메뉴 건너뛰기




Volumn 4, Issue 1, 2005, Pages 73-83

Identification of sumoylated proteins by systematic immunoprecipitation of the budding yeast proteome

Author keywords

[No Author keywords available]

Indexed keywords

PROTEOME; SUMO PROTEIN;

EID: 14644392172     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M400166-MCP200     Document Type: Article
Times cited : (94)

References (47)
  • 1
    • 0942301187 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae ubiquitin-like protein Rub1 conjugates to cullin proteins Rtt101 and Cul3 in vivo
    • Laplaza, J. M., Bostick, M., Scholes, D. T., Curcio, M. J., and Callis, J. (2004) Saccharomyces cerevisiae ubiquitin-like protein Rub1 conjugates to cullin proteins Rtt101 and Cul3 in vivo. Biochem. J. 377, 459-467
    • (2004) Biochem. J. , vol.377 , pp. 459-467
    • Laplaza, J.M.1    Bostick, M.2    Scholes, D.T.3    Curcio, M.J.4    Callis, J.5
  • 2
    • 0344824569 scopus 로고    scopus 로고
    • Urmylation: A ubiquitin-like pathway that functions during invasive growth and budding in yeast
    • Goehring, A. S., Rivers, D. M., and Sprague, G. F., Jr. (2003) Urmylation: a ubiquitin-like pathway that functions during invasive growth and budding in yeast. Mol. Biol. Cell. 14, 4329-4341
    • (2003) Mol. Biol. Cell. , vol.14 , pp. 4329-4341
    • Goehring, A.S.1    Rivers, D.M.2    Sprague Jr., G.F.3
  • 3
    • 0033580444 scopus 로고    scopus 로고
    • A new protease required for cell-cycle progression in yeast
    • Li, S. J., and Hochstrasser, M. (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
  • 4
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • Johnson, E. S. (2004) Protein modification by SUMO. Annu. Rev. Biochem. 73, 355-382
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 5
    • 0030826334 scopus 로고    scopus 로고
    • Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p
    • Johnson, E. S., and Blobel, G. (1997) Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p. J. Biol. Chem. 272, 26799-26802
    • (1997) J. Biol. Chem. , vol.272 , pp. 26799-26802
    • Johnson, E.S.1    Blobel, G.2
  • 6
    • 0033615965 scopus 로고    scopus 로고
    • Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins
    • Johnson, E. S., and Blobel, G. (1999) Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins. J. Cell Biol. 147, 981-994
    • (1999) J. Cell Biol. , vol.147 , pp. 981-994
    • Johnson, E.S.1    Blobel, G.2
  • 7
    • 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., Schwienhorst, I., Dohmen, R. J., and Blobel, G. (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
  • 9
    • 0035929279 scopus 로고    scopus 로고
    • An E3-like factor that promotes SUMO conjugation to the yeast septins
    • Johnson, E. S., and Gupta, A. A. (2001) An E3-like factor that promotes SUMO conjugation to the yeast septins. Cell 106, 735-744
    • (2001) Cell , vol.106 , pp. 735-744
    • Johnson, E.S.1    Gupta, A.A.2
  • 10
    • 0034018312 scopus 로고    scopus 로고
    • The yeast ULP2 (SMT4) gene encodes a novel protease specific for the ubiquitin-like Smt3 protein
    • Li, S. J., and Hochstrasser, M. (2000) The yeast ULP2 (SMT4) gene encodes a novel protease specific for the ubiquitin-like Smt3 protein. Mol. Cell. Biol. 20, 2367-2377
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2367-2377
    • Li, S.J.1    Hochstrasser, M.2
  • 11
    • 0034523266 scopus 로고    scopus 로고
    • SUMO - Nonclassical ubiquitin
    • Melchior, F. (2000) SUMO - nonclassical ubiquitin. Annu. Rev. Cell Dev. Biol. 16, 591-626
