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Volumn 2, Issue 3, 2011, Pages 135-139

Ubiquitin and transcription: The SCFMet30/Met4 pathway, a (protein-) complex issue

Author keywords

Met30; Met4; SCF ligase; Sulfur metabolites; Ubiquitin

Indexed keywords

MESSENGER RNA; MET4 PROTEIN; NUCLEIC ACID BINDING PROTEIN; RNA POLYMERASE II; TRANSCRIPTION FACTOR; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 79958695933     PISSN: 21541264     EISSN: 21541272     Source Type: Journal    
DOI: 10.4161/trns.2.3.15903     Document Type: Article
Times cited : (12)

References (39)
  • 2
    • 33749346301 scopus 로고    scopus 로고
    • Modification of proteins by ubiquitin and ubiquitin-like proteins
    • Kerscher O, Felberbaum R, Hochstrasser M. Modification of proteins by ubiquitin and ubiquitin-like proteins. Annu Rev Cell Dev Biol 2006; 22:159-180.
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 159-180
    • Kerscher, O.1    Felberbaum, R.2    Hochstrasser, M.3
  • 3
    • 0037335034 scopus 로고    scopus 로고
    • How the ubiquitin-protea-some system controls transcription
    • Muratani M, Tansey WP. How the ubiquitin-protea-some system controls transcription. Nat Rev Mol Cell Biol 2003; 4:192-201.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 192-201
    • Muratani, M.1    Tansey, W.P.2
  • 4
    • 78650246421 scopus 로고    scopus 로고
    • A transcriptional activator is part of an SCF ubiquitin ligase to control degradation of its cofactors
    • Ouni I, Flick K, Kaiser P. A transcriptional activator is part of an SCF ubiquitin ligase to control degradation of its cofactors. Mol Cell 2010; 40:954-964.
    • (2010) Mol Cell , vol.40 , pp. 954-964
    • Ouni, I.1    Flick, K.2    Kaiser, P.3
  • 5
    • 78649922622 scopus 로고    scopus 로고
    • The chromatin signaling pathway: Diverse mechanisms of recruitment of histone-modifying enzymes and varied biological outcomes
    • Smith E, Shilatifard A. The chromatin signaling pathway: diverse mechanisms of recruitment of histone-modifying enzymes and varied biological outcomes. Mol Cell 2010; 40:689-701.
    • (2010) Mol Cell , vol.40 , pp. 689-701
    • Smith, E.1    Shilatifard, A.2
  • 6
    • 33847070442 scopus 로고    scopus 로고
    • The role of chromatin during transcription
    • Li B, Carey M, Workman JL. The role of chromatin during transcription. Cell 2007; 128:707-719.
    • (2007) Cell , vol.128 , pp. 707-719
    • Li, B.1    Carey, M.2    Workman, J.L.3
  • 7
    • 0016751733 scopus 로고
    • Isolation and characterization of protein A24, a "histone-like" nonhistone chromosomal protein
    • Goldknopf IL, Taylor CW, Baum RM, Yeoman LC, Olson MO, Prestayko AW, et al. Isolation and characterization of protein A24, a "histone-like" nonhistone chromosomal protein. J Biol Chem 1975; 250:7182-7187
    • (1975) J Biol Chem , vol.250 , pp. 7182-7187
    • Goldknopf, I.L.1    Taylor, C.W.2    Baum, R.M.3    Yeoman, L.C.4    Olson, M.O.5    Prestayko, A.W.6
  • 8
    • 38149098408 scopus 로고    scopus 로고
    • Histone H2A monoubiquitination represses transcription by inhibiting RNA polymerase II transcriptional elongation
    • Zhou W, Zhu P, Wang J, Pascual G, Ohgi KA, Lozach J, et al. Histone H2A monoubiquitination represses transcription by inhibiting RNA polymerase II transcriptional elongation. Mol Cell 2008; 29:69-80.
    • (2008) Mol Cell , vol.29 , pp. 69-80
    • Zhou, W.1    Zhu, P.2    Wang, J.3    Pascual, G.4    Ohgi, K.A.5    Lozach, J.6
  • 10
    • 33845254071 scopus 로고    scopus 로고
    • Histone ubiqui-tylation and the regulation of transcription
    • Osley MA, Fleming AB, Kao CF. Histone ubiqui-tylation and the regulation of transcription. Results Probl Cell Differ 2006; 41:47-75.
