A widespread transposable element masks expression of a yeast copper transport gene

Genes and Development

Volumn 10, Issue 15, 1996, Pages 1917-1929

  Knight, Simon A B ^a   Labbé, Simon ^a   Kwon, Lucy F ^a   Kosman, Daniel J ^b   Thiele, Dennis J ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^b UNIVERSITY AT BUFFALO   (United States)

Author keywords

Copper; transcription; transport; transposon; yeast

Indexed keywords

COPPER; FUNGAL PROTEIN;

ARTICLE; FUNGUS GROWTH; GENE EXPRESSION; GENE MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; SACCHAROMYCES CEREVISIAE; TRANSPOSON; YEAST;

FUNGI; SACCHAROMYCES CEREVISIAE;

EID: 0029786735     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.10.15.1917     Document Type: Article

References (60)

1. Askwith, C., D. Eide, A. Van Ho, P.S. Bernard, L. Li, S. Davis-Kaplan, D.M. Sipe, and J. Kaplan. 1994. The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake. Cell 76: 403-410.
2. Ausubel, F.M., R. Brent, R.E. Kingston, D.D. Moore, J.G. Seidman, J.A. Smith, and K. Struhl, ed. 1987. Current protocols in molecular biology. John Wiley & Sons, NY, NY.
3. Boeke, J.D. 1989. Transposable elements in Saccharomyces cerevisiae. In Mobile DNA (ed. D.E. Berg and M.M. Howe), pp. 335-374. American Society for Microbiology, Washington DC.
4. Boeke, J.D. and S.B. Sandmeyer. 1991. Yeast transposable elements. In The molecular and cellular biology of the yeast Saccharomyces (ed. J.R. Broach, J.R. Pringle, and E.W. Jones), pp. 193-262. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
5. Bu, G., H.J. Geuze, G.J. Strous, and A. L. Schwartz. 1995. 39 kDa receptor-associated protein is an ER residient protein and a molecular chaperone for LDL receptor-related protein. EMBO J. 14: 2269-2280.
6. Catterall, W.A. 1995. Structure and function of voltage-gated ion channels. Annu. Rev. Biochem. 64: 493-531.
7. Cha, J. and D.A. Cooksey. 1991. Copper resistance in Pseudomonas syringae mediated by periplasmic and outer membrane proteins. Proc. Natl. Acad. Sci. 88: 8915-8919.
8. Culotta, V.C., W.R. Howard, and X.F. Liu. 1994. CRS5 encodes a metallothionein-like protein in Saccharomyces cerevisiae. J. Biol. Chem. 269: 25295-25302.
9. Dancis, A., D.G. Roman, G.J. Anderson, A.G. Hinnebusch, and R.D. Klausner. 1992. Ferric reductase of Saccharomyces cerevisiae: Molecular charcacterization, role in iron uptake, and transcriptional control by iron. Proc. Natl. Acad. Sci. 89: 3869-3873.
10. Dancis, A., D. Haile, D.S. Yaun, and R.D. Klausner. 1994a. The Saccharomyces cerevisiae copper transport protein (Ctr1p). J. Biol. Chem. 269: 25660-25667.
11. Dancis, A., D.S. Yuan, D. Haile, C. Askwith, D. Eide, C. Moehle, J. Kaplan, and R.D. Klausner. 1994b. Molecular characterization of a copper transport protein in S. cerevisiae: An unexpected role for copper in iron transport. Cell 76: 393-402.
12. De Silva, D.M., C.C. Askwith, D. Eide, and D. Kaplan. 1995. The FET3 gene product required for high-affinity iron transport in yeast is a cell surface ferroxidase. J. Biol. Chem. 270: 1098-1101.
13. Deininger, P.L. 1989. SINEs: Short interspersed repeated DNA elements in higher eukaryotes. In Mobile DNA (ed. D.E. Berg and M.M. Howel, pp. 619-636. American Society for Microbiology, Washington, D.C.
14. Eibel, H. and P. Philippsen. 1984. Preferential integration of yeast transposable element Ty into a promoter region. Nature 307: 386-388.
15. Eide, D., S. Davis-Kaplan, I. Jordan, D. Sipe, and J. Kaplan. 1992. Regulation of iron uptake in Saccharomyces cerevisiae. The ferrireductase and Fe(II) transporter are regulated independently. J. Biol. Chem. 267: 20774-20781.
