Charge reversal at the Lhcb2 N-terminus impairs phosphorylation and PSI-LHCII complex formation
Authors: Srivastava, A., Schiphorst, C., Berentsen, J., Verhoeven, D., Leeuwen, J. v., Longoni, F., Saccon, F., Wientjes, E.
Category: Plant Biology
Model Organism: Arabidopsis thaliana
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The study introduced charge-altering mutations into the N‑terminal region of Lhcb2 in Arabidopsis thaliana lacking native Lhcb2 to assess how intrinsic charge affects LHCII phosphorylation, state‑transition efficiency, and PSI‑LHCII complex formation. The R2E mutation drastically reduced Lhcb1/2 phosphorylation, impaired state transitions, and prevented PSI‑LHCII assembly, whereas the Q9E mutation had no measurable impact, and neither mutation altered thylakoid ultrastructure. Residual state transitions in the R2E line suggest that other Stn7 substrates can partially compensate for the loss of Lhcb2 phosphorylation.