Fig. 5: The disruptive mutations of the CCL-BRX interaction interfered with LZY3 function.
From: Polar recruitment of RLD by LAZY1-like protein during gravity signaling in root branch angle control
a Sequence alignment of LZYs CCL with the secondary structures are shown at the top with β-strands (arrowhead). The conserved sequences are filled in pink. Residues whose side chain atoms form inter-molecular hydrogen bonds and residues making intermolecular van der Waals contacts are colored in cyan and red, respectively, while residues whose main chain form inter-molecular hydrogen bonds are indicated with open circle. In the consensus sequence, Ψ represents a hydrophobic residue, while x represents any residue. b Pull-down binding assay. RLD2 BRX domain was pulled down with GST-LZY3 CCL (WT and mutants) and analyzed by SDS-PAGE. Arrows indicate the reduced abundance of RLD2 BRX. c, d The importance of CCL-BRX interaction in LZY3-dependent RLD recruitment to the plasma membrane. Co-expression of RLD1-GFP with wild-type LZY3-mCherry (c) and LZY3-mCherry carrying mutations in CCL (d) in Arabidopsis protoplast cells. e, f Complementation test. Ten-day-old seedlings of lzy1 lzy2 lzy3 (e) and lzy1 lzy2 lzy3 uncomplemented by LZY3-mCherry carrying mutations in CCL driven by control of the LZY3 promoter (f). Scale bars, 10 μm (c, d) and 1 cm (e, f).
