ABSTRACT
We show that the allantoin transport system of Saccharomyces cerevisiae responds to two induction systems, one mediated by allophanate or its analog oxalurate and the other mediated by allantoin or its analog hydantoin acetate. The effects of the two inducers were additive in strain M85. Like other allantoin pathway genes, oxalurate-mediated induction of allantoin transport required a functional DAL81 gene product. Hydantoin acetate-mediated induction of the system, on the other hand, occurred normally in dal81 mutants. This suggests that induction was not only mediated by two separate inducers, but also involved different regulatory proteins. Induction is probably a transcriptionally regulated process, because addition of hydantoin acetate or oxalurate to the culture medium increased the steady-state levels of mRNA encoded by a gene required for allantoin transport (DAL4).
Subject(s)
Allantoin/metabolism , Saccharomyces cerevisiae/metabolism , Biological Transport, Active/drug effects , Chemical Phenomena , Chemistry , DNA Restriction Enzymes , Gene Expression Regulation , Genes, Fungal , Genetic Complementation Test , Hydantoins/metabolism , Hydantoins/pharmacology , Mutation , Nucleic Acid Hybridization , Oxamic Acid/analogs & derivatives , Oxamic Acid/metabolism , Oxamic Acid/pharmacology , Plasmids , RNA, Fungal/analysis , RNA, Fungal/metabolism , RNA, Messenger/analysis , RNA, Messenger/metabolism , Saccharomyces cerevisiae/geneticsABSTRACT
Accumulation of intracellular allantoin and allantoate is mediated by two distinct active transport systems in Saccharomyces cerevisiae. Allantoin transport (DAL4 gene) is inducible, while allantoate uptake is constitutive (it occurs at full levels in the absence of any allantoate-related compounds from the culture medium). Both systems appear to be sensitive to nitrogen catabolite repression, feedback inhibition, and trans-inhibition. Mutants (dal5) that lack allantoate transport have been isolated. These strains also exhibit a 60% loss of allantoin transport capability. Conversely, dal4 mutants previously described are unable to transport allantoin and exhibit a 50% loss of allantoate transport. We interpret the pleiotropic behavior of the dal4 and dal5 mutations as deriving from a functional interaction between elements of the two transport systems.