Engineering in vivo instability of firefly luciferase and Escherichia coli β-glucuronidase in higher plants using recognition elements from the ubiquitin pathway
10.1023/a:1006089924093
Crossref journal-article
Springer Science and Business Media LLC
Plant Molecular Biology (297)
Bibliography

Worley, C. K., Ling, R., & Callis, J. (1998). Engineering in vivo instability of firefly luciferase and Escherichia coli β-glucuronidase in higher plants using recognition elements from the ubiquitin pathway. Plant Molecular Biology, 37(2), 337–347.

Authors 3
  1. Cathy Kingdon Worley (first)
  2. Richard Ling (additional)
  3. Judy Callis (additional)
References 49 Referenced 39
  1. Atmann T, Damm B, Helfter U, Willmitzer L, Morris PC: Protoplast transformation and methods to create specific mutants in Arabidopsis thaliana. In: Koncz C, Chua NH, Schell J (ed) Methods in Arabidopsis research, pp. 310–330. World Scientific, Singapore (1992). (10.1142/9789814439701_0012) / Methods in Arabidopsis research by T Atmann (1992)
  2. Bachmair A, Becker F, Schell J: Use of a reporter transgene to generate Arabidopsis mutants in ubiquit-independent protein degradation. Proc Natl Acad Sci USA 90: 418–421 (1993). (10.1073/pnas.90.2.418) / Proc Natl Acad Sci USA by A Bachmair (1993)
  3. Bachmair A, Finley D, Varskavsky A: In vivo half-life of a protein is a function of its amino-terminal residue. Science 234: 179–186 (1986). (10.1126/science.3018930) / Science by A Bachmair (1986)
  4. Bachmair A, Varskavsky A: The degradation signal in a shortlived protein. Cell 56: 1019–1032 (1989). (10.1016/0092-8674(89)90635-1) / Cell by A Bachmair (1989)
  5. Baker RT, Varshavksy A: Yeast N-terminal amidase: a new enzyme and component of the N-end rule pathway. J Biol Chem 270: 12065–12074 (1995). (10.1074/jbc.270.20.12065) / J Biol Chem by RT Baker (1995)
  6. Baker RT, Varshavsky A: Inhibition of the Nend rule pathway in living cells. Proc Natl Acad Sci USA 88: 1090–1094 (1991). (10.1073/pnas.88.4.1090) / Proc Natl Acad Sci USA by RT Baker (1991)
  7. Balzi E, Choder M, Chen W, Varshavsky A, Goffeau A: Cloning and functional analysis of the arginylt-RNA-protein transferase gene ATE1 of Saccharomyces cerevisiae. J Biol Chem 265: 7464–7471 (1990). (10.1016/S0021-9258(19)39136-7) / J Biol Chem by E Balzi (1990)
  8. Bartel B, Wunning I, Varskavsky A: The recognition component of the N-end rule pathway. EMBO J 9: 3179–3189 (1990). (10.1002/j.1460-2075.1990.tb07516.x) / EMBO J by B Bartel (1990)
  9. Beers E, Moreno T, Callis J: Subcellular localization of ubiquitin and ubiquitinated proteins in Arabidopsis thaliana. J Biol Chem 267: 15432–15439 (1992). (10.1016/S0021-9258(19)49552-5) / J Biol Chem by E Beers (1992)
  10. Berlin CM, Schimke RT: Influence of turnover rates on the responses of enzyme to cortisone. Mol Pharm 1: 149–156 (1965). (10.1016/S0026-895X(25)14740-8) / Mol Pharm by CM Berlin (1965)
  11. Bevan M, Barnes WM, Chilton MD: Structure and transcription of the nopaline synthase gene region of TDNA. Nucl Acids Res 11: 369–385 (1983). (10.1093/nar/11.2.369) / Nucl Acids Res by M Bevan (1983)
  12. Bollage DM, Edelstein SJ: Protein concentration determination. In: Protein Methods, pp. 45–69. Academic Press, New York (1991). / Protein Methods by DM Bollage (1991)
  13. Burke T, Callis J, Vierstra RD: Characterization of a polyubiquitin gene from Arabidopsis thaliana. Mol Gen Genet 213: 435–443 (1988). (10.1007/BF00339613) / Mol Gen Genet by T Burke (1988)
  14. Callis J: Regulation of protein degradation in plants. In: Setlow J. (ed) Genetic Engineering: Principles and Methods, pp. 121–148. Plenum Press, New York (1997). (10.1007/978-1-4615-5925-2_7) / Genetic Engineering: Principles and Methods by J Callis (1997)
  15. Chau V, Tobias J, Bachmair A, Marriott D, Ecker D, Gonda D, Varshavsky A: A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science 243: 1576–1583 (1989). (10.1126/science.2538923) / Science by V Chau (1989)
