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Nucleic Acids Research 2005 33(2):650-660; doi:10.1093/nar/gki211
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Published online 31 January 2005

© The Author 2005. 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{at}oupjournals.org.

Article

A highly specific phosphatase that acts on ADP-ribose 1''-phosphate, a metabolite of tRNA splicing in Saccharomyces cerevisiae

Neil P. Shull, Sherry L. Spinelli and Eric M. Phizicky*

Department of Biochemistry and Biophysics, University of Rochester School of Medicine 601 Elmwood Avenue, Rochester, NY 14642, USA

*To whom correspondence should be addressed. Tel: +1 585 275 7268; Fax: +1 585 271 2683; Email: Eric_Phizicky{at}urmc.rochester.edu

Received December 6, 2004. Revised January 7, 2005. Accepted January 7, 2005.

One molecule of ADP-ribose 1'',2''-cyclic phosphate (Appr>p) is formed during each of the approximately 500 000 tRNA splicing events per Saccharomyces cerevisiae generation. The metabolism of Appr>p remains poorly defined. A cyclic phosphodiesterase (Cpd1p) has been shown to convert Appr>p to ADP-ribose-1''-phosphate (Appr1p). We used a biochemical genomics approach to identify two yeast phosphatases that can convert Appr1p to ADP-ribose: the product of ORF YBR022w (now Poa1p), which is completely unrelated to other known phosphatases; and Hal2p, a known 3'-phosphatase of 5',3'-pAp. Poa1p is highly specific for Appr1p, and thus likely acts on this molecule in vivo. Poa1 has a relatively low K M for Appr1p (2.8 µM) and a modest k cat (1.7 min–1), but no detectable activity on several other substrates. Furthermore, Poa1p is strongly inhibited by ADP-ribose (K I, 17 µM), modestly inhibited by other nucleotides containing an ADP-ribose moiety and not inhibited at all by other tested molecules. In contrast, Hal2p is much more active on pAp than on Appr1p, and several other tested molecules were Hal2p substrates or inhibitors. poa1-{Delta} mutants have no obvious growth defect at different temperatures in rich media, and analysis of yeast extracts suggests that ~90% of Appr1p processing activity originates from Poa1p.


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