High impact information on PRS1

• PPS1 was isolated and shown to be a previously undescribed gene coding for a protein similar in amino acid sequence to phosphoribosylpyrophosphate synthase, a rate-limiting enzyme in the biosynthesis of nucleotides, histidine, and tryptophan [1].
• These apparent conflicting results indicate that, apart from the PRS1 PRS3-specified enzyme, PRS-specified enzyme is functional in vivo but unstable when released from the cell [2].
• Interestingly, the prp1+ gene was found to be identical with the zer1+ gene that functions in cell cycle control [3].
• The transcription initiation site of the Saccharomyces cerevisiae PRS1 gene was mapped at -179 bp [4].
• Phosphoribosyl-pyrophosphate synthetase (Prs) catalyses the synthesis of phosphoribosyl pyrophosphate (PRPP), an intermediate in nucleotide metabolism and the biosynthesis of the amino acids histidine and tryptophan [5].

Biological context of PRS1

• The Saccharomyces cerevisiae genome contains a family of five PRS genes, PRS1-PRS5 [5].
• Heterozygotes in PRS1 produced approximately 35% less PRPP synthetase (P = 0.0004) and exhibited a similar reduction in transcript levels [6].
• While no role in morphogenesis is elucidated by this work, the data strongly suggests that PRS1 is an essential gene in C. albicans and supports earlier results that indicated the presence of a single PRS gene in C. albicans [6].

Anatomical context of PRS1

• Using anti-peptide antisera directed against two different epitopes of Prs1p it was shown that Prs1p localizes to granular cytoplasmic structures [5].

Other interactions of PRS1

• A FASTA search indicated that the C. albicans PRS (Ca PRS1) had an overall homology at the amino acid level of 91% with the S. cerevisiae PRS3 [7].

Analytical, diagnostic and therapeutic context of PRS1

• Confirmation of a heterozygous, single disruption in PRS1 was obtained by I-SceI digestion of chromosomal-sized DNA and Southern blot hybridizations [6].

References