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Nucleic Acids Research 2006 34(8):2364-2373; doi:10.1093/nar/gkl247
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Published online 8 May 2006

© The Author 2006. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions@oxfordjournals.org

Article

Oligoribonuclease is a common downstream target of lithium-induced pAp accumulation in Escherichia coli and human cells

Undine Mechold*, Vasily Ogryzko1, Saravuth Ngo and Antoine Danchin

Institut Pasteur, URA 2171, Unite de Génétique des Génomes Bactériens 75724 Paris Cedex 15, France 1 Institut Gustave Roussy, UMR 8126, Unite d' Interactions Moléculaires et Cancer 94805 Villejuif, France

*To whom correspondence should be addressed. Tel: +33 140613870; Fax: +33 145688948; Email: umechold{at}pasteur.fr

Received February 28, 2006. Revised March 12, 2006. Accepted March 29, 2006.

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.


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