메뉴 건너뛰기




Volumn 363, Issue 3, 2006, Pages 660-672

blm3-1 Is an Allele of UBP3, a Ubiquitin Protease that Appears to Act During Transcription of Damaged DNA

Author keywords

bleomycin; Blm10 PA200; Blm3; transcription; Ubp3

Indexed keywords

BLEOMYCIN; BLM 10 PROTEIN; CANAVANINE; ENZYME BLM3 1; ENZYME UBP3; PHLEOMYCIN; PROTEIN; PROTEINASE; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 33749244672     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.08.073     Document Type: Article
Times cited : (9)

References (45)
  • 1
    • 0038495946 scopus 로고    scopus 로고
    • Protective mechanisms against the antitumor agent bleomycin: lessons from Saccharomyces cerevisiae
    • Ramotar D., and Wang H. Protective mechanisms against the antitumor agent bleomycin: lessons from Saccharomyces cerevisiae. Curr. Genet. 43 (2003) 213-224
    • (2003) Curr. Genet. , vol.43 , pp. 213-224
    • Ramotar, D.1    Wang, H.2
  • 2
    • 0025878391 scopus 로고
    • Further characterizations of bleomycin-sensitive (blm) mutants of Saccharomyces cerevisiae with implications for a radiomimetic model
    • Moore C.W. Further characterizations of bleomycin-sensitive (blm) mutants of Saccharomyces cerevisiae with implications for a radiomimetic model. J. Bacteriol. 173 (1991) 3605-3608
    • (1991) J. Bacteriol. , vol.173 , pp. 3605-3608
    • Moore, C.W.1
  • 4
    • 0036646488 scopus 로고    scopus 로고
    • PA200, a nuclear proteasome activator involved in DNA repair
    • Ustrell V., Hoffman L., Pratt G., and Rechsteiner M. PA200, a nuclear proteasome activator involved in DNA repair. EMBO J. 21 (2002) 3516-3525
    • (2002) EMBO J. , vol.21 , pp. 3516-3525
    • Ustrell, V.1    Hoffman, L.2    Pratt, G.3    Rechsteiner, M.4
  • 5
    • 33749241490 scopus 로고    scopus 로고
    • Iwanczyk, J., Sadre-Bazzaz, K., Ferrell, K., Kondrashkina, E., Formosa, T. Hill, C. P. & Ortega, J. Structure of the Blm10-20S proteasome complex by cryo-electron microscopy. Insights into the mechanism of activation of mature yeast proteasomes. J. Mol. Biol. In the press.
  • 8
    • 0037050026 scopus 로고    scopus 로고
    • Functional organization of the yeast proteome by systematic analysis of protein complexes
    • Gavin A.C., Bosche M., Krause R., Grandi P., Marzioch M., Bauer A., et al. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415 (2002) 141-147
    • (2002) Nature , vol.415 , pp. 141-147
    • Gavin, A.C.1    Bosche, M.2    Krause, R.3    Grandi, P.4    Marzioch, M.5    Bauer, A.6
  • 9
    • 0037050004 scopus 로고    scopus 로고
    • Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
    • Ho Y., Gruhler A., Heilbut A., Bader G.D., Moore L., Adams S.L., et al. Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 415 (2002) 180-183
    • (2002) Nature , vol.415 , pp. 180-183
    • Ho, Y.1    Gruhler, A.2    Heilbut, A.3    Bader, G.D.4    Moore, L.5    Adams, S.L.6
  • 10
    • 0242522904 scopus 로고    scopus 로고
    • Blm3 is part of nascent proteasomes and is involved in a late stage of nuclear proteasome assembly
    • Fehlker M., Wendler P., Lehmann A., and Enenkel C. Blm3 is part of nascent proteasomes and is involved in a late stage of nuclear proteasome assembly. EMBO Rep 4 (2002) 959-963
    • (2002) EMBO Rep , vol.4 , pp. 959-963
    • Fehlker, M.1    Wendler, P.2    Lehmann, A.3    Enenkel, C.4
  • 12
    • 0347473810 scopus 로고    scopus 로고
    • Integration of chemical-genetic and genetic interaction data links bioactive compounds to cellular target pathways
    • Parsons A.B., Brost R.L., Ding H., Li Z., Zhang C., Sheikh B., et al. Integration of chemical-genetic and genetic interaction data links bioactive compounds to cellular target pathways. Nature Biotechnol. 22 (2004) 62-69
    • (2004) Nature Biotechnol. , vol.22 , pp. 62-69
    • Parsons, A.B.1    Brost, R.L.2    Ding, H.3    Li, Z.4    Zhang, C.5    Sheikh, B.6
  • 13
