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Volumn 34, Issue 21, 2014, Pages 3955-3967

Efficient mRNA polyadenylation requires a ubiquitin-like domain, a zinc knuckle, and a RING finger domain, all contained in the Mpe1 protein

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; MESSENGER RNA PRECURSOR; MPE1 PROTEIN; PAP1 PROTEIN; PEPTIDES AND PROTEINS; POLYNUCLEOTIDE ADENYLYLTRANSFERASE; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR; FUNGAL RNA; MPE1 PROTEIN, S CEREVISIAE; PAP1 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84907833888     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.00077-14     Document Type: Article
Times cited : (19)

References (83)
  • 1
    • 84879408529 scopus 로고    scopus 로고
    • Alternative cleavage and polyadenylation: extent, regulation and function
    • Elkon R, Ugalde AP, Agami R. 2013. Alternative cleavage and polyadenylation: extent, regulation and function. Nat. Rev. Genet. 14:496-506. http://dx.doi.org/10.1038/nrg3482.
    • (2013) Nat. Rev. Genet. , vol.14 , pp. 496-506
    • Elkon, R.1    Ugalde, A.P.2    Agami, R.3
  • 2
    • 84885078620 scopus 로고    scopus 로고
    • DNA damage induces targeted, genome-wide variation of poly(A) sites in budding yeast
    • Graber JH, Nazeer FI, Yeh PC, Kuehner JN, Borikar S, Hoskinson D, Moore CL. 2013. DNA damage induces targeted, genome-wide variation of poly(A) sites in budding yeast. Genome Res. 23:1690-1703. http://dx.doi.org/10.1101/gr.144964.112.
    • (2013) Genome Res , vol.23 , pp. 1690-1703
    • Graber, J.H.1    Nazeer, F.I.2    Yeh, P.C.3    Kuehner, J.N.4    Borikar, S.5    Hoskinson, D.6    Moore, C.L.7
  • 3
    • 84878151459 scopus 로고    scopus 로고
    • Alternative cleavage and polyadenylation: the long and short of it
    • Tian B, Manley JL. 2013. Alternative cleavage and polyadenylation: the long and short of it. Trends Biochem. Sci. 38:312-320. http://dx.doi.org /10.1016/j.tibs.2013.03.005.
    • (2013) Trends Biochem. Sci. , vol.38 , pp. 312-320
    • Tian, B.1    Manley, J.L.2
  • 4
    • 84857761249 scopus 로고    scopus 로고
    • Pre-mRNA 3'-end processing complex assembly and function
    • Chan S, Choi EA, Shi Y. 2011. Pre-mRNA 3'-end processing complex assembly and function. Wiley Interdiscip. Rev. RNA 2:321-335. http://dx.doi.org/10.1002/wrna.54.
    • (2011) Wiley Interdiscip. Rev. RNA , vol.2 , pp. 321-335
    • Chan, S.1    Choi, E.A.2    Shi, Y.3
  • 5
    • 84858115939 scopus 로고    scopus 로고
    • mRNA 3' end processing factors: a phylogenetic comparison
    • Darmon SK, Lutz CS. 2012. mRNA 3' end processing factors: a phylogenetic comparison. Comp. Funct. Genomics 2012:876893. http://dx.doi.org/10.1155/2012/876893.
    • (2012) Comp. Funct. Genomics. , vol.2012 , pp. 876893
    • Darmon, S.K.1    Lutz, C.S.2
  • 6
    • 77953284100 scopus 로고    scopus 로고
    • Molecular mechanisms of eukaryotic premRNA 3' end processing regulation
    • Millevoi S, Vagner S. 2010. Molecular mechanisms of eukaryotic premRNA 3' end processing regulation. Nucleic Acids Res. 38:2757-2774. http://dx.doi.org/10.1093/nar/gkp1176.
    • (2010) Nucleic Acids Res , vol.38 , pp. 2757-2774
    • Millevoi, S.1    Vagner, S.2
  • 7
    • 0035196964 scopus 로고    scopus 로고
    • Mpe1, a zinc knuckle protein, is an essential component of yeast cleavage and polyadenylation factor required for the cleavage and polyadenylation of mRNA
    • Vo LT, Minet M, Schmitter JM, Lacroute F, Wyers F. 2001. Mpe1, a zinc knuckle protein, is an essential component of yeast cleavage and polyadenylation factor required for the cleavage and polyadenylation of mRNA. Mol. Cell. Biol. 21:8346-8356. http://dx.doi.org/10.1128/MCB.21.24.8346-8356.2001.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 8346-8356
    • Vo, L.T.1    Minet, M.2    Schmitter, J.M.3    Lacroute, F.4    Wyers, F.5
  • 8
    • 32044441848 scopus 로고    scopus 로고
    • DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA pro-cessing and ubiquitin-like pathways
    • Pugh DJ, Eiso AB, Faro A, Lutya PT, Hoffmann E, Rees DJ. 2006. DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA pro-cessing and ubiquitin-like pathways. BMC Struct. Biol. 6:1. http://dx.doi.org/10.1186/1472-6807-6-1.
