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Sequence, structure, and function of the Dps DNA-binding protein from Deinococcus wulumuqiensis R12
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Sequence, structure, and function of the Dps DNA-binding protein from Deinococcus wulumuqiensis R12
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Sequence, structure, and function of the Dps DNA-binding protein from Deinococcus wulumuqiensis R12
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Journal Article
Sequence, structure, and function of the Dps DNA-binding protein from Deinococcus wulumuqiensis R12
2022
Overview
Deinococcus wulumuqiensis
R12, which was isolated from arid irradiated soil in Xinjiang province of China, belongs to a genus that is well-known for its extreme resistance to ionizing radiation and oxidative stress. The DNA-binding protein Dps has been studied for its great contribution to oxidative resistance. To explore the role of Dps in
D. wulumuqiensis
R12, the Dps sequence and homology-modeled structure were analyzed. In addition, the
dps
gene was knocked out and proteomics was used to verify the functions of Dps in
D. wulumuqiensis
R12. Docking data and DNA binding experiments in vitro showed that the R12 Dps protein has a better DNA binding ability than the Dps1 protein from
D. radiodurans
R1. When the
dps
gene was deleted in
D. wulumuqiensis
R12, its resistance to H
2
O
2
and UV rays was greatly reduced, and the cell envelope was destroyed by H
2
O
2
treatment. Additionally, the qRT-PCR and proteomics data suggested that when the
dps
gene was deleted, the catalase gene was significantly down-regulated. The proteomics data indicated that the metabolism, transport and oxidation–reduction processes of
D. wulumuqiensis
R12 were down-regulated after the deletion of the
dps
gene. Overall, the data conformed that Dps protein plays an important role in
D. wulumuqiensis
R12.
Publisher
BioMed Central,BioMed Central Ltd,Springer Nature B.V,BMC
