Identification of the ureidoglycolate hydrolase gene in the DAL gene cluster of Saccharomyces cerevisiae.

Yoo, Hyang–Sook; Genbauffe, F S; Cooper, Terrance G.

doi:10.1128/mcb.5.9.2279

Cited by 61 publications

(77 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Southern blot analysis and radioactive labeling of DNA fragments by nick translation and the T4 polynucleotide kinase reaction were performed by previously published techniques (43 (MET8) and "walking down the chromosome" to the DURI,2 locus by integration-excision techniques (41). Implementation of this strategy began with isolation of plasmids that were able to complement a met8 mutation contained in strain M1014-lc.…”

mentioning

confidence: 99%

Induction and repression of the urea amidolyase gene in Saccharomyces cerevisiae.

Genbauffe¹,

Cooper²

1986

Mol. Cell. Biol.

Self Cite

View full text Add to dashboard Cite

The DUR1,2 gene from Saccharomyces cerevisiae has been isolated on recombinant plasmids along with all DNA between the DURI,2 and MET8 loci. DUR1,2 was found to encode a 5.7-kilobase transcript, which is consistent with our earlier suggestion that the DURi and DUR2 loci are two domains of a single multifunctional gene. Steady-state levels of the DUR1,2 transcript responded to induction and nitrogen catabolite repression in the same way as urea amidolyase activity. da)81 mutants (grown with inducer) contained barely detectable amounts of DURI,2 RNA, whereas dal80 mutants (grown without inducer) contained the same amount as a wild-type induced culture. These observations support our earlier hypothesis that DUR1,2 is transcriptionally regulated, with control being mediated by the DAL80 and DAL8I gene products. We cloned the DUR1,2_Oh mutation and found it to be a Ty insertion near sequences required for complementation of durl,2 mutations.The ROAM phenotype of the DUR1,2_Oh mutation is sharply different from that of cis-dominant, DUR80 mutations, which enhance DUR1,2 expression but do not affect the normal control pattern of the gene. There is evidence that DUR80 mutations may also be Ty insertions, which generate phenotypes that are different from those in DUR1,2-Oh mutations.An appreciation for the molecular mechanisms involved in control and integration of procaryotic metabolic pathways has been gained by studying regulons with widely differing physiological functions (28, 31). Similar information is now beginning to accumulate for eucaryotic systems (42). Nitrogen catabolic systems are particularly useful for such investigations, because most are subject to multiple layers of regulation. Genes encoding the allantoin-degradative system in Saccharomyces cerevisiae, for example, respond to both induction and nitrogen catabolite repression (15,25,38 its 3-min half-life after the addition of asparagine to the medium (12). In contrast, enzyme activity is not lost after the addition of a repressive nitrogen source, but continued enzyme synthesis ceases (12). The lack of enzyme induction does not result from inducer exclusion, because daI80 mutants, which do not require the presence of an inducer for enzyme production, are similarly devoid of allantoindegrading enzymes when grown in glucose-asparagine medium (8).Earlier kinetic studies are consistent with the hypothesis that both induction and nitrogen catabolite repression are exerted at gene expression (1-4, 16, 24-26

show abstract

mentioning

confidence: 99%

Induction and repression of the urea amidolyase gene in Saccharomyces cerevisiae.

Genbauffe¹,

Cooper²

1986

Mol. Cell. Biol.

Self Cite

View full text Add to dashboard Cite

show abstract

“…Expression of several allantoin pathway genes (DAL4, DAL7, and DUR1,2) in Saccharomyces cerevisiae increases 10-to 20-fold when compounds that can be degraded to the inducer, allophanate, are added to the culture medium (4,10,36,39). A similar response is caused by the gratuitous inducer oxalurate (30).…”

mentioning

confidence: 66%

“…A similar response is caused by the gratuitous inducer oxalurate (30). In contrast, when cells are provided with a readily used nitrogen source, such as asparagine or glutamine, mRNA levels drop precipitously whether or not inducer is present, a phenomenon termed nitrogen catabolite repression (4,10,25,36,39). cis-acting elements required for basal-level gene expression, response to inducer, and nitrogen catabolite repression have been shown to be situated upstream of the inducible DAL7 transcribed sequences, suggesting that regulation of the gene occurs at transcription (38).…”

mentioning

confidence: 99%

See 1 more Smart Citation

DAL82, a second gene required for induction of allantoin system gene transcription in Saccharomyces cerevisiae

1991

Self Cite

View full text Add to dashboard Cite

Several highly inducible enzyme activities are required for the degradation of allantoin in Saccharomyces cerevisiae. Induction of these pathway enzymes has been shown to be regulated at transcription, and response to inducer is lost in dal81 and dal82/durM mutants. The similar phenotypes generated by da)81 and dal82 mutations prompted the question of whether they were allelic. We demonstrated that the DAL81 and DAL82 loci are distinct, unlinked genes situated on chromosomes IX and XIV. DAL82 gene expression did not respond to induction by the allantoin pathway inducer or to nitrogen catabolite repression. Expression was also not significantly affected by mutation of the daI80 locus. From the nucleotide sequence of the DAL82 gene, we deduced that it encodes a protein with a mass of 29,079 Da that may possess the structural motifs expected of a regulatory protein. This protein was shown to be required for the function mediated by the cis-acting upstream induction sequence situated in the 5'-flanking regions of the inducible allantoin pathway genes.

show abstract

“…The yeast allantoicase gene DAL2 codes for a 345-amino acid protein (1)(2)(3). Expression of the allantoin pathway enzymes is (i) induced by allophanate, (ii) sensitive to nitrogen catabolite repression, and (iii) responsive to mutation of the DAL80 and DAL81 loci, which have been shown to regulate the allantoin degradation system (4,5).…”

mentioning

confidence: 99%

Crystal Structure of Yeast Allantoicase Reveals a Repeated Jelly Roll Motif

Leulliot

Quevillon‐Chéruel

Sorel

et al. 2004

Journal of Biological Chemistry

View full text Add to dashboard Cite

Allantoicase (EC 3.5.3.4) catalyzes the conversion of allantoate into ureidoglycolate and urea, one of the final steps in the degradation of purines to urea. The mechanism of most enzymes involved in this pathway, which has been known for a long time, is unknown. In this paper we describe the three-dimensional crystal structure of the yeast allantoicase determined at a resolution of 2.6 Å by single anomalous diffraction. This constitutes the first structure for an enzyme of this pathway. The structure reveals a repeated jelly roll ␤-sheet motif, also present in proteins of unrelated biochemical function. Allantoicase has a hexameric arrangement in the crystal (dimer of trimers). Analysis of the protein sequence against the structural data reveals the presence of two totally conserved surface patches, one on each jelly roll motif. The hexameric packing concentrates these patches into conserved pockets that probably constitute the active site.

show abstract

Identification of the ureidoglycolate hydrolase gene in the DAL gene cluster of Saccharomyces cerevisiae.

Cited by 61 publications

References 30 publications

Induction and repression of the urea amidolyase gene in Saccharomyces cerevisiae.

Induction and repression of the urea amidolyase gene in Saccharomyces cerevisiae.

DAL82, a second gene required for induction of allantoin system gene transcription in Saccharomyces cerevisiae

Crystal Structure of Yeast Allantoicase Reveals a Repeated Jelly Roll Motif

Contact Info

Product

Resources

About