Skip to main content
NCBI home page
Plant Physiology logoLink to Plant Physiology
. 1992 Sep;100(1):100–107. doi: 10.1104/pp.100.1.100

Cadmium-Sensitive Mutants of Arabidopsis thaliana1

Ross Howden 1, Christopher S Cobbett 1
PMCID: PMC1075523  PMID: 16652930

Abstract

A screening procedure for identifying Cd-sensitive mutants of Arabidopsis thaliana is described. With this procedure, two Cd-sensitive mutants were isolated. These represent independent mutations in the same locus, referred to as CAD1. Genetic analysis has shown that the sensitive phenotype is recessive to the wild type and segregates as a single Mendelian locus. Crosses of the mutant to marker strains showed that the mutation is closely linked to the tt3 locus on chromosome 5. In addition to Cd, the mutants are also significantly more sensitive to mercuric ions and only slightly more sensitive to Cu and Zn, while being no more sensitive than the wild type to Mn, thus indicating a degree of specificity in the mechanism affected by the mutation. Undifferentiated callus tissue is also Cd sensitive, suggesting that the mutant phenotype is expressed at the cellular level. Both wild-type and mutant plants showed increased sensitivity to Cd in the presence of buthionine sulfoximine, an inhibitor of the biosynthesis of the cadmium-binding (γ-glutamylcysteine)n-glycine peptides, suggesting that the mutant is still able to synthesize these peptides. However, the effects of a cad1 mutation and buthionine sulfoximine together on cadmium sensitivity are essentially nonadditive, indicating that they may affect different aspects of the same detoxification mechanism. Assays of Cd uptake by intact plants indicate that the mutant is deficient in its ability to sequester Cd.

Full text

PDF
100

Images in this article

102Figure 1
on p.102
105Figure 7
on p.105

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Evans I. M., Gatehouse L. N., Gatehouse J. A., Robinson N. J., Croy R. R. A gene from pea (Pisum sativum L.) with homology to metallothionein genes. FEBS Lett. 1990 Mar 12;262(1):29–32. doi: 10.1016/0014-5793(90)80145-9. [DOI] [PubMed] [Google Scholar]
  2. Freedman J. H., Ciriolo M. R., Peisach J. The role of glutathione in copper metabolism and toxicity. J Biol Chem. 1989 Apr 5;264(10):5598–5605. [PubMed] [Google Scholar]
  3. Grill E., Löffler S., Winnacker E. L., Zenk M. H. Phytochelatins, the heavy-metal-binding peptides of plants, are synthesized from glutathione by a specific gamma-glutamylcysteine dipeptidyl transpeptidase (phytochelatin synthase). Proc Natl Acad Sci U S A. 1989 Sep;86(18):6838–6842. doi: 10.1073/pnas.86.18.6838. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Grill E., Winnacker E. L., Zenk M. H. Phytochelatins, a class of heavy-metal-binding peptides from plants, are functionally analogous to metallothioneins. Proc Natl Acad Sci U S A. 1987 Jan;84(2):439–443. doi: 10.1073/pnas.84.2.439. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Mehra R. K., Tarbet E. B., Gray W. R., Winge D. R. Metal-specific synthesis of two metallothioneins and gamma-glutamyl peptides in Candida glabrata. Proc Natl Acad Sci U S A. 1988 Dec;85(23):8815–8819. doi: 10.1073/pnas.85.23.8815. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Mutoh N., Hayashi Y. Isolation of mutants of Schizosaccharomyces pombe unable to synthesize cadystin, small cadmium-binding peptides. Biochem Biophys Res Commun. 1988 Feb 29;151(1):32–39. doi: 10.1016/0006-291x(88)90555-4. [DOI] [PubMed] [Google Scholar]
  7. Rauser W. E. Phytochelatins. Annu Rev Biochem. 1990;59:61–86. doi: 10.1146/annurev.bi.59.070190.000425. [DOI] [PubMed] [Google Scholar]
  8. Reese R. N., Wagner G. J. Effects of buthionine sulfoximine on cd-binding Peptide levels in suspension-cultured tobacco cells treated with cd, zn, or cu. Plant Physiol. 1987 Jul;84(3):574–577. doi: 10.1104/pp.84.3.574. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Reese R. N., Winge D. R. Sulfide stabilization of the cadmium-gamma-glutamyl peptide complex of Schizosaccharomyces pombe. J Biol Chem. 1988 Sep 15;263(26):12832–12835. [PubMed] [Google Scholar]
  10. Steffens J. C., Hunt D. F., Williams B. G. Accumulation of non-protein metal-binding polypeptides (gamma-glutamyl-cysteinyl)n-glycine in selected cadmium-resistant tomato cells. J Biol Chem. 1986 Oct 25;261(30):13879–13882. [PubMed] [Google Scholar]
  11. Suiter K. A., Wendel J. F., Case J. S. LINKAGE-1: a PASCAL computer program for the detection and analysis of genetic linkage. J Hered. 1983 May-Jun;74(3):203–204. doi: 10.1093/oxfordjournals.jhered.a109766. [DOI] [PubMed] [Google Scholar]
  12. Vögeli-Lange R., Wagner G. J. Subcellular localization of cadmium and cadmium-binding peptides in tobacco leaves : implication of a transport function for cadmium-binding peptides. Plant Physiol. 1990 Apr;92(4):1086–1093. doi: 10.1104/pp.92.4.1086. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. de Miranda J. R., Thomas M. A., Thurman D. A., Tomsett A. B. Metallothionein genes from the flowering plant Mimulus guttatus. FEBS Lett. 1990 Jan 29;260(2):277–280. doi: 10.1016/0014-5793(90)80122-y. [DOI] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES