Growth of Escherichia coli in acetate as a sole carbon source is inhibited by ankyrin-like repeats present in the 2',5'-linked oligoadenylate-dependent human RNase L enzyme.

@article{DazGuerra1997GrowthOE,
  title={Growth of Escherichia coli in acetate as a sole carbon source is inhibited by ankyrin-like repeats present in the 2',5'-linked oligoadenylate-dependent human RNase L enzyme.},
  author={Mar{\'i}a Jos{\'e} M D{\'i}az-Guerra and M Carmen Desco Esteban and Jos{\'e} L Mart{\'i}nez},
  journal={FEMS microbiology letters},
  year={1997},
  volume={149 1},
  pages={107-13}
}
Expression of low levels of the 2',5'-linked oligoadenylate-dependent human RNase L, an enzyme induced by interferons, is highly toxic in Escherichia coli. This protein contains an ankyrin domain responsible for RNase L toxicity. The only known ORF in E. coli containing ankyrin repeats is yjaC in the acetate metabolic cluster. We have investigated if expression of mutant forms of RNase L interfere with metabolism of acetate in E. coli. Our findings demonstrate that E. coli expressing RNase L… CONTINUE READING