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Gene Review

CPA1  -  carbamoyl-phosphate synthase (glutamine...

Saccharomyces cerevisiae S288c

Synonyms: Arginine-specific carbamoyl-phosphate synthetase, glutamine chain, CPS-A, Carbamoyl-phosphate synthase arginine-specific small chain, YOR303W
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Disease relevance of CPA1

  • The protein sequence data provide strong evidence that the carbamyl phosphate synthetase I gene of rat, the carAB gene of E. coli, and the CPA1 and CPA2 genes of yeast were derived from common ancestral genes [1].

High impact information on CPA1


Biological context of CPA1

  • In strains overproducing GCN4 protein, the translational control completely overrode transcriptional activation of CPA1 by general amino acid control [6].
  • The observed increase was GCN4 dependent and was genetically separable from arginine-specific repression of CPA1 mRNA translation [6].
  • The nucleotide sequence of a 2.2-kilobase region of the DNA insert carrying the CPA1 gene has been determined [7].
  • The yeast gene CPA1 coding for the small subunit of arginine-specific carbamyl phosphate synthetase has been cloned by complementation of a cpa 1 mutant with a plasmid library of total yeast chromosomal DNA [7].
  • An important new finding illustrated by ARG1 and CPA1, is that contrary to what all the previous data suggested, repression can be mediated by ARC elements located far upstream of the TATA-box [8].

Anatomical context of CPA1

  • In contrast, for mRNA containing the CPA1 uORF, ribosomes reached the downstream start codon by scanning past the uORF [5].

Associations of CPA1 with chemical compounds

  • Arginine deprivation imposed by PALO also caused increased expression of CPA1 and CPA2, coding respectively for the small and large subunits of arginine-specific carbamyl-phosphate synthetase [6].
  • Although differences exist in AAP sequence, there were three absolutely conserved amino acid residues in the predicted peptide, including an aspartic acid crucial for arginine-dependent regulation of arg-2 and CPA1 [9].
  • Finally, we have found that the CPS-A antiserum also cross-reacts with carbamoyl-phosphate synthetases from bacteria, yeast, and mammals [10].

Physical interactions of CPA1

  • Our results indicate that the NMD destabilizes the 5' end of the CPA1 message and this decay is strongly enhanced when arginine is present in the growth medium [11].

Other interactions of CPA1

  • For 53 genes, including GCN4, CPA1, and ICY2, three genes for which translational control is known to play a key role in regulation, most mRNA molecules were associated with a single ribosome [12].
  • Similarly, the behavior of fusions of the leader sequence of CPA1 with those of ARG4 or GAL10 confirmed that the regions of this leader located upstream and downstream from the uORF are dispensable for the regulation by arginine [13].
  • Two of these correspond to previously known genes (CPA1, SLY41), whereas 15 correspond to new genes [14].
  • A similar analysis of expression of the gene CPA1, for which a translational regulation by arginine has been clearly demonstrated (M. Werner, A. Feller, F. Messenguy, and A. Piérard, Cell 49:805-813, 1987), indicates that this gene is also partly regulated at the transcriptional level by the ARGR repressor system [15].
  • The MIP1 gene was cloned by genetic complementation of the mip1-1 allele after cell transformation with a yeast genomic library and was mapped to the right arm of chromosome XV about 20 centimorgans distal to the cpa1 gene by Southern blot hybridization and tetrad analysis [16].

Analytical, diagnostic and therapeutic context of CPA1

  • Oligonucleotide site-directed mutagenesis of this uORF as well as sequencing of constitutive cis-dominant mutations has suggested that the leader peptide product of the CPA1 uORF is an essential negative element for repression of the CPA1 gene by arginine [13].


