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Gene Review

CAR1  -  arginase

Saccharomyces cerevisiae S288c

Synonyms: Arginase, LPH15W, YPL111W
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Disease relevance of CAR1

  • Arginase activity was detected in Escherichia coli cells transformed with the plasmid carrying lambda hARG6 cDNA insert [1].
  • To facilitate investigation of the enzyme and gene structures and to elucidate the nature of the mutation in argininemia, we isolated cDNA clones for human liver arginase [1].
  • Arginine catabolism in the phototrophic bacterium Rhodobacter capsulatus E1F1. Purification and properties of arginase [2].

High impact information on CAR1

  • On the other hand, the cargA + Oh-1 and cargA + Oh-2 mutations, leading to a constitutive and mating-type dependent arginase synthesis, were identified as insertions [3].
  • This result suggests either a surprisingly large arginase regulatory region or an indirect influence of the Ty1 element on gene expression over long distances [3].
  • The nitrogen status for other nitrogen-responsive processes such as catabolic gene expression and sporulation also is signaled by this tRNA: mutant cells inappropriately induce the nitrogen-repressed gene CAR1 and undergo precocious sporulation in nitrogen-rich media [4].
  • The URS1-TRK2 sequence (5'-AGCCGCACG-3') shares six nucleotides with the ubiquitous URS1 element (5'-AGCCGCCGA-3'), and the protein species binding URS1-CAR1 (URSF) is capable of binding URS1-TRK2 in vitro [5].
  • This was not observed, however, when it was situated downstream of a heterologous CYC1 upstream activation sequence indicating that URS function is specifically neutralized by cis-acting elements associated with CAR1 induction [6].

Chemical compound and disease context of CAR1


Biological context of CAR1

  • The nucleotide sequence of this latter region is very similar to essential sequences within the URS elements from the yeast CAR1 and SSA1 genes, respectively [8].
  • The yeast UME6 gene product is required for transcriptional repression mediated by the CAR1 URS1 repressor binding site [9].
  • Arginase (CAR1) gene expression in Saccharomyces cerevisiae is induced by arginine [10].
  • Similar sequences situated upstream of ARG5,6 and ARG3 and reported to negatively regulate their expression are able to functionally substitute for the CAR1 UASI elements and mediate reporter gene expression [10].
  • The 5' regulatory region of CAR1 contains four separable regulatory elements--two inducer-independent upstream activation sequences (UASs) (UASC1 and UASC2), an inducer-dependent UAS (UASI), and an upstream repression sequence (URS1) which negatively regulates CAR1 and many other yeast genes [10].

Anatomical context of CAR1

  • We conclude that arginase deficiency in the red blood cells and probably in the liver is inherited in an autosomal recessive manner and is responsible for the clinical syndrome in this patient [11].
  • Arginase (EC and ornithine delta-aminotransferase (E.C. were found to reside in cytosol [12].
  • The CGH-1/CAR-1 interaction is conserved in Drosophila oocytes [13].
  • Here, we describe a predicted RNA-binding protein, CAR-1, that associates with CGH-1 and Y-box proteins within a conserved germline RNA-protein (RNP) complex, and in cytoplasmic particles in the gonad and early embryo [13].
  • We conclude that CAR-1 is of critical importance for oogenesis, that the association between CAR-1 and CGH-1 has been conserved, and that the regulation of physiological germ cell apoptosis is specifically influenced by certain functions of the CGH-1/CAR-1 RNP complex [13].

Associations of CAR1 with chemical compounds

  • A single URS1 site mediates repression of CAR1 arginine-independent upstream activator site (UAS) activity in the absence of arginine and the presence of a poor nitrogen source (a condition under which the inducer-independent Gln3p can function in association with the UASNTR sites) [14].
  • URS1 is known to be a repressor binding site in Saccharomyces cerevisiae that negatively regulates expression of many genes including CAR1 (arginase), several required for sporulation, mating type switching, inositol metabolism, and oxidative carbon metabolism [9].
  • We show that Gln3p activates CAR1 expression through the GATAA sequences in the absence of an optimal nitrogen source, such as ammonia, glutamine or asparagine [15].
  • Expression of the arginase (CAR1) gene in Saccharomyces cerevisiae is induced by arginine or its analog homoarginine [16].
  • First, the yeast strain was transformed with plasmid pCAT2 (delta car1 SMR1), and strains heterozygous for CAR1 gene were isolated on sulfometuron methyl plates [17].