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 591-626
    • Melchior, F.1
  • 12
    • 0034595239 scopus 로고    scopus 로고
    • Ubiquitin-like proteins: New wines in new bottles
    • Yeh, E. T., Gong, L., and Kamitani, T. (2000) Ubiquitin-like proteins: new wines in new bottles. Gene (Amst.) 248, 1-14
    • (2000) Gene (Amst.) , vol.248 , pp. 1-14
    • Yeh, E.T.1    Gong, L.2    Kamitani, T.3
  • 13
    • 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., Iwase, M., Konishi, M., Tanaka, M., Toh-e, A., and Kikuchi, Y. (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
  • 14
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege, C., Pfander, B., Moldovan, G. L., Pyrowolakis, G., and Jentsch, S. (2002) RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 419, 135-141
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 15
    • 0036291014 scopus 로고    scopus 로고
    • The SUMO-1 isopeptidase Smt4 is linked to centromeric cohesion through SUMO-1 modification of DNA topoisomerase II
    • Bachant, J., Alcasabas, A., Blat, Y., Kleckner, N., and Elledge, S. J. (2002) The SUMO-1 isopeptidase Smt4 is linked to centromeric cohesion through SUMO-1 modification of DNA topoisomerase II. Mol. Cell 9, 1169-1182
    • (2002) Mol. Cell , vol.9 , pp. 1169-1182
    • Bachant, J.1    Alcasabas, A.2    Blat, Y.3    Kleckner, N.4    Elledge, S.J.5
  • 16
    • 0242509262 scopus 로고    scopus 로고
    • SUMO-2/3 regulates topoisomerase II in mitosis
    • Azuma, Y., Arnaoutov, A., and Dasso, M. (2003) SUMO-2/3 regulates topoisomerase II in mitosis. J. Cell Biol. 163, 477-487
    • (2003) J. Cell Biol. , vol.163 , pp. 477-487
    • Azuma, Y.1    Arnaoutov, A.2    Dasso, M.3
  • 17
    • 0344736804 scopus 로고    scopus 로고
    • Pds5p regulates the maintenance of sister chromatid cohesion and is sumoylated to promote the dissolution of cohesion
    • Stead, K., Aguilar, C., Hartman, T., Drexel, M., Meluh, P., and Guacci, V. (2003) Pds5p regulates the maintenance of sister chromatid cohesion and is sumoylated to promote the dissolution of cohesion. J. Cell Biol. 163, 729-741
    • (2003) J. Cell Biol. , vol.163 , pp. 729-741
    • Stead, K.1    Aguilar, C.2    Hartman, T.3    Drexel, M.4    Meluh, P.5    Guacci, V.6
  • 18
    • 2342551489 scopus 로고    scopus 로고
    • Cdc14 and condensin control the dissolution of cohesin-independent chromosome linkages at repeated DNA
    • D'Amours, D., Stegmeier, F., and Amon, A. (2004) Cdc14 and condensin control the dissolution of cohesin-independent chromosome linkages at repeated DNA. Cell 117, 455-469
    • (2004) Cell , vol.117 , pp. 455-469
    • D'Amours, D.1    Stegmeier, F.2    Amon, A.3
  • 19
    • 8544273758 scopus 로고    scopus 로고
    • Global analysis of protein sumoylation in Saccharomyces cerevisiae
    • Wohlschlegel, J. A., Johnson, E. S., Reed, S. I., and Yates, J. R., III (2004) Global analysis of protein sumoylation in Saccharomyces cerevisiae. J. Biol. Chem. 279, 45662-45668
    • (2004) J. Biol. Chem. , vol.279 , pp. 45662-45668
    • Wohlschlegel, J.A.1    Johnson, E.S.2    Reed, S.I.3    Yates III, J.R.4
  • 20
    • 4744360999 scopus 로고    scopus 로고
    • A proteome-wide approach identifies sumoylated substrate proteins in yeast
    • Panse, V. G., Hardeland, U., Werner, T., Kuster, B., and Hurt, E. (2004) A proteome-wide approach identifies sumoylated substrate proteins in yeast. J. Biol. Chem. 279, 41346-41351
    • (2004) J. Biol. Chem. , vol.279 , pp. 41346-41351
