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CAD1  -  glutathione gamma-glutamylcysteinyltransfe...

Arabidopsis thaliana

Synonyms: ARA8, ARABIDOPSIS THALIANA PHYTOCHELATIN SYNTHASE 1, ATPCS1, CADMIUM SENSITIVE 1, MRH10.18, ...
 
 
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Disease relevance of CAD1

 

High impact information on CAD1

  • On the basis of these properties and the sufficiency of immunoaffinity-purified epitope-tagged AtPCS1 polypeptide for high rates of Cd2+-activated phytochelatin synthesis from glutathione in vitro, AtPCS1 is concluded to encode the enzyme phytochelatin synthase [4].
  • Phytochelatin synthase, a dipeptidyltransferase that undergoes multisite acylation with gamma-glutamylcysteine during catalysis: stoichiometric and site-directed mutagenic analysis of arabidopsis thaliana PCS1-catalyzed phytochelatin synthesis [5].
  • Domain organization of phytochelatin synthase: functional properties of truncated enzyme species identified by limited proteolysis [6].
  • It is generally believed, however, that the active site region is located in the more conserved N-terminal portion of PCS, whereas various, as yet unidentified (but supposedly less critical) roles have been proposed for the C-terminal region [6].
  • The dependence of phytochelatin synthase (gamma-glutamylcysteine dipeptidyltranspeptidase (PCS), EC ) on heavy metals for activity has invariably been interpreted in terms of direct metal binding to the enzyme [7].
 

Biological context of CAD1

  • Tissue specific expression of CAD 1, B1, and G genes was determined using their promoters fused to the GUS reporter gene [8].
  • The CAD1 gene, which encodes a protein containing a domain with significant homology to the MACPF (membrane attach complex and perforin) domain of complement components and perforin, is likely to control plant immunity negatively and has a W-box cis-element in its promoter region [9].
  • When AtPCS1 was overexpressed in Arabidopsis from a strong constitutive Arabidopsis actin regulatory sequence (A2), the A2::AtPCS1 plants were highly resistant to arsenic, accumulating 20-100 times more biomass on 250 and 300 microM arsenate than wild type (WT); however, they were hypersensitive to Cd(II) [2].
  • We therefore conclude that the CAD1 protein negatively controls the SA-mediated pathway of programmed cell death in plant immunity [10].
  • Cloning of CAD1 reveals that this gene encodes a protein containing a domain with significant homology to the MACPF (membrane attack complex and perforin) domain of complement components and perforin proteins that are involved in innate immunity in animals [10].
 

Anatomical context of CAD1

  • The Arabidopsis gene CAD1 controls programmed cell death in the plant immune system and encodes a protein containing a MACPF domain [10].
  • Vacuolar sequestration of the conjugate was very fast and outcompeted carboxypeptidation to the gamma-glutamylcysteine-bimane intermediate (gamma-EC-B) by phytochelatin synthase (PCS) in the cytosol [11].
  • These results are discussed in relation to heavy metal trafficking pathways in higher plants and to the interest of using plastid expression of PCS for biotechnological applications [12].
 

Associations of CAD1 with chemical compounds

  • The locations of these MT genes are different from that of CAD1, a gene involved in cadmium tolerance in Arabidopsis [13].
  • The CAD1 expression promoted by BTH and the chitin elicitor was not suppressed in the npr1 mutant, which is insensitive to SA signaling [9].
  • Salicylic Acid and a Chitin Elicitor Both Control Expression of the CAD1 Gene Involved in the Plant Immunity of Arabidopsis [9].
  • We found that expression of the CAD1 gene and other W-box containing genes, such as NPR1 and PR2, was promoted by salicylic acid (SA) and benzothiadiazole (BTH) as a SA agonist [9].
  • Cd(2+) tolerance in cultured rolB roots was increased as a result of overexpression of AtPCS1, and further enhanced when reduced glutathione (GSH, the substrate of PCS1) was added to the culture medium [1].
 

Other interactions of CAD1

 

