Cysteine-Rich Peptide Genes of Wheatgrass Thinopyrum elongatum

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Cysteine-rich peptides play an important role in the plant defense system. The aim of the present work was to search in silico for genes encoding antimicrobial and signaling peptides in the genome of Thinopyrum elongatum (Host) D.R. Dewey (2n = 14, EE) − a wild grass species with high resistance to pathogens and abiotic stress. Bioinformatic analysis revealed 154 new genes of antimicrobial and signaling peptide precursors belonging to 9 families in Th. elongatum genome. Introns were detected in a number of cysteine-rich peptide genes. The structure of peptide precursors and localization of peptide genes in wheat chromosomes were determined. The greatest similarity of the sequences of Th. elongatum peptides with homologous peptides of plants of the genera Triticum and Aegilops was shown, which confirms the cytogenetic data on the relatedness of genome E with genome D and similar genomes. The results obtained contribute to the characterization of molecular components of the immune system of Th. elongatum and will serve as a basis for further studies of resistance mechanisms, as well as for scientifically justified practical use of this species as a resistance donor in wheat breeding.

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M. Slezina

Vavilov Institute of General Genetics, Russian Academy of Sciences

Email: odintsova2005@rambler.ru
俄罗斯联邦, Moscow, 119991

E. Istomina

Vavilov Institute of General Genetics, Russian Academy of Sciences

Email: odintsova2005@rambler.ru
俄罗斯联邦, Moscow, 119991

A. Shiyan

Vavilov Institute of General Genetics, Russian Academy of Sciences

Email: odintsova2005@rambler.ru
俄罗斯联邦, Moscow, 119991

T. Odintsova

Vavilov Institute of General Genetics, Russian Academy of Sciences

编辑信件的主要联系方式.
Email: odintsova2005@rambler.ru
俄罗斯联邦, Moscow, 119991

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2. Fig. 1. Alignment of amino acid sequences of DEFL precursors from Th. elongatum (Te) and T. kiharae (Tk) [27], as well as some plant defensins. Conserved amino acid residues are highlighted in gray. Cysteine ​​residues in the mature peptide are highlighted in white on a black background. Groups of similar peptides are separated by a blank line.

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3. Fig. 2. Alignment of amino acid sequences of precursors: a − snakains of Th. elongatum, TkSN1 of wheat [28] and some snakains of plants of the genus Triticum; b − hevein-like peptide of Th. elongatum and peptide WAMP-1 of wheat (P85966.2); c − thionin-like peptide of Th. elongatum and homologous sequence of T. aestivum; d − peptides of the RALF family of Th. elongatum and other plants; d − peptides of the MEG family of Th. elongatum, peptide MEG2 of Solanum lycopersicum [15] and peptides MEG1 (NP_001384080.1), MEG2-like (NP_001413142.1) of Zea mays; e − peptides of the Ole e 1 family from Th. elongatum, Ole e 1-like peptide from Olea europaea var. sylvestris (XP_022872526.1) and homologous sequences; g − cysteine-rich peptides from Th. elongatum with a new motif and their closest homologues. Conserved amino acid residues are highlighted in grey. Cysteine ​​residues in the mature peptide are highlighted in white on a black background. Groups of similar peptides are separated by an empty line.

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4. Fig. 3. Alignment of amino acid sequences of lipid transfer proteins of Th. elongatum. Conserved amino acid residues are highlighted in gray. Cysteine ​​residues in the mature peptide are highlighted in white on a black background. Similar peptide types are separated by a blank line.

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5. Fig. 4. Map of the location of AMP genes and signal peptides on the chromosomes of Th. elongatum.

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6. Fig. 5. Distribution of AMP genes and signal peptides on couch grass chromosomes. Snakin, Hevein-like, Thionin.

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7. Fig. 6. Representation of genes of peptides of different subgroups in chromosomes of wheatgrass. Snakin, Hevein-like, Thionin.

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