    • 0842282564 scopus 로고    scopus 로고
    • A genome-wide screen in Saccharomyces cerevisiae reveals altered transport as a mechanism of resistance to the anticancer drug bleomycin
    • Aouida M., Page N., Leduc A., Peter M., and Ramotar D. A genome-wide screen in Saccharomyces cerevisiae reveals altered transport as a mechanism of resistance to the anticancer drug bleomycin. Cancer Res. 64 (2004) 1102-1109
    • (2004) Cancer Res. , vol.64 , pp. 1102-1109
    • Aouida, M.1    Page, N.2    Leduc, A.3    Peter, M.4    Ramotar, D.5
  • 14
    • 11844287006 scopus 로고    scopus 로고
    • Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors
    • Rechsteiner M., and Hill C.P. Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors. Trends Cell Biol. 15 (2005) 27-33
    • (2005) Trends Cell Biol. , vol.15 , pp. 27-33
    • Rechsteiner, M.1    Hill, C.P.2
  • 16
    • 0037013202 scopus 로고    scopus 로고
    • Pheromone-dependent ubiquitination of the mitogen-activated protein kinase kinase Ste7
    • Wang Y., and Dohlman H.G. Pheromone-dependent ubiquitination of the mitogen-activated protein kinase kinase Ste7. J. Biol. Chem. 277 (2002) 15766-15772
    • (2002) J. Biol. Chem. , vol.277 , pp. 15766-15772
    • Wang, Y.1    Dohlman, H.G.2
  • 17
    • 0038387865 scopus 로고    scopus 로고
    • Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23
    • Cohen M., Stutz F., Belgareh N., Haguenauer-Tsapis R., and Dargemont C. Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23. Nature Cell Biol. 5 (2003) 661-667
    • (2003) Nature Cell Biol. , vol.5 , pp. 661-667
    • Cohen, M.1    Stutz, F.2    Belgareh, N.3    Haguenauer-Tsapis, R.4    Dargemont, C.5
  • 18
    • 0346101801 scopus 로고    scopus 로고
    • Deubiquitination, a new player in Golgi to endoplasmic reticulum retrograde transport
    • Cohen M., Stutz F., and Dargemont C. Deubiquitination, a new player in Golgi to endoplasmic reticulum retrograde transport. J. Biol. Chem. 278 (2003) 51989-51992
    • (2003) J. Biol. Chem. , vol.278 , pp. 51989-51992
    • Cohen, M.1    Stutz, F.2    Dargemont, C.3
  • 21
    • 0031821736 scopus 로고    scopus 로고
    • Isolation of UBP3, encoding a de-ubiquitinating enzyme, as a multicopy suppressor of a heat-shock mutant strain of S. cerevisiae
    • Baxter B.K., and Craig E.A. Isolation of UBP3, encoding a de-ubiquitinating enzyme, as a multicopy suppressor of a heat-shock mutant strain of S. cerevisiae. Curr. Genet. 33 (1998) 412-419
    • (1998) Curr. Genet. , vol.33 , pp. 412-419
    • Baxter, B.K.1    Craig, E.A.2
  • 22
    • 0030598895 scopus 로고    scopus 로고
    • A deubiquitinating enzyme interacts with SIR4 and regulates silencing in S. cerevisiae
    • Moazed D., and Johnson A.D. A deubiquitinating enzyme interacts with SIR4 and regulates silencing in S. cerevisiae. Cell 86 (1996) 667-677
    • (1996) Cell , vol.86 , pp. 667-677
    • Moazed, D.1    Johnson, A.D.2
  • 23
    • 9644278072 scopus 로고    scopus 로고
    • Purification of active TFIID from Saccharomyces cerevisiae. Extensive promoter contacts and co-activator function
    • Auty R., Steen H., Myers L.C., Persinger J., Bartholomew B., Gygi S.P., and Buratowski S. Purification of active TFIID from Saccharomyces cerevisiae. Extensive promoter contacts and co-activator function. J. Biol. Chem. 279 (2004) 49973-49981
    • (2004) J. Biol. Chem. , vol.279 , pp. 49973-49981
    • Auty, R.1    Steen, H.2    Myers, L.C.3    Persinger, J.4    Bartholomew, B.5    Gygi, S.P.6    Buratowski, S.7
  • 24
    • 6344289159 scopus 로고    scopus 로고
    • Expression of the expanded YFL007w ORF and assignment of the gene name BLM10
    • Doherty K., Pramanik A., Pride L., Lukose J., and Moore C.W. Expression of the expanded YFL007w ORF and assignment of the gene name BLM10. Yeast 21 (2004) 1021-1023
    • (2004) Yeast , vol.21 , pp. 1021-1023
    • Doherty, K.1    Pramanik, A.2    Pride, L.3    Lukose, J.4    Moore, C.W.5
