Nucleotide sequence of cDNA and predicted amino acid sequence of rat liver uricase

Ito, Masaki; Suzuki, Masami; Takagi, Yasuyuki

doi:10.1111/j.1432-1033.1988.tb14021.x

Cited by 21 publications

(6 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In this report we present the full-length sequence of pig urate oxidase cDNA and describe the isolation and characterization of two other urate oxidase cDNAs from mouse and baboon. ¶ We have analyzed in detail the urate oxidase sequence differences between these species and clarified the differences in the rat sequences previously reported by others (12)(13)(14) (16). Antiserum against pig liver urate oxidase was raised in goat (100 ,gg of the purified protein per injection) as described by Warr (17).…”

mentioning

confidence: 75%

“…The sequences we present here contain the same open reading frame and approximately 90% sequence identity with the rat sequence recently reported by Reddy et al (12). This suggests that the substantial sequence differences between various published rat urate oxidase sequences is likely due to sequencing errors that result in frame shifts and shortened open reading frames (13,14).…”

Section: Discussionmentioning

confidence: 99%

“…These results have recently been confirmed by another group (12). The cDNA sequence of rat urate oxidase has recently been reported by three different groups (12)(13)(14); however, there are substantial differences in the published sequences. In this report we present the full-length sequence of pig urate oxidase cDNA and describe the isolation and characterization of two other urate oxidase cDNAs from mouse and baboon.…”

mentioning

confidence: 99%

See 2 more Smart Citations

Urate oxidase: primary structure and evolutionary implications.

Lee

Muzny

et al. 1989

Proc. Natl. Acad. Sci. U.S.A.

300

213

View full text Add to dashboard Cite

Urate oxidase, or uricase (EC 1.7.3.3), is a peroxisomal enzyme that catalyzes the oxidation of uric acid to allantoin in most mammals. In humans and certain other primates, however, the enzyme has been lost by some unknown mechanism. To identify the molecular basis for this loss, urate oxidase cDNA clones were isolated from pig, mouse, and baboon, and their DNA sequences were determined. The mouse urate oxidase open reading frame encodes a 303-amino acid polypeptide, while the pig and baboon urate oxidase cDNAs encode a 304-amino acid polypeptide due to a single codon deletion/insertion event. The authenticity of this single additional codon was confirmed by sequencing the mouse and pig genomic copies of the gene. The urate oxidase sequence contains a domain similar to the type 2 copper binding motif found in other copper binding proteins, suggesting that the copper ion in urate oxidase is coordinated as a type 2 structure. Based upon a comparison of the NH2-terminal peptide and deduced sequences, we propose that the maturation of pig urate oxidase involves the posttranslational cleavage of a six-amino acid peptide. Two nonsense mutations were found in the human urate oxidase gene, which confirms, at the molecular level, that the urate oxidase gene in humans is nonfunctional. The sequence comparisons favor the hypothesis that the loss of urate oxidase in humans is due to a sudden mutational event rather than a progressive mutational process.

show abstract

mentioning

confidence: 75%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Urate oxidase: primary structure and evolutionary implications.

Lee

Muzny

et al. 1989

Proc. Natl. Acad. Sci. U.S.A.

300

213

View full text Add to dashboard Cite

show abstract

“…To obtain full-length cDNA clones, approximately 100000 transformants were screened through hybridization with a 3ZP-labeled cDNA fragment (EcoRI-NcoI) of pURCl (Ito et al, 1988) by the random-primer labeling method. 24 positive clones were isolated and analyzed by digestion with restriction enzymes.…”

Section: Cloning Of Rat Liver Urate Oxidasementioning

confidence: 99%

Urate oxidase is imported into peroxisomes recognizing the C‐terminal SKL motif of proteins

Miura

Oda

Funai

et al. 1994

European Journal of Biochemistry

Self Cite

View full text Add to dashboard Cite

Rat liver urate oxidase synthesized from cDNA through coupled transcription and translation was incubated at 26°C for 60 min with purified peroxisomes from rat liver. Urate oxidase was efficiently imported into the peroxisomes, as determined by resistance to externally added proteinase K. The amount of imported urate oxidase increased with time and the import was temperature dependent. A synthetic peptide composed of the C-terminal 10 amino acid residues of acyl-CoA oxidase (the C-terminal tripeptide is Ser-Lys-Leu) inhibited the import of urate oxidase, whereas other peptides, in which the C-terminal Ser-Lys-Leu (SKL) sequence was deleted or mutated, were not effective. Two mutant urate oxidase proteins in which the C-terminal Ser-Arg-Leu (SRL) sequence was deleted or mutated to Ser-Glu-Leu (SEL) were not imported into peroxisomes. With substitution of a lysine residue for arginine in the SRL tripeptide at the C-terminus the import activity was retained. These results show that urate oxidase is imported into peroxisomes via a common pathway with acyl-CoA oxidase, and that the C-terminal SRL sequence functions as a Among peroxisomal-targeting signal.

