Open AccessGrowth 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(s) -
DíazGuerra Margarita,
Esteban Mariano,
Martínez José L
Publication year - 1997
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1997.tb10316.x
Subject(s) - escherichia coli , ankyrin repeat , rnase p , enzyme , biochemistry , chemistry , biology , microbiology and biotechnology , gene , rna
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 ankyrin repeats is unable to grow in medium containing acetate as the sole carbon source, while it can grow when expressing other domains of the protein. This defect correlates with a severe decrease in the levels of induction of enzymes in the glyoxylate bypass.