    • Panse, V.G.1    Hardeland, U.2    Werner, T.3    Kuster, B.4    Hurt, E.5
  • 21
    • 3543018486 scopus 로고    scopus 로고
    • Global analyses of sumoylated proteins in Saccharomyces cerevisiae: Induction of protein sumoylation by cellular stresses
    • Zhou, W., Ryan, J. J., and Zhou, H. (2004) Global analyses of sumoylated proteins in Saccharomyces cerevisiae: induction of protein sumoylation by cellular stresses. J. Biol. Chem. 279, 32262-32268
    • (2004) J. Biol. Chem. , vol.279 , pp. 32262-32268
    • Zhou, W.1    Ryan, J.J.2    Zhou, H.3
  • 25
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S., and Hieter, P. (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 27
    • 0037872691 scopus 로고    scopus 로고
    • Osprey: A network visualization system
    • Breitkreutz, B. J., Stark, C., and Tyers, M. (2002) Osprey: a network visualization system. Genome Biol. http://genomebiology.com/2003/4/3/R22
    • (2002) Genome Biol.
    • Breitkreutz, B.J.1    Stark, C.2    Tyers, M.3
  • 31
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine, M. S., McKenzie, A., III, Demarini, D. J., Shah, N. G., Wach, A., Brachat, A., Philippsen, P., and Pringle, J. R. (1998) Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14, 953-961
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie III, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 32
    • 0035692234 scopus 로고    scopus 로고
    • Phosphate transport and sensing in Saccharomyces cerevisiae
    • Wykoff, D. D., and O'Shea, E. K. (2001) Phosphate transport and sensing in Saccharomyces cerevisiae. Genetics 159, 1491-1499
    • (2001) Genetics , vol.159 , pp. 1491-1499
    • Wykoff, D.D.1    O'Shea, E.K.2
  • 33
    • 0029852510 scopus 로고    scopus 로고
    • Sequence similarity between the 73-kilodalton protein of mammalian CPSF and a subunit of yeast polyadenylation factor I
    • Jenny, A., Minvielle-Sebastia, L., Preker, P. J., and Keller, W. (1996) Sequence similarity between the 73-kilodalton protein of mammalian CPSF and a subunit of yeast polyadenylation factor I. Science 274, 1514-1517
    • (1996) Science , vol.274 , pp. 1514-1517
    • Jenny, A.1    Minvielle-Sebastia, L.2    Preker, P.J.3    Keller, W.4
  • 34
    • 0034954166 scopus 로고    scopus 로고
    • The TFIID components human TAF(II)140 and Drosophila BIP2 (TAF(II)155) are novel metazoan homologues of yeast TAF(II)47 containing a histone fold and a PHD finger
    • Gangloff, Y. G., Pointud, J. C., Thuault, S., Carre, L., Romier, C., Muratoglu, S., Brand, M., Tora, L., Couderc, J. L., and Davidson, I. (2001) The TFIID components human TAF(II)140 and Drosophila BIP2 (TAF(II)155) are novel metazoan homologues of yeast TAF(II)47 containing a histone fold and a PHD finger. Mol. Cell. Biol. 21, 5109-5121
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5109-5121
    • Gangloff, Y.G.1    Pointud, J.C.2    Thuault, S.3    Carre, L.4    Romier, C.5    Muratoglu, S.6    Brand, M.7    Tora, L.8    Couderc, J.L.9    Davidson, I.10
  • 35
    • 0029083543 scopus 로고
    • Response of a yeast glycogen synthase gene to stress
    • Ni, H. T., and LaPorte, D. C. (1995) Response of a yeast glycogen synthase gene to stress. Mol. Microbiol. 16, 1197-1205
    • (1995) Mol. Microbiol. , vol.16 , pp. 1197-1205
    • Ni, H.T.1    LaPorte, D.C.2
  • 37
    • 0035107140 scopus 로고    scopus 로고
    • Yeast frameshift suppressor mutations in the genes coding for transcription factor Mbf1p and ribosomal protein S3: Evidence for autoregulation of S3 synthesis
