Identification of KFB Family in Moso Bamboo Reveals the Potential Function of PeKFB9 Involved in Stress Response and Lignin Polymerization

• Published in: International journal of molecular sciences Vol. 23; no. 20; p. 12568
• Main Authors: Yang, Kebin, Li, Ziyang, Zhu, Chenglei, Liu, Yan, Sun, Huayu, Li, Xueping, Gao, Zhimin
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 19.10.2022; MDPI
• Subjects: abiotic stress; Amino acids; Biological activity; Biosynthesis; Chromosomes; Drought; Enzymes; Evolution; Gene expression; Gene Expression Regulation, Plant; Genes; KFB; Lignin; Lignin - genetics; Lignin - metabolism; lignin polymerization; Mechanical properties; Metabolites; Peroxidase; peroxidase activity; Peroxidases - metabolism; Phyllostachys edulis; Phylogenetics; Phylogeny; Plant Proteins - genetics; Plant Proteins - metabolism; Poaceae - genetics; Poaceae - metabolism; Polymerization; Post-translation; Proteins; Proteolysis; Roles; Ubiquitin; Ubiquitin-protein ligase; Ubiquitin-Protein Ligases - metabolism; ubiquitination; peroxidase activity; Phyllostachys edulis; ubiquitination; KFB; lignin polymerization; abiotic stress
• ISSN: 1422-0067; 1661-6596; 1422-0067
• DOI: 10.3390/ijms232012568

The Kelch repeat F-box (KFB) protein is an important E3 ubiquitin ligase that has been demonstrated to perform an important post-translational regulatory role in plants by mediating multiple biological processes. Despite their importance, KFBs have not yet been identified and characterized in bamboo. In this study, 19 PeKFBs were identified with F-box and Kelch domains; genes encoding these PeKFBs were unevenly distributed across 12 chromosomes of moso bamboo. Phylogenetic analysis indicated that the PeKFBs were divided into eight subclades based on similar gene structures and highly conserved motifs. A tissue-specific gene expression analysis showed that the s were differentially expressed in various tissues of moso bamboo. All the promoters of the s contained stress-related -elements, which was supported by the differentially expression of s of moso bamboo under drought and cold stresses. Sixteen proteins were screened from the moso bamboo shoots' cDNA library using PeKFB9 as a bait through a yeast two-hybrid (Y2H) assay. Moreover, PeKFB9 physically interacted with PeSKP1-like-1 and PePRX72-1, which mediated the activity of peroxidase in proteolytic turnover. Taken together, these findings improved our understanding of PeKFBs, especially in response to stresses, and laid a foundation for revealing the molecular mechanism of PeKFB9 in regulating lignin polymerization by degrading peroxidase.