    • (2006) Results Probl Cell Differ , vol.41 , pp. 47-75
    • Osley, M.A.1    Fleming, A.B.2    Kao, C.F.3
  • 11
    • 40849106789 scopus 로고    scopus 로고
    • Histone ubiquitination: Triggering gene activity
    • Weake VM, Workman JL. Histone ubiquitination: triggering gene activity. Mol Cell 2008; 29:653-663.
    • (2008) Mol Cell , vol.29 , pp. 653-663
    • Weake, V.M.1    Workman, J.L.2
  • 12
    • 0032827035 scopus 로고    scopus 로고
    • Rsp5 ubiquitin-protein ligase mediates DNA damage-induced degradation of the large subunit of RNA polymerase II in Saccharomyces cerevisiae
    • Beaudenon SL, Huacani MR, Wang G, McDonnell DP, Huibregtse JM. Rsp5 ubiquitin-protein ligase mediates DNA damage-induced degradation of the large subunit of RNA polymerase II in Saccharomyces cerevisiae. Mol Cell Biol 1999; 19:6972-6979.
    • (1999) Mol Cell Biol , vol.19 , pp. 6972-6979
    • Beaudenon, S.L.1    Huacani, M.R.2    Wang, G.3    McDonnell, D.P.4    Huibregtse, J.M.5
  • 13
    • 63049138291 scopus 로고    scopus 로고
    • Damage control: DNA repair, transcription and the ubiquitin-proteasome system
    • Daulny A, Tansey WP. Damage control: DNA repair, transcription and the ubiquitin-proteasome system. DNA Repair (Amst) 2009; 8:444-448.
    • (2009) DNA Repair (Amst) , vol.8 , pp. 444-448
    • Daulny, A.1    Tansey, W.P.2
  • 14
    • 20444428382 scopus 로고    scopus 로고
    • Multiple mechanisms confining RNA polymerase II ubiquitylation to polymerases undergoing transcriptional arrest
    • Somesh BP, Reid J, Liu WF, Sogaard TM, Erdjument-Bromage H, Tempst P, et al. Multiple mechanisms confining RNA polymerase II ubiquitylation to polymerases undergoing transcriptional arrest. Cell 2005; 121:913-923.
    • (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
  • 16
    • 77954523079 scopus 로고    scopus 로고
    • The Prp19 complex and the Usp4Sart3 deubiquitinating enzyme control reversible ubiquitination at the spliceosome
    • Song EJ, Werner SL, Neubauer J, Stegmeier F, Aspden J, Rio D, et al. The Prp19 complex and the Usp4Sart3 deubiquitinating enzyme control reversible ubiquitination at the spliceosome. Genes Dev 2010; 24:1434-1447.
    • (2010) Genes Dev , vol.24 , pp. 1434-1447
    • Song, E.J.1    Werner, S.L.2    Neubauer, J.3    Stegmeier, F.4    Aspden, J.5    Rio, D.6
  • 17
    • 77950578839 scopus 로고    scopus 로고
    • Nuclear export of mRNA and its regulation by ubiquitylation
    • Durairaj G, Garg P, Bhaumik SR. Nuclear export of mRNA and its regulation by ubiquitylation. RNA Biol 2009; 6:531-535.
    • (2009) RNA Biol , vol.6 , pp. 531-535
    • Durairaj, G.1    Garg, P.2    Bhaumik, S.R.3
  • 19
    • 0033574789 scopus 로고    scopus 로고
    • Control of mRNA decay by heat shock-ubiquitin-proteasome pathway
    • Laroia G, Cuesta R, Brewer G, Schneider RJ. Control of mRNA decay by heat shock-ubiquitin-proteasome pathway. Science 1999; 284:499-502.
    • (1999) Science , vol.284 , pp. 499-502
    • Laroia, G.1    Cuesta, R.2    Brewer, G.3    Schneider, R.J.4
  • 20
    • 0034193442 scopus 로고    scopus 로고
    • Transcriptional regulation: Kamikaze activators
    • Thomas D, Tyers M. Transcriptional regulation: Kamikaze activators. Curr Biol 2000; 10:341-343.
