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. 2020 Jun 18;11:1307. doi: 10.3389/fmicb.2020.01307

FIGURE 1.

FIGURE 1

The structure of NCRs, NCR-like peptides (A) and the mode of actions of cationic NCRs (B). (A) Frequency of amino acids and conserved patterns of cysteines in the mature M. truncatula NCRs and NCR-like peptides from Dalbergioid legumes. The height of letters in the stacks indicates the relative frequency of (each amino acid at that position. Color code of amino acids: blue, positively charged (KR) residues; red, hydrophobic (AFILMV) and amphipathic (WY) residues; black, all other amino acids. The underlined G residue in the NCR-like peptides marks the beginning of the γ-core motif. (B) The mode of actions of cationic NCRs based on the example of NCR247 (Created with BioRender.com). NCRs can interact with the bacterial membranes and enter the cytosol with or without pore formation or cause membrane damages and cell lysis. Intracellularly NCRs provoke global transcriptional changes and interact with numerous bacterial proteins that collectively affect essential cellular functions. The framed proteins BacA, HrrP, SMc03872, and polysaccharides EPS and LPS protect the symbiotic bacterium partner from the killing action of NCRs.)