We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Oligoribonuclease is a common downstream target of lithium-induced pAp accumulation in Escherichia coli and human cells.
- Authors
Mechold, Undine; Ogryzko, Vasily; Ngo, Saravuth; Danchin, Antoine
- Abstract
We identified Oligoribonuclease (Orn), an essential Escherichia coli protein and the only exonuclease degrading small ribonucleotides (5mer to 2mer) and its human homologue, small fragment nuclease (Sfn), in a screen for proteins that are potentially regulated by 3'-phosphoadenosine 5'-phosphate (pAp). We show that both enzymes are sensitive to micromolar amounts of pAp in vitro. We also demonstrate that Orn can degrade short DNA oligos in addition to its activity on RNA oligos, similar to what was documented for Sfn. pAp was shown to accumulate as a result of inhibition of the pAp-degrading enzyme by lithium, widely used to treat bipolar disorder, thus its regulatory targets are of significant medical interest. CysQ, the E.coli pAp-phosphatase is strongly inhibited by lithium and calcium in vitro and is a main target of lithium toxicity in vivo. Our findings point to remarkable conservation of the connection between sulfur- and RNA metabolism between E.coli and humans.
- Publication
Nucleic acids research, 2006, Vol 34, Issue 8, p2364
- ISSN
1362-4962
- Publication type
Journal Article
- DOI
10.1093/nar/gkl247