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Volumn 37, Issue 2, 2004, Pages 409-418

Functional transplantation of the sumoylation machinery into Escherichia coli

Author keywords

Aos1; Isopeptide bond; LEF1; Posttranslational modification; Protein polymerization; SUMO; Sumoylation; Uba2; Ubc9

Indexed keywords

DNA; GLUTATHIONE TRANSFERASE; PEPTIDE; PROTEIN; UBIQUITIN CONJUGATING ENZYME;

EID: 4444242508     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2004.07.001     Document Type: Article
Times cited : (26)

References (36)
  • 1
    • 0036237383 scopus 로고    scopus 로고
    • Versatile protein tag, SUMO: Its enzymology and biological function
    • K.I. Kim, S.H. Baek, and C.H. Chung Versatile protein tag, SUMO: its enzymology and biological function J. Cell. Physiol. 191 2002 257 268
    • (2002) J. Cell. Physiol. , vol.191 , pp. 257-268
    • Kim, K.I.1    Baek, S.H.2    Chung, C.H.3
  • 2
    • 0034523266 scopus 로고    scopus 로고
    • SUMOâ€"nonclassical ubiquitin
    • F. Melchior SUMOâ€"nonclassical ubiquitin Annu. Rev. Cell Dev. Biol. 16 2000 591 626
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 591-626
    • Melchior, F.1
  • 4
    • 0034705319 scopus 로고    scopus 로고
    • SUMO-1 modification of Mdm2 prevents its self-ubiquitination and increases Mdm2 ability to ubiquitinate p53
    • T. Buschmann, S.Y. Fuchs, C.G. Lee, Z.Q. Pan, and Z. Ronai SUMO-1 modification of Mdm2 prevents its self-ubiquitination and increases Mdm2 ability to ubiquitinate p53 Cell 101 2000 753 762
    • (2000) Cell , vol.101 , pp. 753-762
    • Buschmann, T.1    Fuchs, S.Y.2    Lee, C.G.3    Pan, Z.Q.4    Ronai, Z.5
  • 5
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation
    • J.M. Desterro, M.S. Rodriguez, and R.T. Hay SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation Mol. Cell 2 1998 233 239
    • (1998) Mol. Cell , vol.2 , pp. 233-239
    • Desterro, J.M.1    Rodriguez, M.S.2    Hay, R.T.3
  • 6
    • 0036300965 scopus 로고    scopus 로고
    • Ubiquitin-related modifier SUMO1 and nucleocytoplasmic transport
    • A. Pichler, and F. Melchior Ubiquitin-related modifier SUMO1 and nucleocytoplasmic transport Traffic 3 2002 381 387
    • (2002) Traffic , vol.3 , pp. 381-387
    • Pichler, A.1    Melchior, F.2
  • 7
    • 2942649047 scopus 로고    scopus 로고
    • How to activate a damage-tolerant polymerase: Consequences of PCNA modifications by ubiquitin and SUMO
    • H.D. Ulrich How to activate a damage-tolerant polymerase: consequences of PCNA modifications by ubiquitin and SUMO Cell Cycle 3 2004 15 18
    • (2004) Cell Cycle , vol.3 , pp. 15-18
    • Ulrich, H.D.1
  • 8
    • 0037088588 scopus 로고    scopus 로고
    • Covalent attachment of the SUMO-1 protein to the negative regulatory domain of the c-Myb transcription factor modifies its stability and transactivation capacity
    • J. Bies, J. Markus, and L. Wolff Covalent attachment of the SUMO-1 protein to the negative regulatory domain of the c-Myb transcription factor modifies its stability and transactivation capacity J. Biol. Chem. 277 2002 8999 9009
    • (2002) J. Biol. Chem. , vol.277 , pp. 8999-9009
    • Bies, J.1    Markus, J.2    Wolff, L.3
  • 9
    • 0037382641 scopus 로고    scopus 로고
    • Post-translational modification by the small ubiquitin-related modifier SUMO has big effects on transcription factor activity
    • G. Gill Post-translational modification by the small ubiquitin-related modifier SUMO has big effects on transcription factor activity Curr. Opin. Genet. Dev. 13 2003 108 113
    • (2003) Curr. Opin. Genet. Dev. , vol.13 , pp. 108-113
    • Gill, G.1
  • 10
    • 0037351924 scopus 로고    scopus 로고
    • Transactivation properties of c-Myb are critically dependent on two SUMO-1 acceptor sites that are conjugated in a PIASy enhanced manner