  1. Characterization and derivation of the gene coding for mitochondrial carbamyl phosphate synthetase I of rat. Nyunoya, H., Broglie, K.E., Widgren, E.E., Lusty, C.J. J. Biol. Chem. (1985) [Pubmed]
  2. The RNA binding protein Pub1 modulates the stability of transcripts containing upstream open reading frames. Ruiz-Echevarría, M.J., Peltz, S.W. Cell (2000) [Pubmed]
  3. The leader peptide of yeast gene CPA1 is essential for the translational repression of its expression. Werner, M., Feller, A., Messenguy, F., Piérard, A. Cell (1987) [Pubmed]
  4. Ribosome occupancy of the yeast CPA1 upstream open reading frame termination codon modulates nonsense-mediated mRNA decay. Gaba, A., Jacobson, A., Sachs, M.S. Mol. Cell (2005) [Pubmed]
  5. Physical evidence for distinct mechanisms of translational control by upstream open reading frames. Gaba, A., Wang, Z., Krishnamoorthy, T., Hinnebusch, A.G., Sachs, M.S. EMBO J. (2001) [Pubmed]
  6. Arginine restriction induced by delta-N-(phosphonacetyl)-L-ornithine signals increased expression of HIS3, TRP5, CPA1, and CPA2 in Saccharomyces cerevisiae. Kinney, D.M., Lusty, C.J. Mol. Cell. Biol. (1989) [Pubmed]
  7. Sequence of the small subunit of yeast carbamyl phosphate synthetase and identification of its catalytic domain. Nyunoya, H., Lusty, C.J. J. Biol. Chem. (1984) [Pubmed]
  8. Further definition of the sequence and position requirements of the arginine control element that mediates repression and induction by arginine in Saccharomyces cerevisiae. Crabeel, M., de Rijcke, M., Seneca, S., Heimberg, H., Pfeiffer, I., Matisova, A. Yeast (1995) [Pubmed]
  9. Evolutionary changes in the fungal carbamoyl-phosphate synthetase small subunit gene and its associated upstream open reading frame. Hood, H.M., Spevak, C.C., Sachs, M.S. Fungal Genet. Biol. (2007) [Pubmed]
  10. Carbamoyl-phosphate synthetases from Neurospora crassa. Immunological relatedness of the enzymes from Neurospora, bacteria, yeast, and mammals. Ness, S.A., Weiss, R.L. J. Biol. Chem. (1985) [Pubmed]
  11. Role of RNA surveillance proteins Upf1/CpaR, Upf2 and Upf3 in the translational regulation of yeast CPA1 gene. Messenguy, F., Vierendeels, F., Piérard, A., Delbecq, P. Curr. Genet. (2002) [Pubmed]
  12. Genome-wide analysis of mRNA translation profiles in Saccharomyces cerevisiae. Arava, Y., Wang, Y., Storey, J.D., Liu, C.L., Brown, P.O., Herschlag, D. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  13. A segment of mRNA encoding the leader peptide of the CPA1 gene confers repression by arginine on a heterologous yeast gene transcript. Delbecq, P., Werner, M., Feller, A., Filipkowski, R.K., Messenguy, F., Piérard, A. Mol. Cell. Biol. (1994) [Pubmed]
  14. Sequence and analysis of a 36.2 kb fragment from the right arm of yeast chromosome XV reveals 19 open reading frames including SNF2 (5' end), CPA1, SLY41, a putative transport ATPase, a putative ribosomal protein and an SNF2 homologue. Poirey, R., Cziepluch, C., Tobiasch, E., Pujol, A., Kordes, E., Jauniaux, J.C. Yeast (1997) [Pubmed]
  15. Arginine-specific repression in Saccharomyces cerevisiae: kinetic data on ARG1 and ARG3 mRNA transcription and stability support a transcriptional control mechanism. Crabeel, M., Lavalle, R., Glansdorff, N. Mol. Cell. Biol. (1990) [Pubmed]
  16. Cloning and sequencing of the nuclear gene MIP1 encoding the catalytic subunit of the yeast mitochondrial DNA polymerase. Foury, F. J. Biol. Chem. (1989) [Pubmed]
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