Volume 40 Issue 8
Aug.  2021
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Wenlin Wu, Hongyun Li, Tiantian Ma, Xiaobo Zhang. Characterization of DNA polymerase δ from deep-sea hydrothermal vent shrimp Rimicaris exoculata[J]. Acta Oceanologica Sinica, 2021, 40(8): 168-175. doi: 10.1007/s13131-021-1823-1
Citation: Wenlin Wu, Hongyun Li, Tiantian Ma, Xiaobo Zhang. Characterization of DNA polymerase δ from deep-sea hydrothermal vent shrimp Rimicaris exoculata[J]. Acta Oceanologica Sinica, 2021, 40(8): 168-175. doi: 10.1007/s13131-021-1823-1

Characterization of DNA polymerase δ from deep-sea hydrothermal vent shrimp Rimicaris exoculata

doi: 10.1007/s13131-021-1823-1
Funds:  The National Basic Research Program of China under contract No. 2015CB755903; the National Natural Science Foundation of China under contract Nos U1605214 and 31470133; the Foundation of Quanzhou Normal University under contract No. 2016YYKJ16.
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  • Corresponding author: These authors contributed equally to this work.; zxb0812@zju.edu.cn
  • Received Date: 2020-03-04
  • Accepted Date: 2020-09-24
  • Available Online: 2021-06-25
  • Publish Date: 2021-08-31
  • DNA polymerase δ (Polδ) plays a crucial and versatile role in DNA replication and DNA repair processes. Vent shrimp Rimicaris exoculata is the primary megafaunal community living in hydrothermal vents. In this study, the Polδ from shrimp Rimicaris exoculata was cloned, expressed and characterized. The results showed that the Polδ catalytic subunit (POLD1), 852 amino acids in length, shared high homology with crayfish Procambarus clarkii and shrimp Oratosquilla oratoria. The recombinant POLD1 expressed in Escherichia coli showed that the enzyme was active in a range of 20°C to 40°C with an optimum temperature at 25°C and in a wide range of pH with an optimum at pH 6.0. The activities of POLD1 were significantly enhanced in the presence of Triton-X 100, Tween 20 and Mn2+. The Km (dNTP) value of POLD1 was 4.7 μmol/L. The present study would be helpful to reveal the characterization of Polδ of deep-sea vent animals.
  • †These authors contributed equally to this work.
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