Abstract
We have reported the isolation of mutants of Chinese hamster cells defective in 11 of the 12 steps of AMP synthesis which have been used to assign genes coding for enzymes of purine synthesis to various human chromosomes. We have now obtained direct evidence that in animals and probably in humans, 3 of the purine biosynthetic enzymes, phosphoribosylglycinaemide (GAR) synthetase, GAR formyltransferase, and phosphoribosylaminoimidazole (AIR) synthetase, previously reported as defective in Ade-C, Ade-E, and Ade−G mutants respectively, are encoded by a single genetic locus and contained on a single polypeptide. In humans, this locus appears to be on chromosome 21. GAR synthetase and AIR synthetase, and probably GAR formyltransferase, are genetically linked in organisms as diverse as Drosophila and human. Ade−E mutants of CHO cells, originally reported as unable to carry out GAR formyltransferase activity, are defective in the trifunctional protein required for 10-formyl FH4 synthesis and not GAR formyltransferase activity. We are attempting to isolate the human genes coding for these enzyme activities and to purify the proteins to understand their structure, function, and regulation. This work was supported by NIH AG 00029 and NIH HD 13432. This is ERICR contribution #562.
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Patterson, D., Henikoff, S., Sloanz, J. et al. STUDIES ON THE ORGANIZATION AND STRUCTURE OF GENES AND ENZYMES OF PURINE SYNTHESIS IN ANIMALS AND MAN: 154. Pediatr Res 19, 769 (1985). https://doi.org/10.1203/00006450-198507000-00174
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DOI: https://doi.org/10.1203/00006450-198507000-00174