    • (2006) BMC Struct. Biol. , vol.6 , pp. 1
    • Pugh, D.J.1    Eiso, A.B.2    Faro, A.3    Lutya, P.T.4    Hoffmann, E.5    Rees, D.J.6
  • 9
    • 0031024084 scopus 로고    scopus 로고
    • PACT: cloning and characterization of a cellular p53 binding protein that interacts with Rb
    • Simons A, Melamed-Bessudo C, Wolkowicz R, Sperling J, Sperling R, Eisenbach L, Rotter V. 1997. PACT: cloning and characterization of a cellular p53 binding protein that interacts with Rb. Oncogene 14:145-155. http://dx.doi.org/10.1038/sj.onc.1200825.
    • (1997) Oncogene , vol.14 , pp. 145-155
    • Simons, A.1    Melamed-Bessudo, C.2    Wolkowicz, R.3    Sperling, J.4    Sperling, R.5    Eisenbach, L.6    Rotter, V.7
  • 12
    • 29144518532 scopus 로고    scopus 로고
    • The ubiquitin domain superfold: structure-based sequence alignments and characterization of binding epitopes
    • Kiel C, Serrano L. 2006. The ubiquitin domain superfold: structure-based sequence alignments and characterization of binding epitopes. J. Mol. Biol. 355:821-844. http://dx.doi.org/10.1016/j.jmb.2005.10.010.
    • (2006) J. Mol. Biol. , vol.355 , pp. 821-844
    • Kiel, C.1    Serrano, L.2
  • 13
    • 68949221689 scopus 로고    scopus 로고
    • Ubiquitin-like and ubiquitin-associated domain proteins: significance in proteasomal degradation
    • Su V, Lau AF. 2009. Ubiquitin-like and ubiquitin-associated domain proteins: significance in proteasomal degradation. Cell. Mol. Life Sci. 66: 2819-2833. http://dx.doi.org/10.1007/s00018-009-0048-9.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 2819-2833
    • Su, V.1    Lau, A.F.2
  • 14
    • 84868576866 scopus 로고    scopus 로고
    • Recognition of the let-7g miRNA precursor by human Lin28B
    • Ali PS, Ghoshdastider U, Hoffmann J, Brutschy B, Filipek S. 2012. Recognition of the let-7g miRNA precursor by human Lin28B. FEBS Lett. 586:3986-3990. http://dx.doi.org/10.1016/j.febslet.2012.09.034.
    • (2012) FEBS Lett , vol.586 , pp. 3986-3990
    • Ali, P.S.1    Ghoshdastider, U.2    Hoffmann, J.3    Brutschy, B.4    Filipek, S.5
  • 15
    • 0033017499 scopus 로고    scopus 로고
    • The splicing factors 9G8 and SRp20 transactivate splicing through different and specific enhancers
    • Cavaloc Y, Bourgeois CF, Kister L, Stevenin J. 1999. The splicing factors 9G8 and SRp20 transactivate splicing through different and specific enhancers. RNA 5:468-483. http://dx.doi.org/10.1017/S1355838299981967.
    • (1999) RNA , vol.5 , pp. 468-483
    • Cavaloc, Y.1    Bourgeois, C.F.2    Kister, L.3    Stevenin, J.4
  • 16
    • 80054811443 scopus 로고    scopus 로고
    • Air1 zinc knuckles 4 and 5 and a conserved IWRXY motif are critical for the function and integrity of the Trf4/5-Air1/2-Mtr4 polyadenylation (TRAMP) RNA quality control complex
    • Fasken MB, Leung SW, Banerjee A, Kodani MO, Chavez R, Bowman EA, Purohit MK, Rubinson ME, Rubinson EH, Corbett AH. 2011. Air1 zinc knuckles 4 and 5 and a conserved IWRXY motif are critical for the function and integrity of the Trf4/5-Air1/2-Mtr4 polyadenylation (TRAMP) RNA quality control complex. J. Biol. Chem. 286:37429 - 37445. http://dx.doi.org/10.1074/jbc.M111.271494.
