Analysis on the Cloning,Expression and Protein Characteristics of PGI Gene from Antrodia cinnamomea
LIU Yu-huang
LU Xin
LIN Juan-juan
ZHONG Xiao-li
YAN Qiao-ling
JIANG Yong-mei
ZHANG Wen-xian
Abstract：Glucose phosphate isomerase(PGI)catalyzes the conversion of 6-phosphate-glucose to 6-phosphate-fructose,which is an important branch node in the process of polysaccharide synthesis.By using PGI protein of Gano-derma lucidum as a probe,based on the genome database of Antrodia cinnamomea,the pgi gene of Antrodia cinnamo-mea was cloned by using the electronic cloning technology,and the characteristics of the protein encoded by the gene were analyzed.The transcript expression level of the gene during the fermentation process was detected by RT-PCR.The results showed that the cDNA length of pgi gene was 1 659 bp,encoding 552 amino acids,and the encoded PGI protein was hydrophilic and had no transmembrane and signal peptide structure.The secondary structure was domina-ted by 47.83%α-helix.The protein sequence had a close genetic relationship with Sparassis crispa and Amylocystis lapponica.In the process of solid culture and liquid culture of Antrodia cinnamomea,the level of pgi gene transcrip-tion expression increased with time,which was inversely proportional to the synthesis of polysaccharides.The results of this study could lay a foundation for the metabolic regulation of polysaccharide synthesis in Antrodia cinnamomea.
Keywords：Antrodia cinnamomeaGlucose phosphate isomerasePolysaccharideProtein characteristics
Publication Date：2025-01-27
Online Publishing Date：2025-08-15(First online date of this platform, not the publication date of the document)
Pages：7( 31-37 )