    • Hendrick, J. L., Wilson, P. G., Edelman, I. I., Sandbaken, M. G., Ursic, D., and Culbertson, M. R. (2001) Yeast frameshift suppressor mutations in the genes coding for transcription factor Mbf1p and ribosomal protein S3: evidence for autoregulation of S3 synthesis. Genetics 157, 1141-1158
    • (2001) Genetics , vol.157 , pp. 1141-1158
    • Hendrick, J.L.1    Wilson, P.G.2    Edelman, I.I.3    Sandbaken, M.G.4    Ursic, D.5    Culbertson, M.R.6
  • 38
    • 0026714724 scopus 로고
    • SDH1, the gene encoding the succinate dehydrogenase flavoprotein subunit from Saccharomyces cerevisiae
    • Chapman, K. B., Solomon, S. D., and Boeke, J. D. (1992) SDH1, the gene encoding the succinate dehydrogenase flavoprotein subunit from Saccharomyces cerevisiae. Gene (Amst.) 118, 131-136
    • (1992) Gene (Amst.) , vol.118 , pp. 131-136
    • Chapman, K.B.1    Solomon, S.D.2    Boeke, J.D.3
  • 40
    • 0031934871 scopus 로고    scopus 로고
    • Mutational analysis of the Tup1 general repressor of yeast
    • Carrico, P. M., and Zitomer, R. S. (1998) Mutational analysis of the Tup1 general repressor of yeast. Genetics 148, 637-644
    • (1998) Genetics , vol.148 , pp. 637-644
    • Carrico, P.M.1    Zitomer, R.S.2
  • 41
    • 0037192523 scopus 로고    scopus 로고
    • Role of a ubiquitin-like modification in polarized morphogenesis
    • Dittmar, G. A., Wilkinson, C. R., Jedrzejewski, P. T., and Finley, D. (2002) Role of a ubiquitin-like modification in polarized morphogenesis. Science 295, 2442-2446
    • (2002) Science , vol.295 , pp. 2442-2446
    • Dittmar, G.A.1    Wilkinson, C.R.2    Jedrzejewski, P.T.3    Finley, D.4
  • 42
    • 0142216125 scopus 로고    scopus 로고
    • Attachment of the ubiquitin-related protein Urm1p to the antioxidant protein Ahp1p
    • Goehring, A. S., Rivers, D. M., and Sprague, G. F., Jr. (2003) Attachment of the ubiquitin-related protein Urm1p to the antioxidant protein Ahp1p. Eukaryot. Cell 2, 930-936
    • (2003) Eukaryot. Cell , vol.2 , pp. 930-936
    • Goehring, A.S.1    Rivers, D.M.2    Sprague Jr., G.F.3
  • 44
    • 0035831475 scopus 로고    scopus 로고
    • Yeast nuclear extract contains two major forms of RNA polymerase II mediator complexes
    • Liu, Y., Ranish, J. A., Aebersold, R., and Hahn, S. (2001) Yeast nuclear extract contains two major forms of RNA polymerase II mediator complexes. J. Biol. Chem. 276, 7169-7175
    • (2001) J. Biol. Chem. , vol.276 , pp. 7169-7175
    • Liu, Y.1    Ranish, J.A.2    Aebersold, R.3    Hahn, S.4
  • 45
    • 0027169905 scopus 로고
    • Yeast and mammalian metallothioneins functionally substitute for yeast copper-zinc superoxide dismutase
    • Tamai, K. T., Gralla, E. B., Ellerby, L. M., Valentine, J. S., and Thiele, D. J. (1993) Yeast and mammalian metallothioneins functionally substitute for yeast copper-zinc superoxide dismutase. Proc. Natl. Acad. Sci. U. S. A. 90, 8013-8017
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 8013-8017
    • Tamai, K.T.1    Gralla, E.B.2    Ellerby, L.M.3    Valentine, J.S.4    Thiele, D.J.5
  • 46
    • 0029073989 scopus 로고
    • Implication of mammalian ribosomal protein S3 in the processing of DNA damage
    • Kim, J., Chubatsu, L. S., Admon, A., Stahl, J., Fellous, R., and Linn, S. (1995) Implication of mammalian ribosomal protein S3 in the processing of DNA damage. J. Biol. Chem. 270, 13620-13629
    • (1995) J. Biol. Chem. , vol.270 , pp. 13620-13629
    • Kim, J.1    Chubatsu, L.S.2    Admon, A.3    Stahl, J.4    Fellous, R.5    Linn, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.