Control of 5′,5′-Dinucleoside Triphosphate Catabolism by APH1, a Saccharomyces cerevisiae Analog of Human FHIT
AUTOR(ES)
Chen, Josiane
FONTE
American Society for Microbiology
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=107174Documentos Relacionados
- Intracellular 5',5'-dinucleoside polyphosphate levels remain constant during the Escherichia coli cell cycle.
- Control of dinucleoside polyphosphates by the FHIT-homologous HNT2 gene, adenine biosynthesis and heat shock in Saccharomyces cerevisiae
- Catabolism of bis(5'-nucleosidyl) tetraphosphates in Saccharomyces cerevisiae.
- Isolation and characterization of a dinucleoside triphosphatase from Saccharomyces cerevisiae.
- Expression in Saccharomyces cerevisiae of human interferon-alpha directed by the TRP1 5' region.