메뉴 건너뛰기




Volumn 20, Issue 7, 2000, Pages 2367-2377

The yeast ULP2 (SMT4) gene encodes a novel protease specific for the ubiquitin-like Smt3 protein

Author keywords

[No Author keywords available]

Indexed keywords

PROTEINASE; UBIQUITIN;

EID: 0034018312     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.20.7.2367-2377.2000     Document Type: Article
Times cited : (320)

References (39)
  • 1
    • 0028898059 scopus 로고
    • The schizosaccharomyces pombe hus5 gene encodes a ubiquitin conjugating enzyme required for normal mitosis
    • al-Khodairy, F., T. Enoch, I. M. Hagan, and A. M. Carr. 1995. The Schizosaccharomyces pombe hus5 gene encodes a ubiquitin conjugating enzyme required for normal mitosis. J. Cell Sci. 108:475-486.
    • (1995) J. Cell Sci. , vol.108 , pp. 475-486
    • Al-Khodairy, F.1    Enoch, T.2    Hagan, I.M.3    Carr, A.M.4
  • 4
    • 0027198563 scopus 로고
    • Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast matα2 represser
    • Chen, P., P. Johnson, T. Sommer, S. Jenisch, and M. Hochstrasser. 1993. Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATα2 represser. Cell 74:357-369.
    • (1993) Cell , vol.74 , pp. 357-369
    • Chen, P.1    Johnson, P.2    Sommer, T.3    Jenisch, S.4    Hochstrasser, M.5
  • 5
    • 0033537828 scopus 로고    scopus 로고
    • Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1
    • Desterro, J. M., M. S. Rodriguez, G. D. Kemp, and R. T. Hay. 1999. Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1. J. Biol. Chem 274:10618-10624.
    • (1999) J. Biol. Chem , vol.274 , pp. 10618-10624
    • Desterro, J.M.1    Rodriguez, M.S.2    Kemp, G.D.3    Hay, R.T.4
  • 6
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IκBα inhibits NF-κB activation
    • Desterro, J. M. P., M. S. Rodriguez, and R. T. Hay. 1998. SUMO-1 modification of IκBα inhibits NF-κB activation. Mol. Cell 2:233-239.
    • (1998) Mol. Cell , vol.2 , pp. 233-239
    • Desterro, J.M.P.1    Rodriguez, M.S.2    Hay, R.T.3
  • 7
    • 0029808466 scopus 로고    scopus 로고
    • Cell cycle checkpoints: Preventing an identity crisis
    • Elledge, S. J. 1996. Cell cycle checkpoints: preventing an identity crisis. Science 274:1664-1672.
    • (1996) Science , vol.274 , pp. 1664-1672
    • Elledge, S.J.1
  • 8
    • 0020325948 scopus 로고
    • Nucleotide sequence comparisons and functional analysis of yeast centromere DNAs
    • Fitzgerald-Hayes, M., L. Clarke, and J. Carbon. 1982. Nucleotide sequence comparisons and functional analysis of yeast centromere DNAs. Cell 29: 235-244.
    • (1982) Cell , vol.29 , pp. 235-244
    • Fitzgerald-Hayes, M.1    Clarke, L.2    Carbon, J.3
  • 9
    • 0024266139 scopus 로고
    • New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Gietz, R. D., and A. Sugino. 1988. New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 74:527-534.
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 10
    • 0030695478 scopus 로고    scopus 로고
    • Pathways of ubiquitin conjugation
    • Haas, A. L., and T. J. Siepmann. 1997. Pathways of ubiquitin conjugation. FASEB J. 11:1257-1268.
    • (1997) Faseb J. , vol.11 , pp. 1257-1268
    • Haas, A.L.1    Siepmann, T.J.2
  • 11
    • 0029791321 scopus 로고    scopus 로고
    • Activation of the budding yeast spindle assembly checkpoint without mitotic spindle disruption
    • Hardwick, K. G., E. Weiss, F. C. Luca, M. Winey, and A. W. Murray. 1996. Activation of the budding yeast spindle assembly checkpoint without mitotic spindle disruption. Science 273:953-956.
    • (1996) Science , vol.273 , pp. 953-956
    • Hardwick, K.G.1    Weiss, E.2    Luca, F.C.3    Winey, M.4    Murray, A.W.5
  • 13
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser, M. 1996. Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30:405-439.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 14
    • 0032053883 scopus 로고    scopus 로고
    • There's the rub: A novel ubiquitin-like modification involved in cell cycle regulation
    • Hochstrasser, M. 1998. There's the Rub: a novel ubiquitin-like modification involved in cell cycle regulation. Genes Dev. 12:901-907.
