Resonance assignments of a VapC family toxin from Clostridium thermocellum
Toxin–antitoxin (TA) systems widely exist in bacterial plasmids, phages, and chromosomes and play important roles in growth persistence and host-pathogen interaction. Virulence associated protein BC (VapBC) family TAs are the most abundant TAs in bacteria and many pathogens contain a large number of vapBC loci in the genome which have been extensively studied. Clostridium thermocellum, a cellulolytic anaerobic gram-positive bacterium with promising applications in biofuel production, also contains a VapBC TA in the genome. Despite the structures of several VapBC family TAs have been determined, the toxin and anti-toxin components of C. thermocellum VapBC have very low sequence identity to the proteins in PDB. Therefore, the structure and functional mechanism of this TA is largely unknown. Here we reported the NMR resonance assignments of the VapC toxin from C. thermocellum as a basis for further structural and functional studies.
KeywordsVapBC toxin–antitoxin Clostridium thermocellum NMR Chemical shift assignment
We thank Dr. Jinfa Ying (in the Ad Bax group of NIDDK, NIH) for providing SMILE software and helpful comments for the NUS data processing. This work was supported by National Natural Science Foundation of China (Grant Nos. 31270784 to Y.F. and 31300635 to J.X.) and Chinese Government Scholarship (No. 201506465020 to J.X.).
Compliance with ethical standards
Conflict of interest
The authors declare that they have no conflict of interest.
- Das U, Pogenberg V, Subhramanyam UKT, Wilmanns M, Gourinath S, Srinivasan A (2014) Crystal structure of the VapBC-15 complex from Mycobacterium tuberculosis reveals a two-metal ion dependent PIN-domain ribonuclease and a variable mode of toxin–antitoxin assembly. J Struct Biol 188(3):249–258. doi: 10.1016/j.jsb.2014.10.002 CrossRefGoogle Scholar
- Min AB, Miallau L, Sawaya MR, Habel J, Cascio D, Eisenberg D (2012) The crystal structure of the Rv0301-Rv0300 VapBC-3 toxin–antitoxin complex from M. tuberculosis reveals a Mg2+ ion in the active site and a putative RNA-binding site. Protein Sci 21(11):1754–1767. doi: 10.1002/pro.2161 CrossRefGoogle Scholar