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An Essential Yeast Gene Encoding a Homolog of Ubiquitin-activating Enzyme

Bibliographic reference Dohmen, RJ. ; Stappen, R. ; Mcgrath, JP. ; Forrova, H. ; Kolarov, J. ; et. al. An Essential Yeast Gene Encoding a Homolog of Ubiquitin-activating Enzyme. In: Journal of Biological Chemistry, Vol. 270, no. 30, p. 18099-18109 (1995)
Permanent URL http://hdl.handle.net/2078.1/47908
  1. Finley Daniel, Ciechanover Aaron, Varshavsky Alexander, Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85, 10.1016/0092-8674(84)90299-x
  2. Ausubel F. M. Brent R. Kingston R. E. Moore D. D. Smith J. A. Seidman J. G. Struhl K. (1992) Current Protocols in Molecular Biology , Wiley-Interscience, New York
  3. Dohmen R. J., Madura K., Bartel B., Varshavsky A., The N-end rule is mediated by the UBC2(RAD6) ubiquitin-conjugating enzyme., 10.1073/pnas.88.16.7351
  4. Dohmen R. Jürgen, Strasser Alexander W. M., Höner Cornelia B., Hollenberg Cornelis P., An efficient transformation procedure enabling long-term storage of competent cells of various yeast genera, 10.1002/yea.320070704
  5. Dunn T M, Shortle D, Null alleles of SAC7 suppress temperature-sensitive actin mutations in Saccharomyces cerevisiae., 10.1128/mcb.10.5.2308
  6. Ecker, J. Biol. Chem., 262, 3524 (1987)
  7. Ellison, J. Biol. Chem., 266, 21150 (1991)
  8. Field J, Nikawa J, Broek D, MacDonald B, Rodgers L, Wilson I A, Lerner R A, Wigler M, Purification of a RAS-responsive adenylyl cyclase complex from Saccharomyces cerevisiae by use of an epitope addition method., 10.1128/mcb.8.5.2159
  9. Finley D, Ubiquitination, 10.1146/annurev.cellbio.7.1.25
  10. Finley Daniel, Ciechanover Aaron, Varshavsky Alexander, Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85, 10.1016/0092-8674(84)90299-x
  11. Finley Daniel, Özkaynak Engin, Varshavsky Alexander, The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses, 10.1016/0092-8674(87)90711-2
  12. Finley D, Sadis S, Monia B P, Boucher P, Ecker D J, Crooke S T, Chau V, Inhibition of proteolysis and cell cycle progression in a multiubiquitination-deficient yeast mutant., 10.1128/mcb.14.8.5501
  13. Ayusawa Dai, Kaneda Sumiko, Itoh Yoshiyasu, Yasuda Hideyo, Murakami Yasuko, Sugasawa Kaoru, Hanaoka Fumio, Seno Takeshi, Complementation by a Cloned Human Ubiquitin-Activating Enzyme E1 of the S-Phase-Arrested Mouse FM3A Cell Mutant with Thermolabile E1., 10.1247/csf.17.113
  14. Gietz R.Daniel, Akio Sugino, New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites, 10.1016/0378-1119(88)90185-0
  15. GOLDBERG Alfred L., The mechanism and functions of ATP-dependent proteases in bacterial and animal cells, 10.1111/j.1432-1033.1992.tb19822.x
  16. Haas, J. Biol. Chem., 257, 2543 (1982)
  17. Haas Arthur L., Warms Jessie V. B., Rose Irwin A., Ubiquitin adenylate: structure and role in ubiquitin activation, 10.1021/bi00288a007
  18. Handley P. M., Mueckler M., Siegel N. R., Ciechanover A., Schwartz A. L., Molecular cloning, sequence, and tissue distribution of the human ubiquitin-activating enzyme E1., 10.1073/pnas.88.1.258
  19. Hatfield, J. Biol. Chem., 267, 14799 (1992)
  20. Hatfield, J. Biol. Chem., 265, 15813 (1990)
  21. Hershko Avram, Ciechanover Aaron, The Ubiquitin System for Protein Degradation, 10.1146/annurev.bi.61.070192.003553
  22. Herskowitz Ira, Jensen Robert E., [8] Putting the HO gene to work: Practical uses for mating-type switching, Guide to Yeast Genetics and Molecular Biology (1991) ISBN:9780121820954 p.132-146, 10.1016/0076-6879(91)94011-z
  23. HOCHSTRASSER M, Ubiquitin and intracellular protein degradation, 10.1016/0955-0674(92)90135-y
  24. Beers, J. Biol. Chem., 268, 21645 (1993)
  25. Hoffmann A., Roeder R.G., Purification of his-tagged proteins in non-denaturing conditions suggests a convenient method for protein interaction studies, 10.1093/nar/19.22.6337
  26. Hovland Peter, Flick Jeffrey, Johnston Mark, Sclafani Robert A., Galactose as a gratuitous inducer of GAL gene expression in yeasts growing on glucose, 10.1016/0378-1119(89)90403-4
  27. Nobuyuki Imai, Sumiko Kaneda, Yukiko Nagai, Takeshi Seno, Dai Ayusawa, Fumio Hanaoka, Fumiaki Yamao, Cloning and sequence of a functionally active cDNA encoding the mouse ubiquitin-activating enzyme E1, 10.1016/0378-1119(92)90200-9
  28. Jentsch Stefan, The Ubiquitin-Conjugation System, 10.1146/annurev.ge.26.120192.001143
  29. Johnson M E, Rajagopalan K V, Involvement of chlA, E, M, and N loci in Escherichia coli molybdopterin biosynthesis., 10.1128/jb.169.1.117-125.1987
