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J Bacteriol, May 1998, p. 2345-2349, Vol. 180, No. 9
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Control of 5',5'-Dinucleoside Triphosphate Catabolism by APH1, a Saccharomyces cerevisiae Analog of Human FHIT

Josiane Chen, Annie Brevet, Sylvain Blanquet, and Pierre Plateau*

Laboratoire de Biochimie, URA 1970 CNRS, Ecole Polytechnique, 91128 Palaiseau Cedex, France

Received 13 November 1997/Accepted 2 March 1998

The putative human tumor suppressor gene FHIT (fragile histidine triad) (M. Ohta et al., Cell 84:587-597, 1996) encodes a protein behaving in vitro as a dinucleoside 5',5'''-P1,P3-triphosphate (Ap3A) hydrolase. In this report, we show that the Saccharomyces cerevisiae APH1 gene product, which resembles human Fhit protein, also hydrolyzes dinucleoside 5',5'-polyphosphates, with Ap3A being the preferred substrate. Accordingly, disruption of the APH1 gene produced viable S. cerevisiae cells containing reduced Ap3A-hydrolyzing activity and a 30-fold-elevated Ap3N concentration.

* Corresponding author. Mailing address: Laboratoire de Biochimie, URA 1970 CNRS, Ecole Polytechnique, 91128 Palaiseau Cedex, France. Phone: (33) 1 69 33 41 81. Fax: (33) 1 69 33 30 13. E-mail: plateau{at}coli.polytechnique.fr.

J Bacteriol, May 1998, p. 2345-2349, Vol. 180, No. 9
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.




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