Analytical, diagnostic and therapeutic context of CAD1

References

  1. Overexpression of Arabidopsis phytochelatin synthase in tobacco plants enhances Cd(2+) tolerance and accumulation but not translocation to the shoot. Pomponi, M., Censi, V., Di Girolamo, V., De Paolis, A., di Toppi, L.S., Aromolo, R., Costantino, P., Cardarelli, M. Planta (2006) [Pubmed]
  2. Overexpression of phytochelatin synthase in Arabidopsis leads to enhanced arsenic tolerance and cadmium hypersensitivity. Li, Y., Dhankher, O.P., Carreira, L., Lee, D., Chen, A., Schroeder, J.I., Balish, R.S., Meagher, R.B. Plant Cell Physiol. (2004) [Pubmed]
  3. Enhancing the tolerance of zebrafish (Danio rerio) to heavy metal toxicity by the expression of plant phytochelatin synthase. Konishi, T., Matsumoto, S., Tsuruwaka, Y., Shiraki, K., Hirata, K., Tamaru, Y., Takagi, M. J. Biotechnol. (2006) [Pubmed]
  4. AtPCS1, a phytochelatin synthase from Arabidopsis: isolation and in vitro reconstitution. Vatamaniuk, O.K., Mari, S., Lu, Y.P., Rea, P.A. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  5. Phytochelatin synthase, a dipeptidyltransferase that undergoes multisite acylation with gamma-glutamylcysteine during catalysis: stoichiometric and site-directed mutagenic analysis of arabidopsis thaliana PCS1-catalyzed phytochelatin synthesis. Vatamaniuk, O.K., Mari, S., Lang, A., Chalasani, S., Demkiv, L.O., Rea, P.A. J. Biol. Chem. (2004) [Pubmed]
  6. Domain organization of phytochelatin synthase: functional properties of truncated enzyme species identified by limited proteolysis. Ruotolo, R., Peracchi, A., Bolchi, A., Infusini, G., Amoresano, A., Ottonello, S. J. Biol. Chem. (2004) [Pubmed]
  7. Mechanism of heavy metal ion activation of phytochelatin (PC) synthase: blocked thiols are sufficient for PC synthase-catalyzed transpeptidation of glutathione and related thiol peptides. Vatamaniuk, O.K., Mari, S., Lu, Y.P., Rea, P.A. J. Biol. Chem. (2000) [Pubmed]
  8. Evidence for a role of AtCAD 1 in lignification of elongating stems of Arabidopsis thaliana. Eudes, A., Pollet, B., Sibout, R., Do, C.T., S??guin, A., Lapierre, C., Jouanin, L. Planta (2006) [Pubmed]
  9. Salicylic Acid and a Chitin Elicitor Both Control Expression of the CAD1 Gene Involved in the Plant Immunity of Arabidopsis. Tsutsui, T., Morita-Yamamuro, C., Asada, Y., Minami, E., Shibuya, N., Ikeda, A., Yamaguchi, J. Biosci. Biotechnol. Biochem. (2006) [Pubmed]
  10. The Arabidopsis gene CAD1 controls programmed cell death in the plant immune system and encodes a protein containing a MACPF domain. Morita-Yamamuro, C., Tsutsui, T., Sato, M., Yoshioka, H., Tamaoki, M., Ogawa, D., Matsuura, H., Yoshihara, T., Ikeda, A., Uyeda, I., Yamaguchi, J. Plant Cell Physiol. (2005) [Pubmed]
  11. Vacuolar sequestration of glutathione S-conjugates outcompetes a possible degradation of the glutathione moiety by phytochelatin synthase. Grzam, A., Tennstedt, P., Clemens, S., Hell, R., Meyer, A.J. FEBS Lett. (2006) [Pubmed]
  12. Chloroplast targeting of phytochelatin synthase in Arabidopsis: effects on heavy metal tolerance and accumulation. Picault, N., Cazal??, A.C., Beyly, A., Cuin??, S., Carrier, P., Luu, D.T., Forestier, C., Peltier, G. Biochimie (2006) [Pubmed]
  13. Structure, organization and expression of the metallothionein gene family in Arabidopsis. Zhou, J., Goldsbrough, P.B. Mol. Gen. Genet. (1995) [Pubmed]
  14. A cadmium-sensitive, glutathione-deficient mutant of Arabidopsis thaliana. Howden, R., Andersen, C.R., Goldsbrough, P.B., Cobbett, C.S. Plant Physiol. (1995) [Pubmed]
  15. Cadmium-sensitive, cad1 mutants of Arabidopsis thaliana are phytochelatin deficient. Howden, R., Goldsbrough, P.B., Andersen, C.R., Cobbett, C.S. Plant Physiol. (1995) [Pubmed]
  16. Expression of Arabidopsis phytochelatin synthase 2 is too low to complement an AtPCS1-defective Cad1-3 mutant. Lee, S., Kang, B.S. Mol. Cells (2005) [Pubmed]
  17. Mutagenic definition of a papain-like catalytic triad, sufficiency of the N-terminal domain for single-site core catalytic enzyme acylation, and C-terminal domain for augmentative metal activation of a eukaryotic phytochelatin synthase. Romanyuk, N.D., Rigden, D.J., Vatamaniuk, O.K., Lang, A., Cahoon, R.E., Jez, J.M., Rea, P.A. Plant Physiol. (2006) [Pubmed]
  18. Rapid isolation of monoclonal antibodies. Monitoring enzymes in the phytochelatin synthesis pathway. Li, Y., Kandasamy, M.K., Meagher, R.B. Plant Physiol. (2001) [Pubmed]
  19. Comparative analysis of the two-step reaction catalyzed by prokaryotic and eukaryotic phytochelatin synthase by an ion-pair liquid chromatography assay. Tsuji, N., Nishikori, S., Iwabe, O., Matsumoto, S., Shiraki, K., Miyasaka, H., Takagi, M., Miyamoto, K., Hirata, K. Planta (2005) [Pubmed]
 
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