    • (1998) Genes Dev. , vol.12 , pp. 901-907
    • Hochstrasser, M.1
  • 15
    • 0029951080 scopus 로고    scopus 로고
    • Two-hybrid interaction of a human UBC9 homolog with centromere proteins of Saccharomyces cerevisiae
    • Jiang, W., and Y. Koltin. 1996. Two-hybrid interaction of a human UBC9 homolog with centromere proteins of Saccharomyces cerevisiae. Mol. Gen. Genet. 251:153-160.
    • (1996) Mol. Gen. Genet. , vol.251 , pp. 153-160
    • Jiang, W.1    Koltin, Y.2
  • 16
    • 0030794729 scopus 로고    scopus 로고
    • The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer
    • Johnson, E. S., I. Schwienhorst, R. J. Dohmen, and G. Blobel. 1997. The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer. EMBO J. 16:5509-5519.
    • (1997) EMBO J. , vol.16 , pp. 5509-5519
    • Johnson, E.S.1    Schwienhorst, I.2    Dohmen, R.J.3    Blobel, G.4
  • 18
    • 0029982968 scopus 로고    scopus 로고
    • Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexes
    • Kovalenko, O. V., A. W. Plug, T. Haaf, D. K. Gonda, T. Ashley, D. C. Ward, C. M. Radding, and E. I. Golub. 1996. Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexes. Proc. Natl. Acad. Sci. USA 93:2958-2963.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2958-2963
    • Kovalenko, O.V.1    Plug, A.W.2    Haaf, T.3    Gonda, D.K.4    Ashley, T.5    Ward, D.C.6    Radding, C.M.7    Golub, E.I.8
  • 19
    • 0033553532 scopus 로고    scopus 로고
    • Substrate targeting in the ubiquitin system
    • Laney, J. D., and M. Hochstrasser. 1999. Substrate targeting in the ubiquitin system. Cell 97:427-430.
    • (1999) Cell , vol.97 , pp. 427-430
    • Laney, J.D.1    Hochstrasser, M.2
  • 20
    • 0027414941 scopus 로고
    • Morphogenesis in the yeast cell cycle: Regulation by Cdc28 and cyclins
    • Lew, D. J., and S. I. Reed. 1993. Morphogenesis in the yeast cell cycle: regulation by Cdc28 and cyclins. J. Cell Biol. 120:1305-1320.
    • (1993) J. Cell Biol. , vol.120 , pp. 1305-1320
    • Lew, D.J.1    Reed, S.I.2
  • 21
    • 0026009964 scopus 로고
    • Feedback control of mitosis in budding yeast
    • Li, R., and A. W. Murray. 1991. Feedback control of mitosis in budding yeast. Cell 66:519-531.
    • (1991) Cell , vol.66 , pp. 519-531
    • Li, R.1    Murray, A.W.2
  • 22
    • 0033580444 scopus 로고    scopus 로고
    • A new protease required for cell-cycle progression in yeast
    • Li, S.-J., and M. Hochstrasser. 1999. A new protease required for cell-cycle progression in yeast. Nature 398:246-251.
    • (1999) Nature , vol.398 , pp. 246-251
    • Li, S.-J.1    Hochstrasser, M.2
  • 23
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
    • Mahajan, R., C. Delphin, T. Guan, L. Gerace, and F. Melchior. 1997. A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell 88:97-107.
    • (1997) Cell , vol.88 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 24
    • 0030455748 scopus 로고    scopus 로고
    • A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex
    • Matunis, M. J., E. Coutavas, and G. Blobel. 1996. A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J. Cell Biol. 135:1457-1470.
    • (1996) J. Cell Biol. , vol.135 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 25
    • 0029044625 scopus 로고
    • Evidence that the MIF2 gene of Saccharomyces cerevisiae encodes a centromere protein with homology to the mammalian centromere protein CENP-C
    • Meluh, P. B., and D. Koshland. 1995. Evidence that the MIF2 gene of Saccharomyces cerevisiae encodes a centromere protein with homology to the mammalian centromere protein CENP-C. Mol. Biol. Cell 6:793-807.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 793-807
    • Meluh, P.B.1    Koshland, D.2
  • 26
    • 0037498052 scopus 로고    scopus 로고
    • Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus
    • Müller, S., M. J. Matunis, and A. Dejean. 1998. Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. EMBO J. 17:61-70.
    • (1998) EMBO J. , vol.17 , pp. 61-70
    • Matunis, M.J.1    Dejean, A.2
  • 27
    • 0027427249 scopus 로고
    • The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene
