Abstract
Toxin–antitoxin (TA) complexes play an important role in stress responses and programmed cell death in bacteria. The RelB-RelE toxin antitoxin system is well studied in Escherichia coli. In this study, we used combined in silico and in vitro approaches to study a novel Xn-RelT toxin from Xenorhabdus nematophila bearing its own antitoxin Xn-RelAT—a RelB homolog of E. coli. The structure for this toxin–antitoxin pair is yet unknown. We generated homology-based models of X. nematophila RelT toxin and antitoxin. The deduced models were further characterized for protein–nucleic acid, protein–protein interactions and gene ontology. A detrimental effect of recombinant Xn-RelT on host E. coli was determined through endogenous toxicity assay. When expressed from a isopropyl β-d-1-thiogalactopyranoside-regulated LacZ promoter, Xn-RelT toxin showed a toxic effect on E. coli cells. These observations imply that the conditional cooperativity governing the Xn-RelT TA operon in X. nematophila plays an important role in stress management and programmed cell death.
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Acknowledgments
The authors thank Science and Engineering Research Board, Department of Science and Technology (DST-SERB), India for financial support for this study. L.K.G. and M.Y. acknowledge DST, Government of India, for a Junior Research Fellowship for this project.
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Gautam, L.K., Yadav, M. & Rathore, J.S. Functional annotation of a novel toxin–antitoxin system Xn-RelT of Xenorhabdus nematophila; a combined in silico and in vitro approach. J Mol Model 23, 189 (2017). https://doi.org/10.1007/s00894-017-3361-5
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DOI: https://doi.org/10.1007/s00894-017-3361-5