  • 25
    • 0037096154 scopus 로고    scopus 로고
    • Revisiting the yeast chromosome VI DNA sequence reveals a correction merging YFL007w and YFL006w to a single ORF
    • Robben J., Hertveldt K., and Volckaert G. Revisiting the yeast chromosome VI DNA sequence reveals a correction merging YFL007w and YFL006w to a single ORF. Yeast 19 (2002) 699-702
    • (2002) Yeast , vol.19 , pp. 699-702
    • Robben, J.1    Hertveldt, K.2    Volckaert, G.3
  • 27
    • 3242887157 scopus 로고    scopus 로고
    • CD-Search: protein domain annotations on the fly
    • Marchler-Bauer A., and Bryant S.H. CD-Search: protein domain annotations on the fly. Nucl. Acids Res. 32 (2004) W327-W331
    • (2004) Nucl. Acids Res. , vol.32
    • Marchler-Bauer, A.1    Bryant, S.H.2
  • 28
    • 0026457302 scopus 로고
    • Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family
    • Baker R.T., Tobias J.W., and Varshavsky A. Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family. J. Biol. Chem. 267 (1992) 23364-23375
    • (1992) J. Biol. Chem. , vol.267 , pp. 23364-23375
    • Baker, R.T.1    Tobias, J.W.2    Varshavsky, A.3
  • 29
    • 0037636027 scopus 로고    scopus 로고
    • The establishment, inheritance, and function of silenced chromatin in Saccharomyces cerevisiae
    • Rusche L.N., Kirchmaier A.L., and Rine J. The establishment, inheritance, and function of silenced chromatin in Saccharomyces cerevisiae. Annu. Rev. Biochem. 72 (2003) 481-516
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 481-516
    • Rusche, L.N.1    Kirchmaier, A.L.2    Rine, J.3
  • 30
    • 0032736986 scopus 로고    scopus 로고
    • An allele of the yeast RPB7 gene, encoding an essential subunit of RNA polymerase II, reduces cellular resistance to the antitumor drug bleomycin
    • He C.H., and Ramotar D. An allele of the yeast RPB7 gene, encoding an essential subunit of RNA polymerase II, reduces cellular resistance to the antitumor drug bleomycin. Biochem. Cell Biol. 77 (1999) 375-382
    • (1999) Biochem. Cell Biol. , vol.77 , pp. 375-382
    • He, C.H.1    Ramotar, D.2
  • 31
    • 1342269199 scopus 로고    scopus 로고
    • Large-scale screening of yeast mutants for sensitivity to the IMP dehydrogenase inhibitor 6-azauracil
    • Riles L., Shaw R.J., Johnston M., and Reines D. Large-scale screening of yeast mutants for sensitivity to the IMP dehydrogenase inhibitor 6-azauracil. Yeast 21 (2004) 241-248
    • (2004) Yeast , vol.21 , pp. 241-248
    • Riles, L.1    Shaw, R.J.2    Johnston, M.3    Reines, D.4
  • 32
    • 0033805924 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae transcription elongation mutants are defective in PUR5 induction in response to nucleotide depletion
    • Shaw R.J., and Reines D. Saccharomyces cerevisiae transcription elongation mutants are defective in PUR5 induction in response to nucleotide depletion. Mol. Cell Biol. 20 (2000) 7427-7437
    • (2000) Mol. Cell Biol. , vol.20 , pp. 7427-7437
    • Shaw, R.J.1    Reines, D.2
  • 33
    • 0033854297 scopus 로고    scopus 로고
    • Genetic interactions between TFIIS and the Swi-Snf chromatin-remodeling complex
    • Davie J.K., and Kane C.M. Genetic interactions between TFIIS and the Swi-Snf chromatin-remodeling complex. Mol. Cell Biol. 20 (2000) 5960-5973
    • (2000) Mol. Cell Biol. , vol.20 , pp. 5960-5973
    • Davie, J.K.1    Kane, C.M.2
  • 34
    • 0037424418 scopus 로고    scopus 로고
    • Cleavage, but not read-through, stimulation activity is responsible for three biologic functions of transcription elongation factor S-II
    • Ubukata T., Shimizu T., Adachi N., Sekimizu K., and Nakanishi T. Cleavage, but not read-through, stimulation activity is responsible for three biologic functions of transcription elongation factor S-II. J. Biol. Chem. 278 (2003) 8580-8585
    • (2003) J. Biol. Chem. , vol.278 , pp. 8580-8585