    • Papa, F., and M. Hochstrasser. 1993. The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene. Nature 366:313-319.
    • (1993) Nature , vol.366 , pp. 313-319
    • Papa, F.1    Hochstrasser, M.2
  • 28
    • 0020555640 scopus 로고
    • An enzyme with ubiquitin carboxy-terminal esterase activity from reticulocytes
    • Rose, I. A., and J. V. Warms. 1983. An enzyme with ubiquitin carboxy-terminal esterase activity from reticulocytes. Biochemistry 22:4234-4237.
    • (1983) Biochemistry , vol.22 , pp. 4234-4237
    • Rose, I.A.1    Warms, J.V.2
  • 30
    • 0342813068 scopus 로고    scopus 로고
    • SUMO-1: Wrestling with a new ubiquitin-related modifier
    • Saitoh, H., R. T. Pu, and M. Dasso. 1997. SUMO-1: wrestling with a new ubiquitin-related modifier. Trends Biochem. Sci. 22:374-376.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 374-376
    • Saitoh, H.1    Pu, R.T.2    Dasso, M.3
  • 32
    • 0028967267 scopus 로고
    • A ubiquitin-conjugating enzyme involved in the degradation of both S-and M-phase cyclins
    • Seufert, W., B. Futcher, and S. Jentsch. 1995. A ubiquitin-conjugating enzyme involved in the degradation of both S-and M-phase cyclins. Nature 373:78-81.
    • (1995) Nature , vol.373 , pp. 78-81
    • Seufert, W.1    Futcher, B.2    Jentsch, S.3
  • 33
    • 0030842957 scopus 로고    scopus 로고
    • Characterisation of Schizosaccharomyces pombe rad31, a UBA-related gene required for DNA damage tolerance
    • Shayeghi, M., C. L. Doe, M. Tavassoli, and F. Z. Watts. 1997. Characterisation of Schizosaccharomyces pombe rad31, a UBA-related gene required for DNA damage tolerance. Nucleic Acids Res. 25:1162-1169.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1162-1169
    • Shayeghi, M.1    Doe, C.L.2    Tavassoli, M.3    Watts, F.Z.4
  • 34
    • 0030588127 scopus 로고    scopus 로고
    • Associations of UBE2I with RAD52, UBL1, p53, and RAD51 proteins in a yeast two-hybrid system
    • Shen, Z., P. E. Pardington-Purtymun, J. C. Comeaux, R. K. Moyzis, and D. J. Chen. 1996. Associations of UBE2I with RAD52, UBL1, p53, and RAD51 proteins in a yeast two-hybrid system. Genomics 37:183-186.
    • (1996) Genomics , vol.37 , pp. 183-186
    • Shen, Z.1    Pardington-Purtymun, P.E.2    Comeaux, J.C.3    Moyzis, R.K.4    Chen, D.J.5
  • 35
    • 0031426631 scopus 로고    scopus 로고
    • Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/ SUMO-1
    • Sternsdorf, T., K. Jensen, and H. Will. 1997. Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/ SUMO-1. J. Cell Biol. 139:1621-1634.
    • (1997) J. Cell Biol. , vol.139 , pp. 1621-1634
    • Sternsdorf, T.1    Jensen, K.2    Will, H.3
  • 36
    • 0033574967 scopus 로고    scopus 로고
    • Smt3, a SUMO-1 homolog, is conjugated to Cdc3, a component of septin rings at the mother-bud neck in budding yeast
    • Takahashi, Y., M. Iwase, M. Konishi, M. Tanaka, A. Toh-e, and Y. Kikuchi. 1999. Smt3, a SUMO-1 homolog, is conjugated to Cdc3, a component of septin rings at the mother-bud neck in budding yeast. Biochem. Biophys. Res. Commun. 259:582-587.
    • (1999) Biochem. Biophys. Res. Commun. , vol.259 , pp. 582-587
    • Takahashi, Y.1    Iwase, M.2    Konishi, M.3    Tanaka, M.4    Toh-E, A.5    Kikuchi, Y.6
  • 37
    • 0033032942 scopus 로고    scopus 로고
    • Substrate sequestration by a proteolytically inactive lon mutant
    • Van Melderen, L., and S. Gottesman. 1999. Substrate sequestration by a proteolytically inactive Lon mutant. Proc. Natl. Acad. Sci. USA 96:6064-6071.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6064-6071
    • Van Melderen, L.1    Gottesman, S.2
  • 38
  • 39
    • 0002657323 scopus 로고    scopus 로고
    • The deubiquitinating enzymes
    • J.-M. Peters, J. R. Horris, and D. Finley (ed.), Plenum Press, New York, N.Y.
    • Wilkinson, K. D., and M. Hochstrasser. 1998. The deubiquitinating enzymes. p. 99-125. In J.-M. Peters, J. R. Horris, and D. Finley (ed.), Ubiquitin and the biology of the cell. Plenum Press, New York, N.Y.
    • (1998) Ubiquitin and the Biology of the Cell , pp. 99-125
    • Wilkinson, K.D.1    Hochstrasser, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.