Escherichia coli mutants deficient in guanine-xanthine phosphoribosyltransferase.

AUTOR(ES)

Holden, J A

RESUMO

We studied the purine phosphoribosyltransferases (PRTases) of Escherichia coli and were able to isolate a mutant that is defective in its ability to convert guanine and xanthine to their respective ribonucleotides. The affected gene (gpt) lies between metD and proA and is 78.6% co-transducible with proA. Both this point mutant and a strain with a pro-lac deletion contain less than 2% of wild-type xanthine PRTase activity, yet still contain about 30% of wild-type guanine PRTase activity. Thus, the gpt gene is only one of at least two genes responsible for guanine PRTase activity in E. coli.

Documentos Relacionados

• Genetic Separation of Hypoxanthine and Guanine-Xanthine Phosphoribosyltransferase Activities by Deletion Mutations in Salmonella typhimurium
• Selection for animal cells that express the Escherichia coli gene coding for xanthine-guanine phosphoribosyltransferase.
• Hypoxanthine-guanine phosphoribosyltransferase. Genetic evidence for identical mutations in two partially deficient subjects.
• Rapid assay for detection of Escherichia coli xanthine-guanine phosphoribosyltransferase activity in transduced cells.
• Hypoxanthine-guanine phosphoribosyltransferase. Characterization of a mutant in a patient with gout.