NARA Discovery
Article Details
← Back to Search Results
Journal Article

Gene identification, expression analysis, and molecular docking of SAT and OASTL in the metabolic pathway of selenium in Cardamine hupingshanensis

Yushan Chen; Yao Li; Guoqiang Luo; Cihang Luo; Zhijing Xiao; Yanke Lu; Zhixin Xiang; Zhi Hou; Qiang Xiao; Yifeng Zhou; Qiaoyu Tang
Plant Cell Reports · Vol. 43, Issue 6 · 2024

Abstract

Key message Identification of selenium stress-responsive expression and molecular docking of serine acetyltransferase (SAT) and O -acetyl serine (thiol) lyase (OASTL) in Cardamine hupingshanensis. Abstract A complex coupled with serine acetyltransferase (SAT) and O -acetyl serine (thiol) lyase (OASTL) is the key enzyme that catalyzes selenocysteine (Sec) synthesis in plants. The functions of SAT and OASTL genes were identified in some plants, but it is still unclear whether SAT and OASTL are involved in the selenium metabolic pathway in Cardamine hupingshanensis . In this study, genome-wide identification and comparative analysis of ChSAT s and ChOASTL s were performed. The eight ChSAT genes were divided into three branches, and the thirteen ChOASTL genes were divided into four branches by phylogenetic analysis and sequence alignment, indicating the evolutionary conservation of the gene structure and its association with other plant species. qRT-PCR analysis showed that the ChSAT and ChOASTL genes were differentially expressed in different tissues under various selenium levels, suggesting their important roles in Sec synthesis. The ChSAT1;2 and ChOASTLA1;2 were silenced by the VIGS system to investigate their involvement in selenium metabolites in C. hupingshanensis . The findings contribute to understanding the gene functions of ChSAT s and ChOASTL s in the selenium stress and provide a reference for further exploration of the selenium metabolic pathway in plants.

Bibliographic Information

JournalPlant Cell Reports
PublisherSpringer
Publication Date2024-06-01
Publication Year2024
Volume43
Issue6
Document TypeJournal Article
Print ISSN0721-7714
eISSN1432-203X
DOI10.1007/s00299-024-03227-6

Access Information

NARA Access Coverage1981-01-01~Current
Journal Homepagehttps://www.springer.com/journal/299
Publisher PageOpen Publisher Page
Full-text access depends on NARA's subscribed coverage and institutional access.