  30. Kay Graham F., Ashworth Alan, Penny Graeme D., Dunlop Morag, Swift Sally, Brockdorff Neil, Rastant Sohaila, A candidate spermatogenesis gene on the mouse Y chromosome is homologous to ubiquitin-activating enzyme E1, 10.1038/354486a0
  31. Kok K., Hofstra R., Pilz A., van den Berg A., Terpstra P., Buys C. H., Carritt B., A gene in the chromosomal region 3p21 with greatly reduced expression in lung cancer is similar to the gene for ubiquitin-activating enzyme., 10.1073/pnas.90.13.6071
  32. Kulka, J. Biol. Chem., 263, 15726 (1988)
  33. Kunkel T. A., Rapid and efficient site-specific mutagenesis without phenotypic selection., 10.1073/pnas.82.2.488
  34. Leyser H. M. Ottoline, Lincoln Cynthia A., Timpte Candace, Lammer Douglas, Turner Jocelyn, Estelle Mark, Arabidopsis auxin-resistance gene AXR1 encodes a protein related to ubiquitin-activating enzyme E1, 10.1038/364161a0
  35. Brizzard, BioTechniques, 16, 730 (1994)
  36. Lingner Joachim, Kellermann Josef, Keller Walter, Cloning and expression of the essential gene for poly(A) polymerase from S. cerevisiae, 10.1038/354496a0
  37. Madura, J. Biol. Chem., 268, 12046 (1993)
  38. McGrath, EMBO J., 10, 227 (1991)
  39. Mendenhall Michael D., Culbertson Michael R., The yeastSUF3frameshift suppressor encodes a mutant glycine tRNAccc, 10.1093/nar/16.17.8713
  40. Minvielle-Sebastia L, Preker P., Keller W, RNA14 and RNA15 proteins as components of a yeast pre-mRNA 3'-end processing factor, 10.1126/science.7992054
  41. Mitchell Michael J., Woods Diane R., Tucker Priscilla K., Opp Judith S., Bishop Colin E., Homology of a candidate spermatogenic gene from the mouse Y chromosome to the ubiquitin-activating enzyme El, 10.1038/354483a0
  42. Nishitani Hideo, Goto Hiroshige, Kaneda Sumiko, Yamao Fumiaki, Seno Takesi, Handley Patricia, Schwartz Alan L., Nishimoto Takeharu, tsBN75 and tsBN423, temperature-sensitive X-linked mutants of the BHK21 cell line, can be complemented by the ubiquitin-activating enzyme E1 cDNA, 10.1016/0006-291x(92)90692-e
  43. Parsell D A, Lindquist S, The Function of Heat-Shock Proteins in Stress Tolerance: Degradation and Reactivation of Damaged Proteins, 10.1146/annurev.ge.27.120193.002253
  44. Pickart Cecile M., Ubiquitin Activation and Ligation, Ubiquitin (1988) ISBN:9781489920515 p.77-99, 10.1007/978-1-4899-2049-2_4
  45. Chalfie M, Tu Y, Euskirchen G, Ward W., Prasher D., Green fluorescent protein as a marker for gene expression, 10.1126/science.8303295
  46. Pickart, J. Biol. Chem., 269, 7115 (1994)
  47. Rechsteiner Martin, Natural substrates of the Ubiquitin proteolytic pathway, 10.1016/0092-8674(91)90104-7
  48. Author index for volume 2, 10.1016/s1046-2023(05)80070-2
  49. Scheffner Martin, Nuber Ulrike, Huibregtse Jon M., Protein ubiquitination involving an E1–E2–E3 enzyme ubiquitin thioester cascade, 10.1038/373081a0
  50. Sharp Paul M., Li Wen-Hsiung, The codon adaptation index-a measure of directional synonymous codon usage bias, and its potential applications, 10.1093/nar/15.3.1281
  51. Sherman F. Fink G. R. Hicks J. B. (1986) Methods in Yeast Genetics , Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
  52. Sikorski, Genetics, 122, 19 (1989)
  53. Struhl K., Stinchcomb D. T., Scherer S., Davis R. W., High-frequency transformation of yeast: autonomous replication of hybrid DNA molecules., 10.1073/pnas.76.3.1035
  54. Sung, EMBO J., 10, 2187 (1991)
  55. Varshavsky Alexander, The N-end rule, 10.1016/0092-8674(92)90285-k
  56. Vierstra R D, Protein Degradation in Plants, 10.1146/annurev.pp.44.060193.002125
  57. Chen J, Moore C, Separation of factors required for cleavage and polyadenylation of yeast pre-mRNA., 10.1128/mcb.12.8.3470
  58. Wierenga Rik K., Hol Wim G. J., Predicted nucleotide-binding properties of p21 protein and its cancer-associated variant, 10.1038/302842a0
  59. Winston Fred, Minehart Patricia L., Analysis of the yeastSPT3gene and identification of its product, a positive regulator of Ty trarscription, 10.1093/nar/14.17.6885
  60. Young R., Davis R., Yeast RNA polymerase II genes: isolation with antibody probes, 10.1126/science.6356359
  61. Chien C. T., Bartel P. L., Sternglanz R., Fields S., The two-hybrid system: a method to identify and clone genes for proteins that interact with a protein of interest., 10.1073/pnas.88.21.9578
  62. Ciechanover Aaron, The ubiquitin-proteasome proteolytic pathway, 10.1016/0092-8674(94)90396-4
  63. Ciechanover, J. Biol. Chem., 257, 2537 (1982)