    • Ubukata, T.1    Shimizu, T.2    Adachi, N.3    Sekimizu, K.4    Nakanishi, T.5
  • 35
    • 0037591460 scopus 로고    scopus 로고
    • Intrinsic transcript cleavage in yeast RNA polymerase II elongation complexes
    • Weilbaecher R.G., Awrey D.E., Edwards A.M., and Kane C.M. Intrinsic transcript cleavage in yeast RNA polymerase II elongation complexes. J. Biol. Chem. 278 (2003) 24189-24199
    • (2003) J. Biol. Chem. , vol.278 , pp. 24189-24199
    • Weilbaecher, R.G.1    Awrey, D.E.2    Edwards, A.M.3    Kane, C.M.4
  • 36
    • 1942421800 scopus 로고    scopus 로고
    • Genetic interactions of DST1 in Saccharomyces cerevisiae suggest a role of TFIIS in the initiation-elongation transition
    • Malagon F., Tong A.H., Shafer B.K., and Strathern J.N. Genetic interactions of DST1 in Saccharomyces cerevisiae suggest a role of TFIIS in the initiation-elongation transition. Genetics 166 (2004) 1215-1227
    • (2004) Genetics , vol.166 , pp. 1215-1227
    • Malagon, F.1    Tong, A.H.2    Shafer, B.K.3    Strathern, J.N.4
  • 37
    • 20444428382 scopus 로고    scopus 로고
    • Multiple mechanisms confining RNA polymerase II ubiquitylation to polymerases undergoing transcriptional arrest
    • Somesh B.P., Reid J., Liu W.F., Sogaard T.M., Erdjument-Bromage H., Tempst P., and Svejstrup J.Q. Multiple mechanisms confining RNA polymerase II ubiquitylation to polymerases undergoing transcriptional arrest. Cell 121 (2005) 913-923
    • (2005) Cell , vol.121 , pp. 913-923
    • Somesh, B.P.1    Reid, J.2    Liu, W.F.3    Sogaard, T.M.4    Erdjument-Bromage, H.5    Tempst, P.6    Svejstrup, J.Q.7
  • 38
    • 0033166761 scopus 로고    scopus 로고
    • A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme
    • Wittschieben B.O., Otero G., de Bizemont T., Fellows J., Erdjument-Bromage H., Ohba R., et al. A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme. Mol. Cell 4 (1999) 123-128
    • (1999) Mol. Cell , vol.4 , pp. 123-128
    • Wittschieben, B.O.1    Otero, G.2    de Bizemont, T.3    Fellows, J.4    Erdjument-Bromage, H.5    Ohba, R.6
  • 39
    • 0032911635 scopus 로고    scopus 로고
    • Functional organization of the yeast SAGA complex: distinct components involved in structural integrity, nucleosome acetylation, and TATA-binding protein interaction
    • Sterner D.E., Grant P.A., Roberts S.M., Duggan L.J., Belotserkovskaya R., Pacella L.A., et al. Functional organization of the yeast SAGA complex: distinct components involved in structural integrity, nucleosome acetylation, and TATA-binding protein interaction. Mol. Cell Biol. 19 (1999) 86-98
    • (1999) Mol. Cell Biol. , vol.19 , pp. 86-98
    • Sterner, D.E.1    Grant, P.A.2    Roberts, S.M.3    Duggan, L.J.4    Belotserkovskaya, R.5    Pacella, L.A.6
  • 40
    • 0032004953 scopus 로고    scopus 로고
    • Evidence that Spt4, Spt5, and Spt6 control transcription elongation by RNA polymerase II in Saccharomyces cerevisiae
    • Hartzog G.A., Wada T., Handa H., and Winston F. Evidence that Spt4, Spt5, and Spt6 control transcription elongation by RNA polymerase II in Saccharomyces cerevisiae. Genes Dev. 12 (1998) 357-369
    • (1998) Genes Dev. , vol.12 , pp. 357-369
    • Hartzog, G.A.1    Wada, T.2    Handa, H.3    Winston, F.4
  • 41
    • 1942489340 scopus 로고    scopus 로고
    • New HEAT-like repeat motifs in proteins regulating proteasome structure and function
    • Kajava A.V., Gorbea C., Ortega J., Rechsteiner M., and Steven A.C. New HEAT-like repeat motifs in proteins regulating proteasome structure and function. J. Struct. Biol. 146 (2004) 425-430
    • (2004) J. Struct. Biol. , vol.146 , pp. 425-430
    • Kajava, A.V.1    Gorbea, C.2    Ortega, J.3    Rechsteiner, M.4    Steven, A.C.5
  • 42
    • 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 Sugino A. New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 74 (1988) 527-534
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.