Physical interactions of CAR1


Regulatory relationships of CAR1

  • Within this negative region a ten base-pair sequence was detected that shows high homology to a sequence located within a negative control region of the CYC1 gene and some homology to the negative control elements of the S. cerevisiae CAR1 and CAR2 genes [21].

Other interactions of CAR1

  • The products of three genes named CARGRI, CARGRII, and CARGRIII were shown to repress the expression of CAR1 and CAR2 genes, involved in arginine catabolism [22].
  • Participation of RAP1 protein in expression of the Saccharomyces cerevisiae arginase (CAR1) gene [23].
  • Similarly we have measured the mRNA levels for two genes subject to the arginine specific regulation: ARG3 and CAR1, the former gene belongs to the arginine anabolic pathway and the latter to the arginine catabolic one [24].
  • We demonstrate here that these gene products, along with that of the MCM1 gene, are required for the inducer-dependent USAI-A, UASI-B and UASI-C elements to function but they are not required for operation of inducer-independent CAR1 UASC1 or UASC2 [25].
  • CAR1 and YGP1 genes are not specifically induced under conditions of nitrogen starvation [26].

Analytical, diagnostic and therapeutic context of CAR1


  1. Molecular cloning and nucleotide sequence of cDNA for human liver arginase. Haraguchi, Y., Takiguchi, M., Amaya, Y., Kawamoto, S., Matsuda, I., Mori, M. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  2. Arginine catabolism in the phototrophic bacterium Rhodobacter capsulatus E1F1. Purification and properties of arginase. Moreno-Vivián, C., Soler, G., Castillo, F. Eur. J. Biochem. (1992) [Pubmed]
  3. Molecular cloning, DNA structure, and RNA analysis of the arginase gene in Saccharomyces cerevisiae. A study of cis-dominant regulatory mutations. Jauniaux, J.C., Dubois, E., Vissers, S., Crabeel, M., Wiame, J.M. EMBO J. (1982) [Pubmed]
  4. A yeast glutamine tRNA signals nitrogen status for regulation of dimorphic growth and sporulation. Murray, L.E., Rowley, N., Dawes, I.W., Johnston, G.C., Singer, R.A. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  5. Identification of essential nucleotides in an upstream repressing sequence of Saccharomyces cerevisiae by selection for increased expression of TRK2. Vidal, M., Buckley, A.M., Yohn, C., Hoeppner, D.J., Gaber, R.F. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  6. Ubiquitous upstream repression sequences control activation of the inducible arginase gene in yeast. Sumrada, R.A., Cooper, T.G. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  7. Chemical modification and inactivation of rat liver arginase by N-bromosuccinimide: reaction with His141. Daghigh, F., Cavalli, R.C., Soprano, D.R., Ash, D.E. Arch. Biochem. Biophys. (1996) [Pubmed]
  8. The upstream repression sequence from the yeast enolase gene ENO1 is a complex regulatory element that binds multiple trans-acting factors including REB1. Carmen, A.A., Holland, M.J. J. Biol. Chem. (1994) [Pubmed]
  9. The yeast UME6 gene product is required for transcriptional repression mediated by the CAR1 URS1 repressor binding site. Park, H.D., Luche, R.M., Cooper, T.G. Nucleic Acids Res. (1992) [Pubmed]
  10. Tripartite structure of the Saccharomyces cerevisiae arginase (CAR1) gene inducer-responsive upstream activation sequence. Viljoen, M., Kovari, L.Z., Kovari, I.A., Park, H.D., van Vuuren, H.J., Cooper, T.G. J. Bacteriol. (1992) [Pubmed]
  11. Hyperargininemia. Cederbaum, S.D., Shaw, K.N., Valente, M. J. Pediatr. (1977) [Pubmed]
