Genetic and physiological characterization of a formate-dependent 5'-phosphoribosyl-1-glycinamide transformylase activity in Bacillus subtilis.
We have found that Bacillus subtilis possesses a second 5'-phosphoribosyl-1-glycinamide (GAR) transformylase catalysing the first one-carbon transfer reaction in the purine biosynthetic pathway. Inactivation of the purN gene encoding the N10-formyl tetrahydrofolate-dependent enzyme did not result in purine auxotrophy. However, growth of a purN strain was stimulated when either purine or formate was added to the growth medium. In cell-free extracts GAR could be formylated, provided formate was added to the assay mixture. From the purN strain, purine-requiring mutants were isolated. One of these mutant strains was defective in the formate-dependent formylation of GAR in vitro. The gene containing this second mutation was designated purT, and was mapped to approximately 20 degrees on the genetic map between the cysA and aroI markers.
Saxild
H H
HH
Department of Microbiology, Technical University of Denmark, Lyngby.
Jacobsen
J H
JH
Nygaard
P
P
D000217:Acyltransferases / Q000235:genetics / Q000378:metabolism*; D001412:Bacillus subtilis / Q000201:enzymology* / Q000235:genetics; D003001:Cloning, Molecular; D005561:Formates / Q000494:pharmacology; D005798:Genes, Bacterial; D019877:Hydroxymethyl and Formyl Transferases; D009154:Mutation; D051026:Phosphoribosylglycinamide Formyltransferase; D014170:Transformation, Genetic
D005561:Formates; C030544:formic acid; D019877:Hydroxymethyl and Formyl Transferases; D051026:Phosphoribosylglycinamide Formyltransferase; D000217:Acyltransferases