grown under moderate light (ML) or extreme low light (LL). Thylakoid protein samples equivalent to 1 μg of chlorophyll were resolved in 12.5% PAA gels and blotted. Immune detection was conducted with antibodies against the Cytb₆f subunits PetA, PetB, PETC, and PetD. The light-harvesting complex protein LHCB2 served as a marker for equal chlorophyll-based loading, and the Coomassie-stained PAA gel (CBB) is shown below each series of immunoblots. Note that, due to their low chlorophyll content, the amount of loaded protein is substantially higher in the deip1-1 and deip1-3 mutants grown under ML. n = 3 independent biological replicates.