16. Franzusoff, A., J. Rothblatt, and R. Schekman. 1991. Analysis of polypeptide transit through yeast secretory pathway. Methods Enzymol. 194: 662-674.
17. Fujiki, F., A.L. Hubbard, S. Fowler, and P.B. Lazarow. 1982. Isolation of intracellular membranes by means of sodium carbonate treatment: Application of endoplasmic reticulum. J. Cell. Biol. 93: 97-102.
18. Georgatsou, E. and D. Alexandraki. 1994. Two distinctly regulated genes are required for ferric reduction, the first step of iron uptake in Saccharomyces cerevisiae. Mol. Cell. Biol. 14: 3065-3073.
19. Hahn, S., S. Buratowski, P.A. Sharp, and L. Guarente. 1989. Yeast TATA-binding protein TFIID binds to TATA elements with both consensus and nonconsensus DNA sequences. Proc. Natl. Acad. Sci. 86: 5718-5722.
20. Halliwell, B. and J.M.C. Gutteridge. 1984. Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem. J. 219: 1-14.
21. Hassett, R. and D.J. Kosman. 1995. Evidence for Cu(II) reduction as a component of copper uptake by Saccharomyces cerevisiae. J. Biol. Chem. 270: 128-134.
22. Helenius, A., D. Mellman, D. Wall, and A. Hubbard. 1983. Endosomes. Trends Biochem. Sci. 8: 245-250.
23. Hofmann, K. and W. Stoffel. 1993. TMbase - A database of membrane spanning proteins segments. Biol. Chem. Hoppe-Seyler 347: 166.
24. Hutchinson III, C.A., S.C. Hardies, D.D. Loeb, W.R. Shehee, and M.H. Edgell. 1989. LINEs and related retroposons: Long interspersed repeated sequences in the eukaryotic genome. In Mobile DNA (ed. D.E. Berg and M.M. Howe), pp. 593-618. American Society for Microbiology, Washington, DC.
25. Ito, H., Y. Fukada, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkalis cations. J. Bacteriol 153: 163-168.
26. Jackson, M.R., T. Nilsson, and P.A. Peterson. 1990. Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum. EMBO J. 9: 3153-3162.
27. Kampfenkel, K., S. Kushnir, E. Babiychuk, D. Inze, and M. Van Montagu. 1995. Molecular characterization of a putative Arabidopsis thaliana copper transporter and its yeast homologue. J. Biol. Chem. 270: 28479-28486.
28. Kleckner, N. 1989. Transposon Tn10. In Mobile DNA (ed. D.E. Berg and M.M. Howe), pp. 227-268. American Society for Microbiology, Washington, DC.
29. Kolling, R. and C.P. Hollenberg. 1994. The ABC-transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants. EMBO J. 13: 3261-3271.
30. Kolodziej, P.A. and R.A. Young. 1991. Epitope tagging and protein surveillance. Methods Enzymol. 194: 508-519.
31. Kuchler, K., H.G. Dohlman, and J. Thorner. 1993. The a-factor transporter (STE6 gene product) and cell polarity in the yeast Saccharomyces cerevisiae. J. Cell. Biol. 120: 1203-1215.
32. Lesuisse, E. and P. Labbe. 1989. Reductive and non-reductive mechanisms of iron assimilation by the yeast Saccharomyces cerevisiae. J. Gen. Microbiol. 135: 257-263.
33. Linder, M.C. 1991. Biochemistry of copper. Plenum Press, New York, NY.
34. McCusker, J.H., K.V. Clemons, D.A. Stevens, and R.W. Davis. 1994. Genetic characterization of pathogenic Saccharomyces cerevisiae isolates. Genetics 136: 1261-1269.
35. Mortimer, R.K. and J.R. Johnston. 1986. Genealogy of principal strains of the yeast genetic stock center. Genetics 113: 35-43.
36. Nagata, K. 1996. Hsp47: A collagen-specific molecular chaperone. Trends Biochem. Sci. 21: 23-26.
37. Nilsson, T., M. Jackson, and P.A. Peterson. 1989. Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic reticulum. Cell 58: 707-718.
38. Niman, H.L., R.A. Houghten, L.E. Walker, R.A. Reisfeld, I.A. Wilson, J.M. Hogle, and R.A. Lerner. 1983. Generation of protein-reactive antibodies by short peptides is an event of high frequency: Implications for the structural basis of immune recognition. Proc. Natl. Acad. Sci. 80: 4949-4953.