  12. Intracellular localization of Aspergillus nidulans ornithine carbamoyltransferase in native host cells and in Saccharomyces cerevisiae cells harbouring its cloned structural gene. Maleszka, R., Dmochowska, A., Zaborowska, D., Cybis, J., Wegleński, P. Acta Biochim. Pol. (1986) [Pubmed]
  13. A conserved RNA-protein complex component involved in physiological germline apoptosis regulation in C. elegans. Boag, P.R., Nakamura, A., Blackwell, T.K. Development (2005) [Pubmed]
  14. Combinatorial regulation of the Saccharomyces cerevisiae CAR1 (arginase) promoter in response to multiple environmental signals. Smart, W.C., Coffman, J.A., Cooper, T.G. Mol. Cell. Biol. (1996) [Pubmed]
  15. Integration of the multiple controls regulating the expression of the arginase gene CAR1 of Saccharomyces cerevisiae in response to differentnitrogen signals: role of Gln3p, ArgRp-Mcm1p, and Ume6p. Dubois, E., Messenguy, F. Mol. Gen. Genet. (1997) [Pubmed]
  16. Multiple positive and negative cis-acting elements mediate induced arginase (CAR1) gene expression in Saccharomyces cerevisiae. Kovari, L., Sumrada, R., Kovari, I., Cooper, T.G. Mol. Cell. Biol. (1990) [Pubmed]
  17. Genetic engineering of a sake yeast producing no urea by successive disruption of arginase gene. Kitamoto, K., Oda, K., Gomi, K., Takahashi, K. Appl. Environ. Microbiol. (1991) [Pubmed]
  18. Genetic evidence for a role for MCM1 in the regulation of arginine metabolism in Saccharomyces cerevisiae. Messenguy, F., Dubois, E. Mol. Cell. Biol. (1993) [Pubmed]
  19. Participation of ABF-1 protein in expression of the Saccharomyces cerevisiae CAR1 gene. Kovari, L.Z., Cooper, T.G. J. Bacteriol. (1991) [Pubmed]
  20. L-Ornithine carbamoyltransferase from Saccharomyces cerevisiae: steady-state kinetic analysis. Simon, J.P., Stalon, V. Eur. J. Biochem. (1977) [Pubmed]
  21. Heme control region of the catalase T gene of the yeast Saccharomyces cerevisiae. Spevak, W., Hartig, A., Meindl, P., Ruis, H. Mol. Gen. Genet. (1986) [Pubmed]
  22. In Saccharomyces cerevisiae, expression of arginine catabolic genes CAR1 and CAR2 in response to exogenous nitrogen availability is mediated by the Ume6 (CargRI)-Sin3 (CargRII)-Rpd3 (CargRIII) complex. Messenguy, F., Vierendeels, F., Scherens, B., Dubois, E. J. Bacteriol. (2000) [Pubmed]
  23. Participation of RAP1 protein in expression of the Saccharomyces cerevisiae arginase (CAR1) gene. Kovari, L.Z., Kovari, I., Cooper, T.G. J. Bacteriol. (1993) [Pubmed]
  24. Participation of transcriptional and post-transcriptional regulatory mechanisms in the control of arginine metabolism in yeast. Messenguy, F., Dubois, E. Mol. Gen. Genet. (1983) [Pubmed]
  25. Analysis of the inducer-responsive CAR1 upstream activation sequence (UASI) and the factors required for its operation. Kovari, L.Z., Fourie, M., Park, H.D., Kovari, I.A., Van Vuuren, H.J., Cooper, T.G. Yeast (1993) [Pubmed]
  26. Arginase activity is a useful marker of nitrogen limitation during alcoholic fermentations. Carrasco, P., Pérez-Ortín, J.E., del Olmo, M. Syst. Appl. Microbiol. (2003) [Pubmed]
  27. Antisense-mediated inhibition of arginase (CAR1) gene expression in Saccharomyces cerevisiae. Park, H., Shin, M., Woo, I. J. Biosci. Bioeng. (2001) [Pubmed]
  28. Regulation of arginine metabolism in Saccharomyces cerevisiae. Association of arginase and ornithine transcarbamoylase. Eisenstein, E., Duong, L.T., Ornberg, R.L., Osborne, J.C., Hensley, P. J. Biol. Chem. (1986) [Pubmed]
  29. The quaternary structure of ornithine transcarbamoylase and arginase from Saccharomyces cerevisiae. Duong, L.T., Eisenstein, E., Green, S.M., Ornberg, R.L., Hensley, P. J. Biol. Chem. (1986) [Pubmed]
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