show abstract

“…The single-letter amino acid code is used. Three deduced amino acid sequences for rat UO have been reported which differ from one another at the amino and carboxy termini (33,57,70). In this figure, the deduced rat UO sequence from Reddy et al (70) that is primed by P1 and gives rise to the 158-nucleotide extension product.…”

mentioning

confidence: 99%

Molecular characterization of the Drosophila melanogaster urate oxidase gene, an ecdysone-repressible gene expressed only in the malpighian tubules.

Wallrath¹,

Burnett²,

Friedman³

1990

Mol. Cell. Biol.

View full text Add to dashboard Cite

The urate oxidase (UO) gene of Drosophila melanogaster is expressed during the third-instar larval and adult stages, exclusively within a subset of cells of the Malpighian tubules. The UO gene contains a 69-base-pair intron and encodes mature mRNAs of 1,224, 1,227, and 1,244 nucleotides, depending on the site of 3' endonucleolytic cleavage prior to polyadenylation. A direct repeat, 5'-AAGTGAGAGTGAT-3', is the proposed cis-regulatory element involved in 20-hydroxyecdysone repression of the UO gene. The deduced amino acid sequences of UO of D. melanogaster, rat, mouse, and pig and uricase II of soybean show 32 to 38% identity, with 22% of amino acid residues identical in all six species. With use of P-element-mediated germ line transformation, 826 base pairs 5' and approximately 1,200 base pairs 3' of the D. melanogaster UO transcribed region contain all of the cis elements allowing for appropriate temporal regulation and Malpighian tubule-specific expression of the UO gene.In Drosophila melanogaster, particular purines serve as precursors of nucleotides and pterins (35,62). Excess purine is converted to uric acid, which is either stored, excreted, or catabolized, depending on the developmental stage. Uric acid in the third-instar larva and adult is converted by urate oxidase (UO) to allantoin and then excreted by the Malpighian tubules (19,40). The gene encoding UO is transcribed exclusively within the cells of the Malpighian tubules. UO mRNA is not detected by Northern (RNA) analysis until the beginning of the third-instar larval stage; by the middle of this stage, UO mRNA represents approximately 1% of the total poly(A)+ RNA of the Malpighian tubules (40). By the end of the third-instar larval stage, UO mRNA and UO protein abruptly disappear in response to a rising concentration of the steroid hormone 20-hydroxyecdysone (41). The UO gene remains transcriptionally inactive from the late-third instar larval stage through the pupal stage, with UO mRNA reappearing exclusively within the Malpighian tubules after emergence of the adult (40).Though the molecular mechanisms are unknown, two experimentally distinguishable phenomena are involved in this reactivation of transcription of the UO gene in the adult: a UO-inducing factor in the hemolymph and an autonomous clock-like mechanism in the Malpighian tubules. The UOinducing factor was first detected in xanthine dehydrogenase-deficient Drosophila, strains ry2 (3-52.0; 24) and ma-i (1-64.8; 9), which have 5-to 10-fold-higher levels of UO mRNA and UO protein in the adult than in the wild-type adult. High levels of UO-inducing factor in the hemolymph of a xanthine dehydrogenase-deficient adult stimulated a 5-to 10-fold increase in UO activity in a wild-type Malpighian tubule transplanted into the abdomen of a xanthine dehydrogenase-deficient adult (19,21,41

show abstract

Nucleotide sequence of cDNA and predicted amino acid sequence of rat liver uricase

Cited by 21 publications

References 31 publications

Urate oxidase: primary structure and evolutionary implications.

Urate oxidase: primary structure and evolutionary implications.

Urate oxidase is imported into peroxisomes recognizing the C‐terminal SKL motif of proteins

Molecular characterization of the Drosophila melanogaster urate oxidase gene, an ecdysone-repressible gene expressed only in the malpighian tubules.

Contact Info

Product

Resources

About