39. Nothwehr, S.F., C.J. Roberts, and T.H. Stevens. 1993. Membrane protein retention in the yeast Golgi apparatus: Dipeptidyl aminopeptidase A is retained by a cytoplasmic signal containing aromatic residues. J. Cell. Biol. 121: 1197-1209.
40. Odermatt, A., H. Suter, R. Krapt, and M. Solioz. 1993. Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae. J. Biol. Chem. 268: 12775-12779.
41. Oyanagui, Y. 1984. Reevaluation of assay methods and establishment of kit for superoxide dismutase activity. Anal. Biochem. 142: 290-296.
42. Preuss, D., J. Mulholland, A. Franzusoff, N. Segev, and D. Botstein. 1992. Characterization of the Saccharomyces Golgi complex through the cell cycle by immunoelectron microscopy. Mol. Biol. Cell 3: 789-803.
43. Raths, S., J. Rohrer, F. Crausaz, and H. Riezman. 1993. end3 and end4: Two mutants defective in receptor-mediated and fluid-phase endocytosis in Saccharomyces cerevisiae. J. Cell Biol. 120: 55-65.
44. Redding, K., C. Holcomb, and R.S. Fuller. 1991. Immunolocalization of Kex2 protease identifies a putative late Golgi compartment in the yeast Saccharomyces cerevisiae. J. Cell. Biol. 113: 527-538.
45. Riezman, H. 1985. Endocytosis in yeast: Several of the yeast secretory mutants are defective in endocytosis. Cell 40: 1001-1009.
46. Roeder, G.S., P.J. Farabaugh, D.T. Chaleff, and G.R. Fink. 1980. The origins of gene instability in yeast. Science 209: 1375-1380.
47. Roeder, G.S. and G.R. Fink. 1983. Transposable elements in yeast. In Mobile genetic elements (ed. J.A. Shapiro), pp. 300-328. Academic Press, New York, NY.
48. Rose, M.D., L.M. Misra, and J.P. Vogel. 1989. KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/ GRP78 gene. Cell 57: 1211-1221.
49. Sherman, F., G.R. Fink, and J.B. Hicks. 1986. Methods in yeast genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
50. Sibilia, M. and E.F. Wagner. 1995. Strain-dependent epithelial defects in mice lacking the EGF receptor. Science 269: 234-238.
51. Sikorski, R.S. and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulations of DNA in Saccharomyces cerevisiae. Genetics 122: 19-27.
52. Stadtman, E.R. and C.N. Oliver. 1991. Metal-catalysed oxidation of proteins. J. Biol. Chem. 266: 2005-2008.
53. Stearman, R., D.S. Yuan, Y. Yamaguchi-Iwai, R.D. Klausner, and A. Dancis. 1996. A permease-oxidase complex involved in high-affinity uptake in yeast. Science 271: 1552-1557.
54. Threadgill, D.W., A.A. Dlugosz, L.A. Hansen, T. Tennenbaum, U. Lichti, D. Yee, C. LaMantia, T. Mourton, K. Herrup, R.C. Harris, J.A. Barnard, S.H. Yuspa, R.J. Coffey, and T. Magnuson. 1995. Targeted disruption of mouse EGF receptor: Effect of genetic background on mutant phenotype. Science 269: 230-234.
55. Townsley, F.M. and H.R. Pelham. 1994. The KKXX signal mediates retrieval of membrane proteins from the Golgi to the ER in yeast. Eur. J. Cell. Biol. 64: 211-216.
56. Vulpe, C.D. and S. Packman. 1995. Cellular copper transport. Annu. Rev. Nutr. 15: 293-322.
57. Wach, A., A. Brachat, R. Pohlmann, and P. Philippsen. 1994. New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae. Yeast 10: 1793-1808.
58. Wilcox, C.A., K. Redding, R. Wright, and R. S. Fuller. 1992. Mutation of a tyrosine localization signal in the cytosolic tail of yeast Kex2 protease disrupts Golgi retention and results in default transport to the vacuole. Mol. Biol. Cell. 3: 1353-1371.
59. Winge, D.R., K.B. Nielson, W.R. Gray, and D.H. Hamer. 1985. Yeast Metallothionien: Sequence and metal binding properties. J. Biol. Chem. 260: 14464-14470.
60. Zhu, Z., M.S. Szczypka, and D.J. Thiele. 1995. Transcriptional regulation and function of yeast metallothionein genes. In Genetic response to metals (ed. B. Sarkar), pp. 379-395. Marcel Dekker, New York, NY.