Abstract
Hexaploid wheat displays limited genetic variation. As a direct A and B genome donor of hexaploid wheat, tetraploid wheat represents an important gene pool for cultivated bread wheat. Many disease resistant genes express conserved domains of the nucleotide-binding site and leucine-rich repeats (NBS-LRR). In this study, we isolated a CC-NBS-LRR gene locating on chromosome 7B from durum wheat variety Italy 363, and designated it TdRGA-7Ba. Its open reading frame was 4014 bp, encoding a 1337 amino acid protein with a complete NBS domain and 18 LRR repeats, sharing 44.7% identity with the PM3B protein. TdRGA-7Ba expression was continuously seen at low levels and was highest in leaves. TdRGA-7Ba has another allele TdRGA-7Bb with a 4 bp deletion at position +1892 in other cultivars of tetraploid wheat. In Ae. speltoides, as a B genome progenitor, both TdRGA-7Ba and TdRGA-7Bb were detected. In all six species of hexaploid wheats (AABBDD), only TdRGA-7Bb existed. Phylogenic analysis showed that all TdRGA-7Bb type genes were grouped in one sub-branch. We speculate that TdRGA-7Bb was derived from a TdRGA-7Ba mutation, and it happened in Ae. speltoides. Both types of TdRGA-7B participated in tetraploid wheat formation. However, only the TdRGA-7Bb was retained in hexaploid wheat.
Highlights
nucleotide-binding site and leucine-rich repeats (NBS-LRR) genes are one of the largest families of resistance genes (R gene) in plants
The function of NBS-LRR genes is to participate in plant resistance to pathogens by directly/indirectly interacting with the pathogen’s effectors
We focused only on this sequence and named it as TdRGA-7Ba
Summary
NBS-LRR genes are one of the largest families of resistance genes (R gene) in plants. They encode proteins that have a central nucleotide-binding site (NBS) and a C- terminal leucine-rich repeat (LRR) [1]. In the Arabidopsis genome there are 200 NBS-LRR class homologues [2]. There are 600 NBS-LRR class homologues [3]. The function of NBS-LRR genes is to participate in plant resistance to pathogens by directly/indirectly interacting with the pathogen’s effectors. The LRR domain is a major determinant of resistance specificity, and acts as a versatile structural framework for the formation protein-protein interactions with pathogen effectors [6]
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