    • (2000) Curr Biol , vol.10 , pp. 341-343
    • Thomas, D.1    Tyers, M.2
  • 21
    • 0035979738 scopus 로고    scopus 로고
    • Regulation of transcriptional activation domain function by ubiquitin
    • Salghetti SE, Caudy AA, Chenoweth JG, Tansey WP. Regulation of transcriptional activation domain function by ubiquitin. Science 2001; 293:1651-1653.
    • (2001) Science , vol.293 , pp. 1651-1653
    • Salghetti, S.E.1    Caudy, A.A.2    Chenoweth, J.G.3    Tansey, W.P.4
  • 22
    • 0034268493 scopus 로고    scopus 로고
    • Activation of a membrane-bound transcription factor by regulated ubiqui-tin/proteasome-dependent processing
    • Hoppe T, Matuschewski K, Rape M, Schlenker S, Ulrich HD, Jentsch S. Activation of a membrane-bound transcription factor by regulated ubiqui-tin/proteasome-dependent processing. Cell 2000; 102:577-586.
    • (2000) Cell , vol.102 , pp. 577-586
    • Hoppe, T.1    Matuschewski, K.2    Rape, M.3    Schlenker, S.4    Ulrich, H.D.5    Jentsch, S.6
  • 23
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NFkB1 precursor protein and the activation of NFkB
    • Palombella VJ, Rando OJ, Goldberg AL, Maniatis T The ubiquitin-proteasome pathway is required for processing the NFkB1 precursor protein and the activation of NFkB. Cell 1994; 78:773-785.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 24
    • 0348134742 scopus 로고    scopus 로고
    • Mono versus polyubiquitination: Differential control of p53 fate by Mdm2
    • Li M, Brooks CL, Wu-Baer F, Chen D, Baer R, Gu W Mono versus polyubiquitination: differential control of p53 fate by Mdm2. Science 2003; 302:1972-1975.
    • (2003) Science , vol.302 , pp. 1972-1975
    • Li, M.1    Brooks, C.L.2    Wu-Baer, F.3    Chen, D.4    Baer, R.5    Gu, W.6
  • 26
    • 0031457095 scopus 로고    scopus 로고
    • Metabolism of sulfur amino acids in Saccharomyces cerevisiae
    • Thomas D, Surdin-Kerjan Y. Metabolism of sulfur amino acids in Saccharomyces cerevisiae. Microbiol Mol Biol Rev 1997; 61:503-532.
    • (1997) Microbiol Mol Biol Rev , vol.61 , pp. 503-532
    • Thomas, D.1    Surdin-Kerjan, Y.2
  • 27
    • 34248354813 scopus 로고    scopus 로고
    • Met30: Connecting environmental and intracellular conditions to cell division
    • Met30: connecting environmental and intracellular conditions to cell division. Cell Div 2006; 1:16.
    • (2006) Cell Div , vol.1 , pp. 16
    • Kaiser, P.1    Su, N.Y.2    Yen, J.L.3    Ouni, I.4    Flick, K.5
  • 28
    • 0034604341 scopus 로고    scopus 로고
    • Regulation of transcription by ubiquitination without proteolysis: Cdc34/SCF(Met30)-mediated inactivation of the transcription factor Met4
    • Kaiser P, Flick K, Wittenberg C, Reed SI. Regulation of transcription by ubiquitination without proteolysis: Cdc34/SCF(Met30)-mediated inactivation of the transcription factor Met4. Cell 2000; 102:303-314.
    • (2000) Cell , vol.102 , pp. 303-314
    • Kaiser, P.1    Flick, K.2    Wittenberg, C.3    Reed, S.I.4
  • 29
    • 0034677224 scopus 로고    scopus 로고
    • Feedback-regulated degradation of the transcriptional activator Met4 is triggered by the SCF(Met30) complex
    • Rouillon A, Barbey R, Patton EE, Tyers M, Thomas D. Feedback-regulated degradation of the transcriptional activator Met4 is triggered by the SCF(Met30) complex. EMBO J 2000; 19:282-294.
