Thioredoxin （Trx） proteins are involved in many biological processes especially the regulation of cellular redox homeostasis. In this study, two Trx cDNAs were cloned from the mussel Mytilus galloprovincialis using ...Thioredoxin （Trx） proteins are involved in many biological processes especially the regulation of cellular redox homeostasis. In this study, two Trx cDNAs were cloned from the mussel Mytilus galloprovincialis using rapid amplification of cDNA ends-polymerase chain reaction （RACE-PCR）. The two cDNAs were named MgTrxl and MgTrx2, respectively. The open reading frames of MgTrxl and MgTrx2 were 318 and 507 base pairs （bp） and they encoded proteins of 105 and 168 amino acids with estimated molecular masses of 11.45 and 18.93 kDa, respectively. Sequence analysis revealed that both proteins possessed the conserved active site dithiol motif Cys-Gly-Pro-Cys. In addition, MgTrx2 also possessed a putative mitochondrial targeting signal suggesting that it is located in the mitochondria. Quantitative real-time polymerase chain reaction （qPCR） revealed that both MgTrxl and MgTrx2 were constitutively expressed in all tissues examined. The MgTrxl transcript was most abundant in hemocytes and gills, whereas the MgTrx2 transcript was most abundant in gonad, hepatopancreas, gill and hemocytes. Following Vibrio anguillarum challenge, the expression of MgTrxl was up-regulated and reached its peak, at a value 10-fold the initial value, at 24 h. Subsequently, expression returned back to the original level. In contrast, the expression level of MgTrx2 was down-regulated following bacterial stimulation, with one fifth of the control level evident at 12 h post challenge. These results suggest that MgTrxl and MgTrx2 may play important roles in the response ofM. galloprovincialis to bacterial challenge.展开更多
基金Supported by the National Natural Science Foundation of China(No.31172388)the 100 Talents Program of the Chinese Academy of Sciencesthe Key Laboratory for Ecological Environment in Coastal Areas(201011),State Oceanic Administration
文摘Thioredoxin （Trx） proteins are involved in many biological processes especially the regulation of cellular redox homeostasis. In this study, two Trx cDNAs were cloned from the mussel Mytilus galloprovincialis using rapid amplification of cDNA ends-polymerase chain reaction （RACE-PCR）. The two cDNAs were named MgTrxl and MgTrx2, respectively. The open reading frames of MgTrxl and MgTrx2 were 318 and 507 base pairs （bp） and they encoded proteins of 105 and 168 amino acids with estimated molecular masses of 11.45 and 18.93 kDa, respectively. Sequence analysis revealed that both proteins possessed the conserved active site dithiol motif Cys-Gly-Pro-Cys. In addition, MgTrx2 also possessed a putative mitochondrial targeting signal suggesting that it is located in the mitochondria. Quantitative real-time polymerase chain reaction （qPCR） revealed that both MgTrxl and MgTrx2 were constitutively expressed in all tissues examined. The MgTrxl transcript was most abundant in hemocytes and gills, whereas the MgTrx2 transcript was most abundant in gonad, hepatopancreas, gill and hemocytes. Following Vibrio anguillarum challenge, the expression of MgTrxl was up-regulated and reached its peak, at a value 10-fold the initial value, at 24 h. Subsequently, expression returned back to the original level. In contrast, the expression level of MgTrx2 was down-regulated following bacterial stimulation, with one fifth of the control level evident at 12 h post challenge. These results suggest that MgTrxl and MgTrx2 may play important roles in the response ofM. galloprovincialis to bacterial challenge.
