Synthesis and Location of Thionins in Developing Endosperms of Barley and Wheat

Olmedo, Francisco García; Zalduegui, Pilar Carbonero; Lucas, Carlos Hernandez; Ascaso, Fernando Ponz; Vicente, Óscar; Sierra, José Monzón

doi:10.1515/9783112541807-025

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“…The lectins adhere to carbohydrates on the pathogen’s surface, which can degrade the cell wall and inhibit microbes from binding to host cells ( Roberts and Goldstein, 1982 ; Pusztai and Grant, 1998 ; Fonseca et al., 2022 ). Similarly, crambin is another hydrophobic plant protein that belongs to the thionin family ( Teeter et al., 1981 ; García Olmedo et al., 1989 ). Thionins have antifungal and antibacterial properties and a role in plant defense mechanisms ( Bohlmann and Broekaert, 1994 ).…”

Section: Resultsmentioning

confidence: 99%

In silico characterization of differentially expressed short-read nucleotide sequences identified in dieback stress-induced transcriptomic analysis reveals their role as antimicrobial peptides

Ijaz

Haq²,

Malik³

et al. 2023

Front. Plant Sci.

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We investigated the in silico characterization of short-length nucleotide sequences that were differentially expressed in dieback stress-induced transcriptomic analysis. They displayed homology with C-terminal flanking peptides and defensins-like proteins, revealing their antimicrobial activity. Their predicted fingerprints displayed protein signatures related to antimicrobial peptides. These short-length RGAs have been shown to possess structural motifs such as APLT P-type ATPase, casein kinase II (CK2), protein kinase 3, protein kinase C (PKC), and N-glycosylation site that are the attributes of disease resistance genes. The prediction of arginine and lysine residues in active binding sites in ligand docking analysis prophesied them as antimicrobial peptides due to their strong relation with antimicrobial activity. The in silico structural–functional characterization has predicted their role in resistance against microbial pathogens. Moreover, the predicted antimicrobial peptide regions showed their homology with the signature domain of PR-5-like protein and AMP family Thaumatin

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