Abstract
The 14-3-3 gene family, which is conserved in eukaryotes, is involved in protein-protein interactions and mediates signal transduction. However, detailed investigations of the 14-3-3 gene family in Medicago truncatula are largely unknown. In this study, the identification and study of M. truncatula 14-3-3-family genes were performed based on the latest M. truncatula genome. In the M. truncatula genome, 10 14-3-3 family genes were identified, and they can be grouped into ε and non-ε groups. An exon-intron analysis showed that the gene structures are conserved in the same group. The protein structure analysis showed that 14-3-3 proteins in M. truncatula are composed of nine typical antiparallel α-helices. The expression patterns of Mt14-3-3 genes indicated that they are expressed in all tissues. Furthermore, the gene expression levels of Mt14-3-3 under hormone treatment and Sinorhizobium meliloti infection showed that the Mt14-3-3 genes were involve in nodule formation. Our findings lay a solid foundation for further functional studies of 14-3-3 in M. truncatula.
Highlights
The 14-3-3s form a family that is universally expressed in eukaryotes
To study the 14-3-3 family in M. truncatula, we identified 10 family members and studied their gene and protein structures, performed phylogenetic and promoter analyses, and analyzed their expression patterns in different tissues, as well as after hormone treatments and Sinorhizobium meliloti infection
After analyzing the phytozome website, 11 potential 14-3-3family genes were used as query against the M. truncatula genome
Summary
The 14-3-3s form a family that is universally expressed in eukaryotes. They are involved in proteinprotein interaction and mediate signal transduction, which requires specific phosphorylated motifs. Structural studies showed that the 14-3-3 proteins consist of nine typical antiparallel α-helices (Jones et al, 1995). They often form homodimers or heterodimers, and each 14-3-3 protein in the dimer is able to interact with a different protein (Wilker et al, 2005). The target binding sites are RSXpSXP, RSXXpSXP, and YpT (Sehnke et al, 2002)
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