Abstract
MYB is a large family of plant transcription factors. Its function has been identified in several plants, while there are few reports in Medicago truncatula. In this study, we used RNA-seq data to analyze and identify R2R3-MYB genes in the genome of Medicago truncatula. Phylogenetic analysis classified 150 MtMYB genes into 21 subfamilies with homologs. Out of the 150 MtMYB genes, 139 were distributed among 8 chromosomes, with tandem duplications (TD) and segment duplications (SD). Microarray data were used for functional analysis of the MtMYB genes during growth and developmental processes providing evidence for a role in tissues differentiation, seed development processes, and especially the nodulation process. Furthermore, we investigated the expression of MtMYB genes in response to abiotic stresses using RNA-seq data, which confirmed the critical roles in signal transduction and regulation processes under abiotic stress. We used quantitative real-time PCR (qRT-PCR) to validate expression profiles. The expression pattern of M. truncatula MYB genes under different abiotic stress conditions suggest that some may play a major role in cross-talk among different signal transduction pathways in response to abiotic stresses. Our study will serve as a foundation for future research into the molecular function of M. truncatula R2R3-MYB genes.
Highlights
Myeloblastosis (MYB) genes are one of the largest transcription factors families in the plant kingdom (Romero et al, 1998; Rosinski and Atchley, 1998)
We investigated the expression of MtMYB genes in response to abiotic stresses using RNA-seq data, which confirmed the critical roles in signal transduction and regulation processes under abiotic stress
The expression pattern of M. truncatula MYB genes under different abiotic stress conditions suggest that some may play a major role in cross-talk among different signal transduction pathways in response to abiotic stresses
Summary
Myeloblastosis (MYB) genes are one of the largest transcription factors families in the plant kingdom (Romero et al, 1998; Rosinski and Atchley, 1998). MYB typically contain an MYB-binding domain at the N-terminus, composed of 1-4 imperfect repeats, with approximately 51-52 amino acid residues of incomplete conserved peptides encoding three a-helices (Kanei-Ishii et al, 1990; Lipsick, 1996; Stracke et al, 2001). These three a-helices form a helix-turn-helix (HTH) structure and fold with three relatively conserved tryptophan residues, separated by 18-19 amino acid residues of regular arrangement, and further participate in the formation of hydrophobic interactions (Ogata et al, 1995). College of Life Science and Technology, Harbin Normal University, No 1 of Shida Road, Harbin, Heilongjiang, China
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