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Genetic and physiological characterization of a formate-dependent 5′-phosphoribosyl-1-glycinamide transformylase activity in Bacillus subtilis

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Abstract

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° on the genetic map between the cysA and aroI markers.

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Communicated by J. Lengeler

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Saxild, H.H., Jacobsen, J.H. & Nygaard, P. Genetic and physiological characterization of a formate-dependent 5′-phosphoribosyl-1-glycinamide transformylase activity in Bacillus subtilis . Molec. Gen. Genet. 242, 415–420 (1994). https://doi.org/10.1007/BF00281791

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  • DOI: https://doi.org/10.1007/BF00281791

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