US EPA

1337651 

Journal Article 

A new arsenate reductase involved in arsenic detoxification in Anabaena sp. PCC7120 

Pandey, S; Shrivastava, AK; Singh, VK; Rai, R; Singh, PK; Rai, S; Rai, LC 

2013 

Yes 

Functional & Integrative Genomics
ISSN: 1438-793X
EISSN: 1438-7948 

13 

1 

43-55 

English 

23086594 

10.1007/s10142-012-0296-x 

WOS:000316690000005 

In silico analysis followed by experimental validation leads us to propose that the predicted protein All0195 of Anabaena sp. PCC7120 showing enhanced expression under sodium arsenate (Na(2)HAsO(4)) stress belongs to the thioredoxin superfamily with structural similarity to bacterial arsenate reductase. The All0195 protein demonstrated C-X-TC-X-K, NTSG-X(2)-YR, and D-X(2)-L-X-KRP as functional motifs that show similarity to seven known bacterial arsenate reductase family protein homologs with Cys, Arg, and Pro as conserved residues. In view of physicochemical properties, such as aliphatic index, ratio of Glu + Lys to Gln + His, and secondary structure, it was evident that All0195 was also a thermostable protein. The predicted three-dimensional structure on molecular docking with arsenate oxyanion ([Formula: see text]) revealed its interaction with conserved Cys residue as also known for other bacterial arsenate reductase. In silico derived properties were experimentally attested by cloning and heterologous expression of all0195. Furthermore, this protein functionally complemented the arsenate reductase-deficient sodium arsenate-hypersensitive phenotype of Escherichia coli strainWC3110 (ΔarsC) and depicted arsenate reductase activity on purification. In view of the above properties, All0195 appears to be a new arsenate reductase involved in arsenic detoxification in Anabaena sp. PCC7120. 

Arsenic; Arsenate reductase; Homology modeling; Complementation