Large-scale analysis of NBS domain-encoding resistance gene analogs in Triticeae
AUTOR(ES)
Bouktila, Dhia, Khalfallah, Yosra, Habachi-Houimli, Yosra, Mezghani-Khemakhem, Maha, Makni, Mohamed, Makni, Hanem
FONTE
Genet. Mol. Biol.
DATA DE PUBLICAÇÃO
2014-09
RESUMO
Proteins containing nucleotide binding sites (NBS) encoded by plant resistance genes play an important role in the response of plants to a wide array of pathogens. In this paper, an in silico search was conducted in order to identify and characterize members of NBS-encoding gene family in the tribe of Triticeae. A final dataset of 199 sequences was obtained by four search methods. Motif analysis confirmed the general structural organization of the NBS domain in cereals, characterized by the presence of the six commonly conserved motifs: P-loop, RNBS-A, Kinase-2, Kinase-3a, RNBS-C and GLPL. We revealed the existence of 11 distinct distribution patterns of these motifs along the NBS domain. Four additional conserved motifs were shown to be significantly present in all 199 sequences. Phylogenetic analyses, based on genetic distance and parsimony, revealed a significant overlap between Triticeae sequences and Coiled coil-Nucleotide binding site-Leucine rich repeat (CNL)-type functional genes from monocotyledons. Furthermore, several Triticeae sequences belonged to clades containing functional homologs from non Triticeae species, which has allowed for these sequences to be functionally assigned. The findings reported, in this study, will provide a strong groundwork for the isolation of candidate R-genes in Triticeae crops and the understanding of their evolution.
Documentos Relacionados
- GECKO: a complete large-scale gene expression analysis platform
- Inactivating mutations in an SH2 domain-encoding gene in X-linked lymphoproliferative syndrome
- Large-Scale Analysis of the Meningococcus Genome by Gene Disruption: Resistance to Complement-Mediated Lysis
- Using large-scale perturbations in gene network reconstruction
- Large-Scale Proteomic Analysis of the Human Spliceosome