    • O. Dahle, T.O. Andersen, O. Nordgard, V. Matre, G. Del Sal, and O.S. Gabrielsen Transactivation properties of c-Myb are critically dependent on two SUMO-1 acceptor sites that are conjugated in a PIASy enhanced manner Eur. J. Biochem. 270 2003 1338 1348
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1338-1348
    • Dahle, O.1    Andersen, T.O.2    Nordgard, O.3    Matre, V.4    Del Sal, G.5    Gabrielsen, O.S.6
  • 11
    • 0037295721 scopus 로고    scopus 로고
    • Modification with SUMO. a role in transcriptional regulation
    • A. Verger, J. Perdomo, and M. Crossley Modification with SUMO. A role in transcriptional regulation EMBO Rep. 4 2003 137 142
    • (2003) EMBO Rep. , vol.4 , pp. 137-142
    • Verger, A.1    Perdomo, J.2    Crossley, M.3
  • 12
    • 0035986065 scopus 로고    scopus 로고
    • The promyelocytic leukemia nuclear body: Sites of activity?
    • C.H. Eskiw, and D.P. Bazett-Jones The promyelocytic leukemia nuclear body: sites of activity? Biochem. Cell Biol. 80 2002 301 310
    • (2002) Biochem. Cell Biol. , vol.80 , pp. 301-310
    • Eskiw, C.H.1    Bazett-Jones, D.P.2
  • 13
    • 0035576737 scopus 로고    scopus 로고
    • A new RING for SUMO: Wrestling transcriptional responses into nuclear bodies with PIAS family E3 SUMO ligases
    • P.K. Jackson A new RING for SUMO: wrestling transcriptional responses into nuclear bodies with PIAS family E3 SUMO ligases Genes Dev. 15 2001 3053 3058
    • (2001) Genes Dev. , vol.15 , pp. 3053-3058
    • Jackson, P.K.1
  • 14
    • 0036069554 scopus 로고    scopus 로고
    • Top-SUMO wrestles centromeric cohesion
    • B.A. Pinsky, and S. Biggins Top-SUMO wrestles centromeric cohesion Dev. Cell 3 2002 4 6
    • (2002) Dev. Cell , vol.3 , pp. 4-6
    • Pinsky, B.A.1    Biggins, S.2
  • 16
    • 0034054669 scopus 로고    scopus 로고
    • Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3
    • H. Saitoh, and J. Hinchey Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3 J. Biol. Chem. 275 2000 6252 6258
    • (2000) J. Biol. Chem. , vol.275 , pp. 6252-6258
    • Saitoh, H.1    Hinchey, J.2
  • 18
    • 0030794729 scopus 로고    scopus 로고
    • The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer
    • E.S. Johnson, I. Schwienhorst, R.J. Dohmen, and G. Blobel The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer EMBO J. 16 1997 5509 5519
    • (1997) EMBO J. , vol.16 , pp. 5509-5519
    • Johnson, E.S.1    Schwienhorst, I.2    Dohmen, R.J.3    Blobel, G.4
  • 19
    • 0030826334 scopus 로고    scopus 로고
    • Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p
    • E.S. Johnson, and G. Blobel Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p J. Biol. Chem. 272 1997 26799 26802
    • (1997) J. Biol. Chem. , vol.272 , pp. 26799-26802
    • Johnson, E.S.1    Blobel, G.2
  • 20
    • 0033537828 scopus 로고    scopus 로고
    • Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1
    • J.M. Desterro, M.S. Rodriguez, G.D. Kemp, and R.T. Hay Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1 J. Biol. Chem. 274 1999 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
  • 22
    • 0035877693 scopus 로고    scopus 로고
    • The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification
    • D.A. Sampson, M. Wang, and M.J. Matunis The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification J. Biol. Chem. 276 2001 21664 21669
    • (2001) J. Biol. Chem. , vol.276 , pp. 21664-21669
    • Sampson, D.A.1    Wang, M.2    Matunis, M.J.3
  • 24
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • C.M. Pickart Mechanisms underlying ubiquitination Annu. Rev. Biochem. 70 2001 503 533
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 25
    • 0035966066 scopus 로고    scopus 로고
    • Yeast Ull1/Siz1 is a novel SUMO1/Smt3 ligase for septin components and functions as an adaptor between conjugating enzyme and substrates
    • Y. Takahashi, T. Kahyo, E.A. Toh, H. Yasuda, and Y. Kikuchi Yeast Ull1/Siz1 is a novel SUMO1/Smt3 ligase for septin components and functions as an adaptor between conjugating enzyme and substrates J. Biol. Chem. 276 2001 48973 48977
