Abstract
Lignin is a complex phenolic compound that can enhance the stiffness, hydrophobicity, and antioxidant capacity of the cell wall; it thus provides a critical barrier against pathogen and insect invaders. Caffeoyl shikimate esterase (CSE) is a key novel enzyme involved in lignin biosynthesis that is associated with genetic improvements in lignocellulosic biomass; however, no research thus far have revealed the role of CSE in resistance to pathogenic stress. CsCSE1 (Cucsa.134370) has previously been shown to highly associated with the response of cucumber to attack by Podosphaera xanthii through RNA sequencing. Here, we detected the exactly role of CsCSE1 in the defence of cucumber to P. xanthii infection. Homologous sequence alignment revealed that CsCSE1 contains two highly conserved lyase domains (GXSXG), suggesting that CsCSE1 possesses CSE activity. Subcellular localization analysis manifested that CsCSE1 was localized to the plasma membrane and endoplasmic reticulum (ER). Functional analysis demonstrated that the transient silencing of CsCSE1 in cucumber dramatically attenuated resistance to P. xanthii, whereas overexpression of CsCSE1 in cucumber markedly increased resistance to P. xanthii. Further investigation of the abundance of lignin in transient transgenic plants revealed that CsCSE1 might actively mediate the disease resistance of cucumber by promoting lignin biosynthesis. CsCSE1 also affects the expression of its downstream lignin biosynthesis-related genes, like CsLAC, CsCOMT, CsCCR, and CsCAD. The results of this study provide targets for the genetic breeding of tolerant cucumber cultivars as well as new insights that could aid the control of plant diseases.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.