Control of 5',5'-dinucleoside triphosphate catabolism by APH1, a Saccharomyces cerevisiae analog of human FHIT

J Chen; A Brevet; S Blanquet; P Plateau

doi:10.1128/JB.180.9.2345-2349.1998

Control of 5',5'-dinucleoside triphosphate catabolism by APH1, a Saccharomyces cerevisiae analog of human FHIT

J Bacteriol. 1998 May;180(9):2345-9. doi: 10.1128/JB.180.9.2345-2349.1998.

Authors

J Chen¹, A Brevet, S Blanquet, P Plateau

Affiliation

¹ Laboratoire de Biochimie, URA 1970 CNRS, Ecole Polytechnique, Palaiseau, France.

Abstract

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.

Publication types

Comparative Study

MeSH terms

Acid Anhydride Hydrolases
Dinucleoside Phosphates / metabolism*
Escherichia coli / genetics
Humans
Mutagenesis
Neoplasm Proteins*
Phosphoric Diester Hydrolases / deficiency
Phosphoric Diester Hydrolases / genetics
Phosphoric Diester Hydrolases / metabolism*
Proteins
Recombinant Proteins / metabolism
Saccharomyces cerevisiae / enzymology*
Saccharomyces cerevisiae / genetics
Species Specificity
Substrate Specificity

Substances

Dinucleoside Phosphates
Neoplasm Proteins
Proteins
Recombinant Proteins
fragile histidine triad protein
Phosphoric Diester Hydrolases
Acid Anhydride Hydrolases
bis(5'-nucleosyl)tetraphosphatase (asymmetrical)