    • (2001) J. Biol. Chem. , vol.276 , pp. 48973-48977
    • Takahashi, Y.1    Kahyo, T.2    Toh, E.A.3    Yasuda, H.4    Kikuchi, Y.5
  • 26
    • 0036291475 scopus 로고    scopus 로고
    • PIAS proteins modulate transcription factors by functioning as SUMO-1 ligases
    • N. Kotaja, U. Karvonen, O.A. Janne, and J.J. Palvimo PIAS proteins modulate transcription factors by functioning as SUMO-1 ligases Mol. Cell. Biol. 22 2002 5222 5234
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5222-5234
    • Kotaja, N.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 27
    • 0035918226 scopus 로고    scopus 로고
    • SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting
    • M.S. Rodriguez, C. Dargemont, and R.T. Hay SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting J. Biol. Chem. 276 2001 12654 12659
    • (2001) J. Biol. Chem. , vol.276 , pp. 12654-12659
    • Rodriguez, M.S.1    Dargemont, C.2    Hay, R.T.3
  • 28
    • 0038434056 scopus 로고    scopus 로고
    • A superfamily of protein tags: Ubiquitin, SUMO and related modifiers
    • D.C. Schwartz, and M. Hochstrasser A superfamily of protein tags: ubiquitin, SUMO and related modifiers Trends Biochem. Sci. 28 2003 321 328
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 321-328
    • Schwartz, D.C.1    Hochstrasser, M.2
  • 30
    • 0034065822 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis: Biological regulation via destruction
    • A. Ciechanover, A. Orian, and A.L. Schwartz Ubiquitin-mediated proteolysis: biological regulation via destruction Bioessays 22 2000 442 451
    • (2000) Bioessays , vol.22 , pp. 442-451
    • Ciechanover, A.1    Orian, A.2    Schwartz, A.L.3
  • 31
    • 0035576878 scopus 로고    scopus 로고
    • PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies
    • S. Sachdev, L. Bruhn, H. Sieber, A. Pichler, F. Melchior, and R. Grosschedl PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies Genes Dev. 15 2001 3088 3103
    • (2001) Genes Dev. , vol.15 , pp. 3088-3103
    • Sachdev, S.1    Bruhn, L.2    Sieber, H.3    Pichler, A.4    Melchior, F.5    Grosschedl, R.6
  • 32
    • 1842850624 scopus 로고    scopus 로고
    • Generation of SUMO-1 modified proteins in E. coli: Towards understanding the biochemistry/structural biology of the SUMO-1 pathway
    • Y. Uchimura, M. Nakao, and H. Saitoh Generation of SUMO-1 modified proteins in E. coli: towards understanding the biochemistry/structural biology of the SUMO-1 pathway FEBS Lett. 564 2004 85 90
    • (2004) FEBS Lett. , vol.564 , pp. 85-90
    • Uchimura, Y.1    Nakao, M.2    Saitoh, H.3
  • 33
    • 0030819591 scopus 로고    scopus 로고
    • Improved broad-host-range RK2 vectors useful for high and low regulated gene expression levels in gram-negative bacteria
    • J.M. Blatny, T. Brautaset, H.C. Winther-Larsen, P. Karunakaran, and S. Valla Improved broad-host-range RK2 vectors useful for high and low regulated gene expression levels in gram-negative bacteria Plasmid 38 1997 35 51
    • (1997) Plasmid , vol.38 , pp. 35-51
    • Blatny, J.M.1    Brautaset, T.2    Winther-Larsen, H.C.3    Karunakaran, P.4    Valla, S.5
  • 35
    • 0028879976 scopus 로고
    • Automation of micro-preparation and enzymatic cleavage of gel electrophoretically separated proteins
    • T. Houthaeve, H. Gausepohl, M. Mann, and K. Ashman Automation of micro-preparation and enzymatic cleavage of gel electrophoretically separated proteins FEBS Lett. 376 1995 91 94
    • (1995) FEBS Lett. , vol.376 , pp. 91-94
    • Houthaeve, T.1    Gausepohl, H.2    Mann, M.3    Ashman, K.4
  • 36
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • A. Shevchenko, M. Wilm, O. Vorm, and M. Mann Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels Anal. Chem. 68 1996 850 858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4


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