皱纹盘鲍芳基硫酸酯酶ARSB的复制及功能分化分析OA北大核心CSCDCSTPCD

Abalone feed on macroalgae that are rich in sulfated polysaccharides,such as fucoidan and agarose.Their digestive process depends on the hydrolysis of sulfate bonds by sulfatase;however,the functional evolution mechanism of sulfatase within animal digestive systems remains to be elucidated.This study analyzed the genome of the Pacific abalone(Haliotis discus Hannia)and identified a tandemly repeated gene cluster composed of four arylsulfatase B(ARSB)gene family members.Moreover,homologous alignment and phylogenetic analysis re-vealed that the gene cluster existed in three related abalone species,indicating that this tandem replication event likely occurred in the genome of the common abalone ancestor and was preserved in the offspring species.Analysis of the gene cluster structure showed that there were some differences in the gene structure and amino acid mutations in conserved sites.The qPCR results also demonstrated that the replicated genes were expressed differently in Haliotis discus hannai when they were fed with different macroalgae.To further investigate the functional charac-teristics of the duplicated sulfatase genes,this study cloned HdARSB2 and the formylglycine-generating enzyme gene HdFGE from the abalone,co-expressed them in a prokaryotic system,and successfully obtained soluble re-combinant proteins.However,no sulfatase activity was detected in the supernatant.Furthermore,in situ hybridiza-tion analysis revealed that the HdARSB2 gene was specifically expressed in a gland with concentrated function in the abalones'hepatopancreas.By analyzing the evolution and expression of these sulfatase genes,this study re-vealed new clues regarding the molecular mechanisms that enable abalone to adapt to diverse food sources and changing marine environments.In addition,these results provide theoretical support for abalone aquaculture,selec-tive breeding,and the potential utilization of sulfatases.