  16. Ciechanover A, Finley D, Varshavsky A: Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85. Cell 37: 57–66 (1984). (10.1016/0092-8674(84)90300-3) / Cell by A Ciechanover (1984)
  17. Conti E, Franks NP, Brick P: Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure 4: 287–298 (1996). (10.1016/S0969-2126(96)00033-0) / Structure by E Conti (1996)
  18. DeWet JR, Wood KV, DeLuca M, Helinski DR, Subramani S: Firefly luciferase gene: structure and expression inmammalian cells. Mol Cell Biol 2: 1044–1051 (1987). / Mol Cell Biol by JR DeWet (1987)
  19. Ecker DG, Butt TR, Marsh HJ, Sternberg EJ, Margolis N, Monia BP, Jonnalagadda S, Khan MI, Weber PL, Muellar L, Crooke ST: Gene synthesis, expression structures, and functional activities of sitespecific mutants of ubiquitin. J Biol Chem 262: 14213–14221 (1987). (10.1016/S0021-9258(18)47925-2) / J Biol Chem by DG Ecker (1987)
  20. Ferber, Ciechanover A: role of arginine-tRNA in protein degradation by the ubiquitin pathway. Nature 326: 808–811 (1987). (10.1038/326808a0) / Nature by C. A. Ferber (1987)
  21. Finley D, Ozkaynak E, Varshavsky A: The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation and other stresses. Cell 48: 1035–1046 (1987). (10.1016/0092-8674(87)90711-2) / Cell by D Finley (1987)
  22. Gallaher S, Winston SE, Fuller SA, Hurrell JGR: Immunoblotting and immunodetection. In: Ausubel FM, Brent R, Kingston RE (ed) Current Protocols in Molecular Biology, pp. 10.8.1–17. Greene Publishing Associates/WileyInterscience, New York (1994). / Current Protocols in Molecular Biology by S Gallaher (1994)
  23. Gonda D, Bachmair A, Wunning I, Tobias J, Lane W, Varshavsky A: Universality and structure of the N-end rule. J Biol Chem 264: 16700–16712 (1989). (10.1016/S0021-9258(19)84762-2) / J Biol Chem by D Gonda (1989)
  24. Gould SJ, Keller GA, Schneider M, Howell SH, Garrard LJ, Goodman JM, Distel B, Tabak H, Subramani S: Peroxisomal protein import is conserved between yeast, plants, insects, and mammals. EMBO J 9: 85–90 (1990). (10.1002/j.1460-2075.1990.tb08083.x) / EMBO J by SJ Gould (1990)
  25. Heller H, Hershko A: A ubiquitin-protein ligase specific for type III protein substrates. J Biol Chem 265: 6532–6535 (1990). (10.1016/S0021-9258(19)39177-X) / J Biol Chem by H Heller (1990)
  26. Hershko A, Heller J, Eytan E, Reiss Y: The protein substrate binding site of the ubiquitin-protein ligase system. J Biol Chem 261: 11992–11999 (1986). (10.1016/S0021-9258(18)67192-3) / J Biol Chem by A Hershko (1986)
  27. Hochstrasser M: Ubiquitin-dependent protein degradation. Annu Rev Genet 30: 405–439 (1996). (10.1146/annurev.genet.30.1.405) / Annu Rev Genet by M Hochstrasser (1996)
  28. Holloway SL, Glotzer M, King RW, Murray AW: Anaphase is initiated by proteolysis rather than by the inactivation of maturation-promoting factor. Cell 73: 1393–1402 (1993). (10.1016/0092-8674(93)90364-V) / Cell by SL Holloway (1993)
  29. Ito H, Yasuki Y, Murata K, Kimura A: Transformation of intact yeast cells treated with alkali cations. J Bact 153: 163–168 (1983). (10.1128/jb.153.1.163-168.1983) / J Bact by H Ito (1983)
  30. Jefferson R: Assaying chimeric genes in plants: the GUS gene fusion system. Plant Mol Biol Rep 5: 387–405 (1987). (10.1007/BF02667740) / Plant Mol Biol Rep by R Jefferson (1987)
  31. Jefferson R, Kavanagh T, Bevan M: GUS fusions: βglucuronidase as a sensitive and versatile genemarker in higher plants. EMBO J 6: 3901–3907 (1987). (10.1002/j.1460-2075.1987.tb02730.x) / EMBO J by R Jefferson (1987)
  32. Johnson ES, Bartel B, Seufert W, Varshavsky A: Ubiquitin as a degradation signal. EMBO J 11: 497–505 (1992). (10.1002/j.1460-2075.1992.tb05080.x) / EMBO J by ES Johnson (1992)
  33. Keller GA, Gould S, DeLuca M, Subramani S: Firefly luciferase is targeted to peroxisomes in mammalian cells. Proc Natl Acad Sci USA 84: 3264–3268 (1987). (10.1073/pnas.84.10.3264) / Proc Natl Acad Sci USA by GA Keller (1987)
  34. Kunkel TA: Rapid and efficient sitedirected mutagenesis without phenotypic selection. Proc Natl Acad Sci USA 82: 488–492 (1985). (10.1073/pnas.82.2.488) / Proc Natl Acad Sci USA by TA Kunkel (1985)
