Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetates / metabolism
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Acetates / pharmacology*
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Ankyrins / genetics*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Cloning, Molecular
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Endoribonucleases / genetics*
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Endoribonucleases / metabolism
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Escherichia coli / enzymology
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Escherichia coli / genetics
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Escherichia coli / growth & development*
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Gene Expression Regulation, Bacterial / physiology
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Gene Expression Regulation, Enzymologic / physiology
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Glucose / pharmacology
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Glutamic Acid / pharmacology
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Humans
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Isocitrate Lyase / metabolism
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Malate Synthase / metabolism
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Plasmids
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Protein Kinases / genetics
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Protein Kinases / metabolism
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Pyruvic Acid / pharmacology
Substances
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Acetates
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Ankyrins
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Bacterial Proteins
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Glutamic Acid
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Pyruvic Acid
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Malate Synthase
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Protein Kinases
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Endoribonucleases
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2-5A-dependent ribonuclease
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Isocitrate Lyase
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Glucose