    • (2011) J. Biol. Chem. , vol.286 , pp. 37429-37445
    • Fasken, M.B.1    Leung, S.W.2    Banerjee, A.3    Kodani, M.O.4    Chavez, R.5    Bowman, E.A.6    Purohit, M.K.7    Rubinson, M.E.8    Rubinson, E.H.9    Corbett, A.H.10
  • 17
    • 33748757138 scopus 로고    scopus 로고
    • An extended RNA binding site for the yeast branch point-binding protein and the role of its zinc knuckle domains in RNA binding
    • Garrey SM, Voelker R, Berglund JA. 2006. An extended RNA binding site for the yeast branch point-binding protein and the role of its zinc knuckle domains in RNA binding. J. Biol. Chem. 281:27443-27453. http://dx.doi.org/10.1074/jbc.M603137200.
    • (2006) J. Biol. Chem. , vol.281 , pp. 27443-27453
    • Garrey, S.M.1    Voelker, R.2    Berglund, J.A.3
  • 18
    • 84863204260 scopus 로고    scopus 로고
    • Air2p is critical for the assembly and RNA-binding of the TRAMP complex and the KOW domain of Mtr4p is crucial for exosome activation
    • Holub P, Lalakova J, Cerna H, Pasulka J, Sarazova M, Hrazdilova K, Arce MS, Hobor F, Stefl R, Vanacova S. 2012. Air2p is critical for the assembly and RNA-binding of the TRAMP complex and the KOW domain of Mtr4p is crucial for exosome activation. Nucleic Acids Res. 40: 5679-5693. http://dx.doi.org/10.1093/nar/gks223.
    • (2012) Nucleic Acids Res , vol.40 , pp. 5679-5693
    • Holub, P.1    Lalakova, J.2    Cerna, H.3    Pasulka, J.4    Sarazova, M.5    Hrazdilova, K.6    Arce, M.S.7    Hobor, F.8    Stefl, R.9    Vanacova, S.10
  • 19
    • 84855421472 scopus 로고    scopus 로고
    • Structural basis of pre-let-7miRNArecognition by the zinc knuckles of pluripotency factor Lin28
    • Loughlin FE, Gebert LF, Towbin H, Brunschweiger A, Hall J, Allain FH. 2012. Structural basis of pre-let-7miRNArecognition by the zinc knuckles of pluripotency factor Lin28. Nat. Struct. Mol. Biol. 19:84-89. http://dx.doi.org/10.1038/nsmb.2202.
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 84-89
    • Loughlin, F.E.1    Gebert, L.F.2    Towbin, H.3    Brunschweiger, A.4    Hall, J.5    Allain, F.H.6
  • 20
    • 80051766524 scopus 로고    scopus 로고
    • Structural determinants and mechanism of HIV-1 genome packaging
    • Lu K, Heng X, Summers MF. 2011. Structural determinants and mechanism of HIV-1 genome packaging. J. Mol. Biol. 410:609-633. http://dx.doi.org/10.1016/j.jmb.2011.04.029.
    • (2011) J. Mol. Biol. , vol.410 , pp. 609-633
    • Lu, K.1    Heng, X.2    Summers, M.F.3
  • 21
    • 67649964217 scopus 로고    scopus 로고
    • RING domain E3 ubiquitin ligases
    • Deshaies RJ, Joazeiro CA. 2009. RING domain E3 ubiquitin ligases. Annu. Rev. Biochem. 78:399-434. http://dx.doi.org/10.1146/annurev.biochem.78.101807.093809.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 399-434
    • Deshaies, R.J.1    Joazeiro, C.A.2
  • 22
    • 0037459172 scopus 로고    scopus 로고
    • U-box proteins as a new family of ubiquitin ligases
    • Hatakeyama S, Nakayama KI. 2003. U-box proteins as a new family of ubiquitin ligases. Biochem. Biophys. Res. Commun. 302:635-645. http: //dx.doi.org/10.1016/S0006-291X(03)00245-6.
    • (2003) Biochem. Biophys. Res. Commun. , vol.302 , pp. 635-645
    • Hatakeyama, S.1    Nakayama, K.I.2
  • 24
    • 84890176335 scopus 로고    scopus 로고
    • RING-type E3 ligases: master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination
    • Metzger MB, Pruneda JN, Klevit RE, Weissman AM. 2014. RING-type E3 ligases: master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination. Biochim. Biophys. Acta 1843:47-60. http://dx.doi.org/10.1016/j.bbamcr.2013.05.026.
