Yttrium（Y） accumulation in soil is a serious environment problem in China. To understand the mechanisms involved in Y tolerance and detoxification in rice seedling, the bioaccumulation, subcellular distribution, and...Yttrium（Y） accumulation in soil is a serious environment problem in China. To understand the mechanisms involved in Y tolerance and detoxification in rice seedling, the bioaccumulation, subcellular distribution, and chemical forms of Y was investigated in the present study. The results show that the content of Y both in roots and shoots increases with the increasing concentration of Y, and a large amount of Y is stored in roots. Subcellular distribution of Y in rice indicates that the majority of Y is bound to cell wall. Meanwhile, various chemical forms of Y is absorbed by rice. The greatest amount of Y is extracted by 2% hydrate acetic acid（HAc） and 0.6 mol/L HCl（particularly 2% HAc）, which indicates that most of Y is combined with un-dissolved phosphate and oxalate（particularly phosphate）. Cluster analysis, based on Y abundance levels, reveals the relationship between Y distribution patterns and chemical forms. Our results imply that Y forming of precipitates with phosphate（and/or oxalate） and depositing in the cell wall may be a key strategy for Y detoxicity and tolerance in rice.展开更多
Major histocompatibility complex(MHC)molecules play a critical role in the immune response of vertebrate animals by presenting foreign antigens to T lymphocytes.In this study,we first cloned and identified a classical...Major histocompatibility complex(MHC)molecules play a critical role in the immune response of vertebrate animals by presenting foreign antigens to T lymphocytes.In this study,we first cloned and identified a classical and a novel nonclassical MHC Iαmolecules from Japanese eel(Anguilla japonica),named as AjMHC I-UBA and AjMHC I-L,respectively.The full-length cDNA of AjMHC I-UBA contains an open reading frame(ORF)of 1047 bp encoding a predicted protein of 348 amino acids,while AjMHC I-L 1089 bp encodes 362 amino acids.The multiple alignment of the amino acid sequence showed that AjMHC I-UBA and AjMHC I-L consist of an N-terminal MHC I superfamily domain withinα1 andα2 helices,an IgC-MHC Iα3 domain,and a transmembrane region close to the C-terminal,which are similar to other fish and mammal species.Molecular polymorphism analysis showed that eight different major alleles of AjMHC I-UBA,named as AjMHC I-UBA*0101~1001,were identified from six Japanese eel individuals.Furthermore,a distinguishing signature of the nonclassical L-lineage genes specific motif“HINMTL”,including an N-glycosylation site(NXS/T),was present in theα3 domain of AjMHC I-L sequences.Although the predicted three-dimensional structures of AjMHC I-UBA and AjMHC I-L are similar to that of human MHC Iα,phylogenetic analysis showed that these two protein molecules belong to classical MHC I UBA gene of U-lineage and nonclassical MHC I gene of L-lineage,respectively.Quantitative real-time polymerase chain reaction(qRT-PCR)analysis revealed that the highest expression of AjMHC I-UBA and AjMHC I-L was found in the intestine and the expression level of AjMHC I-UBA in all of the examined tissues was significantly higher than that of AjMHC I-L.The expressions of AjMHC I-UBA and AjMHC I-L in liver,kidney and spleen were significantly induced following injection with the viral mimic poly I:C,LPS,and Aeromonas hydrophila infection.In vitro,the AjMHC I-UBA and AjMHC I-L transcripts of Japanese eel liver cells were significantly enhanced by the treatment 展开更多
基金Project supported by Natural Science Foundation of Shandong Province,China(ZR2014DM010,ZR2015CL009)National Natural Science Foundation of China(30900071)
文摘Yttrium（Y） accumulation in soil is a serious environment problem in China. To understand the mechanisms involved in Y tolerance and detoxification in rice seedling, the bioaccumulation, subcellular distribution, and chemical forms of Y was investigated in the present study. The results show that the content of Y both in roots and shoots increases with the increasing concentration of Y, and a large amount of Y is stored in roots. Subcellular distribution of Y in rice indicates that the majority of Y is bound to cell wall. Meanwhile, various chemical forms of Y is absorbed by rice. The greatest amount of Y is extracted by 2% hydrate acetic acid（HAc） and 0.6 mol/L HCl（particularly 2% HAc）, which indicates that most of Y is combined with un-dissolved phosphate and oxalate（particularly phosphate）. Cluster analysis, based on Y abundance levels, reveals the relationship between Y distribution patterns and chemical forms. Our results imply that Y forming of precipitates with phosphate（and/or oxalate） and depositing in the cell wall may be a key strategy for Y detoxicity and tolerance in rice.
基金supported by“Nature Science Foundation of Fujian Province”(No.2020J01671)“The Science Foundation of Jimei University,China”(No.ZP2020017)+1 种基金“Engineering Research Center of the Modern Technology for Eel Industry,Ministry of Education,P.R.China”(No.RE202110)“Key Laboratory and Healthy Mariculture for the East China Sea,Ministry of Agriculture and Rural Affairs,P.R.China”(No.2020ESHML02).
文摘Major histocompatibility complex(MHC)molecules play a critical role in the immune response of vertebrate animals by presenting foreign antigens to T lymphocytes.In this study,we first cloned and identified a classical and a novel nonclassical MHC Iαmolecules from Japanese eel(Anguilla japonica),named as AjMHC I-UBA and AjMHC I-L,respectively.The full-length cDNA of AjMHC I-UBA contains an open reading frame(ORF)of 1047 bp encoding a predicted protein of 348 amino acids,while AjMHC I-L 1089 bp encodes 362 amino acids.The multiple alignment of the amino acid sequence showed that AjMHC I-UBA and AjMHC I-L consist of an N-terminal MHC I superfamily domain withinα1 andα2 helices,an IgC-MHC Iα3 domain,and a transmembrane region close to the C-terminal,which are similar to other fish and mammal species.Molecular polymorphism analysis showed that eight different major alleles of AjMHC I-UBA,named as AjMHC I-UBA*0101~1001,were identified from six Japanese eel individuals.Furthermore,a distinguishing signature of the nonclassical L-lineage genes specific motif“HINMTL”,including an N-glycosylation site(NXS/T),was present in theα3 domain of AjMHC I-L sequences.Although the predicted three-dimensional structures of AjMHC I-UBA and AjMHC I-L are similar to that of human MHC Iα,phylogenetic analysis showed that these two protein molecules belong to classical MHC I UBA gene of U-lineage and nonclassical MHC I gene of L-lineage,respectively.Quantitative real-time polymerase chain reaction(qRT-PCR)analysis revealed that the highest expression of AjMHC I-UBA and AjMHC I-L was found in the intestine and the expression level of AjMHC I-UBA in all of the examined tissues was significantly higher than that of AjMHC I-L.The expressions of AjMHC I-UBA and AjMHC I-L in liver,kidney and spleen were significantly induced following injection with the viral mimic poly I:C,LPS,and Aeromonas hydrophila infection.In vitro,the AjMHC I-UBA and AjMHC I-L transcripts of Japanese eel liver cells were significantly enhanced by the treatment