  35. Madura K, Varshavsky A: Degradation of G alpha by the N-end rule pathway. Science 265: 1454–1458 (1994). (10.1126/science.8073290) / Science by K Madura (1994)
  36. Millar A, Straume M, Chory J, Chua NH, Kay SA: The regulation of circadian period by phototransduction pathways in Arabidopsis. Science 267: 1163–1166 (1995). (10.1126/science.7855596) / Science by A Millar (1995)
  37. Norris S, Meyer S, Callis J: The intron of Arabidopsis polyubiquitin genes is conserved in location and is a quantitative determinant of chimeric gene expression. Plant Mol Biol 21: 895–906 (1993). (10.1007/BF00027120) / Plant Mol Biol by S Norris (1993)
  38. Pickart CM, Rose I: Ubiquitin carboxyl-terminal hydrolase acts on ubiquitin carboxyl-terminal amides. J Biol Chem 261: 7903–7910 (1985). (10.1016/S0021-9258(17)39538-8) / J Biol Chem by CM Pickart (1985)
  39. Reiss Y, Kaim D, Hershko A: Specificity of binding of N-terminal residue of proteins to ubiquitinprotein ligase. Use of amino acid derivative to characterize specific binding sites. J Biol Chem 263: 2693–2698 (1988). (10.1016/S0021-9258(18)69123-9) / J Biol Chem by Y Reiss (1988)
  40. Restrepo MA, Freed DD, Carrington JC: Nuclear transport of plant polyviral proteins. Plant Cell 2: 987–998 (1990). / Plant Cell by MA Restrepo (1990)
  41. Reynolds SJ, Smith SM: Regulation of expression of the cucumber isocitrate lyase gene in cotyledons upon seed germination and by sucrose. Plant Mol Biol 29: 885–896 (1995). (10.1007/BF00014963) / Plant Mol Biol by SJ Reynolds (1995)
  42. Richter-Ruoff B, Wolf DH, Hochstrasser M: Degradation of the yeast MATβ2 transcriptional regulator is mediated by the proteasome. FEBS Lett 354: 50–52 (1994). (10.1016/0014-5793(94)01085-4) / FEBS Lett by B Richter-Ruoff (1994)
  43. Sambrook J, Fritsch EF, Maniatis T: Molecular Cloning: A Laboratory Manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY (1989). / Molecular Cloning: A Laboratory Manual by J Sambrook (1989)
  44. Tobias J, Varshavsky A: Cloning and functional analysis of the ubiquitinspecific protease gene UBP1 of Saccharomyces cerevisiae. J Biol Chem 266: 12021–12028 (1991). (10.1016/S0021-9258(18)99059-9) / J Biol Chem by J Tobias (1991)
  45. Tobias JW, Shrader TE, Rocap G, Varshavsky A: The N-end rule in bacteria. Science 254: 1374–1377 (1991). (10.1126/science.1962196) / Science by JW Tobias (1991)
  46. Varshavsky A: The N-end rule: functions, mysteries, uses. Proc Natl Acad Sci USA 93: 12142–12149 (1996). (10.1073/pnas.93.22.12142) / Proc Natl Acad Sci USA by A Varshavsky (1996)
  47. Varshavsky A: The N-end role pathway of protein degradation. Genes Cells 2: 13–28 (1997). (10.1046/j.1365-2443.1997.1020301.x) / Genes Cells by A Varshavsky (1997)
  48. Vierstra RD: Proteolysis in plants: mechanisms and functions. Plant Mol Biol 275–302 (1996). (10.1007/978-94-009-0353-1_12)
  49. Wiebel FF, Kunau WH: The Pas2 protein essential for peroxisome biogenesis is related to ubiquitin-conjugating enzymes. Nature 359: 73–76 (1992). (10.1038/359073a0) / Nature by FF Wiebel (1992)
Dates
Type When
Created 22 years, 8 months ago (Dec. 21, 2002, 2:38 p.m.)
Deposited 2 weeks, 5 days ago (Aug. 4, 2025, 12:51 a.m.)
Indexed 1 week, 1 day ago (Aug. 14, 2025, 8:03 p.m.)
Issued 27 years, 3 months ago (May 1, 1998)
Published 27 years, 3 months ago (May 1, 1998)
Published Print 27 years, 3 months ago (May 1, 1998)
Funders 0

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@article{Worley_1998, title={Engineering in vivo instability of firefly luciferase and Escherichia coli β-glucuronidase in higher plants using recognition elements from the ubiquitin pathway}, volume={37}, ISSN={1573-5028}, url={http://dx.doi.org/10.1023/a:1006089924093}, DOI={10.1023/a:1006089924093}, number={2}, journal={Plant Molecular Biology}, publisher={Springer Science and Business Media LLC}, author={Worley, Cathy Kingdon and Ling, Richard and Callis, Judy}, year={1998}, month=may, pages={337–347} }