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 47-60
    • Metzger, M.B.1    Pruneda, J.N.2    Klevit, R.E.3    Weissman, A.M.4
  • 25
    • 16244373679 scopus 로고    scopus 로고
    • Multiubiquitylation by E4 enzymes: 'one size' doesn't fit all
    • Hoppe T. 2005. Multiubiquitylation by E4 enzymes: 'one size' doesn't fit all. Trends Biochem. Sci. 30:183-187. http://dx.doi.org/10.1016/j.tibs.2005.02.004.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 183-187
    • Hoppe, T.1
  • 26
    • 56249103765 scopus 로고    scopus 로고
    • RBBP6 interacts with multifunctional protein YB-1 through its RING finger domain, leading to ubiquitination and proteosomal degradation of YB-1
    • Chibi M, Meyer M, Skepu A, Rees DJG, Moolman-Smook JC, Pugh DJR. 2008. RBBP6 interacts with multifunctional protein YB-1 through its RING finger domain, leading to ubiquitination and proteosomal degradation of YB-1. J. Mol. Biol. 384:908-916. http://dx.doi.org/10.1016/j.jmb.2008.09.060.
    • (2008) J. Mol. Biol. , vol.384 , pp. 908-916
    • Chibi, M.1    Meyer, M.2    Skepu, A.3    Rees, D.J.G.4    Moolman-Smook, J.C.5    Pugh, D.J.R.6
  • 29
    • 84861869979 scopus 로고    scopus 로고
    • Ubiquitin and proteasomes in transcription
    • Geng F, Wenzel S, Tansey WP. 2012. Ubiquitin and proteasomes in transcription. Annu. Rev. Biochem. 81:177-201. http://dx.doi.org/10.1146/annurev-biochem-052110-120012.
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 177-201
    • Geng, F.1    Wenzel, S.2    Tansey, W.P.3
  • 31
    • 79957496447 scopus 로고    scopus 로고
    • Keeping mRNPs in check during assembly and nuclear export
    • Tutucci E, Stutz F. 2011. Keeping mRNPs in check during assembly and nuclear export. Nat. Rev. Mol. Cell Biol. 12:377-384. http://dx.doi.org/10.1038/nrm3119.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 377-384
    • Tutucci, E.1    Stutz, F.2
  • 32
    • 0032548998 scopus 로고    scopus 로고
    • Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly
    • Ramos PC, Hockendorff J, Johnson ES, Varshavsky A, Dohmen RJ. 1998. Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly. Cell 92:489- 499. http://dx.doi.org/10.1016/S0092-8674(00)80942-3.
    • (1998) Cell , vol.92 , pp. 489-499
    • Ramos, P.C.1    Hockendorff, J.2    Johnson, E.S.3    Varshavsky, A.4    Dohmen, R.J.5
  • 33
    • 0027457543 scopus 로고
    • The PRE4 gene codes for a subunit of the yeast proteasome necessary for peptidylglutamyl-peptide-hydrolyzing activity Mutations link the proteasome to stress- and ubiquitin-dependent proteolysis
    • Hilt W, Enenkel C, Gruhler A, Singer T, Wolf DH. 1993. The PRE4 gene codes for a subunit of the yeast proteasome necessary for peptidylglutamyl-peptide-hydrolyzing activity. Mutations link the proteasome to stress- and ubiquitin-dependent proteolysis. J. Biol. Chem. 268:3479- 3486.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3479-3486
    • Hilt, W.1    Enenkel, C.2    Gruhler, A.3    Singer, T.4    Wolf, D.H.5
  • 34
    • 24044539185 scopus 로고    scopus 로고
    • Regulation of yeast mRNA 3' end processing by phosphorylation
    • He X, Moore C. 2005. Regulation of yeast mRNA 3' end processing by phosphorylation. Mol. Cell 19:619-629. http://dx.doi.org/10.1016/j.molcel.2005.07.016.
    • (2005) Mol. Cell , vol.19 , pp. 619-629
    • He, X.1    Moore, C.2
  • 35
    • 0030455820 scopus 로고    scopus 로고
    • Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast
    • James P, Halladay J, Craig EA. 1996. Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast. Genetics 144: 1425-1436.
    • (1996) Genetics , vol.144 , pp. 1425-1436
    • James, P.1    Halladay, J.2    Craig, E.A.3
  • 36
    • 0030974313 scopus 로고    scopus 로고
    • 'Marker swap' plasmids: convenient tools for budding yeast molecular genetics
    • Cross FR. 1997. 'Marker swap' plasmids: convenient tools for budding yeast molecular genetics. Yeast 13:647-653. http://dx.doi.org/10.1002 /(SICI)1097-0061(19970615)13:7_647::AID-YEA115 3.0.CO;2-#.
