Format

Send to

Choose Destination
Ecotoxicol Environ Saf. 2017 Mar;137:29-34. doi: 10.1016/j.ecoenv.2016.11.012. Epub 2016 Dec 19.

Triphenyltin degradation and proteomic response by an engineered Escherichia coli expressing cytochrome P450 enzyme.

Author information

1
Key Laboratory of Environmental Exposure and Health of Guangzhou City, School of Environment, Jinan University, Guangzhou 510632, Guangdong, China.
2
Key Laboratory of Environmental Exposure and Health of Guangzhou City, School of Environment, Jinan University, Guangzhou 510632, Guangdong, China; Joint Genome Institute, Lawrence Berkeley National Laboratory, Walnut Creek 94598, CA, USA. Electronic address: jinshaoye@lbl.gov.
3
Joint Genome Institute, Lawrence Berkeley National Laboratory, Walnut Creek 94598, CA, USA.

Abstract

Although triphenyltin (TPT) degradation pathway has been determined, information about the enzyme and protein networks involved was severely limited. To this end, a cytochrome P450 hydroxylase (CYP450) gene from Bacillus thuringiensis was cloned and expressed in Escherichia coli BL21 (DE3), namely E. coli pET32a-CYP450, whose dosage at 1gL-1 could degrade 54.6% TPT at 1mgL-1 within 6 d through attacking the carbon-tin bonds of TPT by CYP450. Sequence analysis verified that the CYP450 gene had a 1214bp open reading frame, encoding a protein with 404 amino acids. Proteomic analysis determined that 60 proteins were significantly differentially regulated expression in E. coli pET32a-CYP450 after TPT degradation. The up-regulated proteins enriched in a network related to transport, cell division, biosynthesis of amino acids and secondary metabolites, and microbial metabolism in diverse environments. The current findings demonstrated for the first time that P450 received electrons transferring from NADH could effectively cleave carbon-metal bonds.

KEYWORDS:

Bacillus thuringiensis; Gene clone; ITRAQ; Organotin; Proteomics

PMID:
27907843
DOI:
10.1016/j.ecoenv.2016.11.012
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center