    • (2000) EMBO J , vol.19 , pp. 282-294
    • Rouillon, A.1    Barbey, R.2    Patton, E.E.3    Tyers, M.4    Thomas, D.5
  • 30
    • 3242696232 scopus 로고    scopus 로고
    • Proteolysis-independent regulation of the transcription factor Met4 by a single Lys 48-linked ubiquitin chain
    • Flick K, Ouni I, Wohlschlegel JA, Capati C, McDonald WH, Yates JR, et al. Proteolysis-independent regulation of the transcription factor Met4 by a single Lys 48-linked ubiquitin chain. Nat Cell Biol 2004; 6:634-641.
    • (2004) Nat Cell Biol , vol.6 , pp. 634-641
    • Flick, K.1    Ouni, I.2    Wohlschlegel, J.A.3    Capati, C.4    McDonald, W.H.5    Yates, J.R.6
  • 31
    • 0036348150 scopus 로고    scopus 로고
    • Dual regulation of the met4 transcription factor by ubiquitin-dependent degradation and inhibition of promoter recruitment
    • Kuras L, Rouillon A, Lee T, Barbey R, Tyers M, Thomas D. Dual regulation of the met4 transcription factor by ubiquitin-dependent degradation and inhibition of promoter recruitment. Mol Cell 2002; 10:69-80.
    • (2002) Mol Cell , vol.10 , pp. 69-80
    • Kuras, L.1    Rouillon, A.2    Lee, T.3    Barbey, R.4    Tyers, M.5    Thomas, D.6
  • 33
    • 33744967943 scopus 로고    scopus 로고
    • A ubiquitin-interacting motif protects polyubiquitinated Met4 from degradation by the 26S proteasome
    • Flick K, Raasi S, Zhang H, Yen JL, Kaiser P. A ubiquitin-interacting motif protects polyubiquitinated Met4 from degradation by the 26S proteasome. Nat Cell Biol 2006; 8:509-515.
    • (2006) Nat Cell Biol , vol.8 , pp. 509-515
    • Flick, K.1    Raasi, S.2    Zhang, H.3    Yen, J.L.4    Kaiser, P.5
  • 34
    • 78650534710 scopus 로고    scopus 로고
    • Physiologically relevant and portable tandem ubiquitin-binding domain stabilizes polyu-biquitylated proteins
    • Tyrrell A, Flick K, Kleiger G, Zhang H, Deshaies RJ, Kaiser P. Physiologically relevant and portable tandem ubiquitin-binding domain stabilizes polyu-biquitylated proteins. Proc Natl Acad Sci USA 2010; 107:19796-19801.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 19796-19801
    • Tyrrell, A.1    Flick, K.2    Kleiger, G.3    Zhang, H.4    Deshaies, R.J.5    Kaiser, P.6
  • 35
    • 78650241154 scopus 로고    scopus 로고
    • Targeted ubiquitylation: The prey becomes predator
    • Yan J, Xiong Y Targeted ubiquitylation: the prey becomes predator. Mol Cell 2010; 40:853-855.
    • (2010) Mol Cell , vol.40 , pp. 853-855
    • Yan, J.1    Xiong, Y.2
  • 36
    • 0032476584 scopus 로고    scopus 로고
    • Multiple transcriptional activation complexes tether the yeast activator Met4 to DNA
    • Blaiseau PL, Thomas D. Multiple transcriptional activation complexes tether the yeast activator Met4 to DNA. EMBO J 1998; 17:6327-6336.
    • (1998) EMBO J , vol.17 , pp. 6327-6336
    • Blaiseau, P.L.1    Thomas, D.2
  • 39
    • 34247194608 scopus 로고    scopus 로고
    • Single-stranded DNA-binding proteins regulate the abundance of LIM domain and LIM domain-binding proteins
    • Xu Z, Meng X, Cai Y, Liang H, Nagarajan L, Brandt SJ. Single-stranded DNA-binding proteins regulate the abundance of LIM domain and LIM domain-binding proteins. Genes Dev 2007; 21:942-955.
    • (2007) Genes Dev , vol.21 , pp. 942-955
    • Xu, Z.1    Meng, X.2    Cai, Y.3    Liang, H.4    Nagarajan, L.5    Brandt, S.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.