    • (1997) Yeast , vol.13 , pp. 647-653
    • Cross, F.R.1
  • 37
    • 0023484186 scopus 로고
    • 5-Fluoroorotic acid as a selective agent in yeast molecular genetics
    • Boeke JD, Trueheart J, Natsoulis G, Fink GR. 1987. 5-Fluoroorotic acid as a selective agent in yeast molecular genetics. Methods Enzymol. 154: 164-175. http://dx.doi.org/10.1016/0076-6879(87)54076-9.
    • (1987) Methods Enzymol , vol.154 , pp. 164-175
    • Boeke, J.D.1    Trueheart, J.2    Natsoulis, G.3    Fink, G.R.4
  • 38
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho SN, Hunt HD, Horton RM, Pullen JK, Pease LR. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51-59. http://dx.doi.org/10.1016/0378-1119(89)90358-2.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 39
    • 0032721092 scopus 로고    scopus 로고
    • Pta1, a component of yeast CF II, is required for both cleavage and poly(A) addition of mRNA precursor
    • Zhao J, Kessler M, Helmling S, O'Connor JP, Moore C. 1999. Pta1, a component of yeast CF II, is required for both cleavage and poly(A) addition of mRNA precursor. Mol. Cell. Biol. 19:7733-7740.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7733-7740
    • Zhao, J.1    Kessler, M.2    Helmling, S.3    O'Connor, J.P.4    Moore, C.5
  • 40
    • 0025853324 scopus 로고
    • The shortlivedMAT _2 transcriptional regulator is ubiquitinated in vivo
    • Hochstrasser M, Ellison MJ, Chau V, Varshavsky A. 1991. The shortlivedMAT _2 transcriptional regulator is ubiquitinated in vivo. Proc. Natl. Acad. Sci. U. S. A. 88:4606-4610. http://dx.doi.org/10.1073/pnas.88.11.4606.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 4606-4610
    • Hochstrasser, M.1    Ellison, M.J.2    Chau, V.3    Varshavsky, A.4
  • 41
    • 0035933149 scopus 로고    scopus 로고
    • Five subunits are required for reconstitution of the cleavage and polyadenylation activities of Saccharomyces cerevisiae cleavage factor I
    • Gross S, Moore C. 2001. Five subunits are required for reconstitution of the cleavage and polyadenylation activities of Saccharomyces cerevisiae cleavage factor I. Proc. Natl. Acad. Sci. U. S. A. 98:6080-6085. http://dx.doi.org/10.1073/pnas.101046598.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 6080-6085
    • Gross, S.1    Moore, C.2
  • 42
    • 0035000153 scopus 로고    scopus 로고
    • Fip1 regulates the activity of poly(A) polymerase through multiple interactions
    • Helmling S, Zhelkovsky A, Moore CL. 2001. Fip1 regulates the activity of poly(A) polymerase through multiple interactions. Mol. Cell. Biol. 21: 2026-2037. http://dx.doi.org/10.1128/MCB.21.6.2026-2037.2001.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2026-2037
    • Helmling, S.1    Zhelkovsky, A.2    Moore, C.L.3
  • 43
    • 0025334099 scopus 로고
    • RNA processing in vitro produces mature 3' ends of a variety of Saccharomyces cerevisiae mRNAs
    • Butler JS, Sadhale PP, Platt T. 1990. RNA processing in vitro produces mature 3' ends of a variety of Saccharomyces cerevisiae mRNAs. Mol. Cell. Biol. 10:2599-2605.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2599-2605
    • Butler, J.S.1    Sadhale, P.P.2    Platt, T.3
  • 44
    • 0035876112 scopus 로고    scopus 로고
    • Recognition of polyadenylation sites in yeast pre-mRNAs by cleavage and polyadenylation factor
    • Dichtl B, Keller W. 2001. Recognition of polyadenylation sites in yeast pre-mRNAs by cleavage and polyadenylation factor. EMBO J. 20:3197- 3209. http://dx.doi.org/10.1093/emboj/20.12.3197.
    • (2001) EMBO J , vol.20 , pp. 3197-3209
    • Dichtl, B.1    Keller, W.2
  • 45
    • 0034841844 scopus 로고    scopus 로고
    • The tandem affinity purification (TAP) method: a general procedure of protein complex purification
    • Puig O, Caspary F, Rigaut G, Rutz B, Bouveret E, Bragado-Nilsson E, Wilm M, Seraphin B. 2001. The tandem affinity purification (TAP) method: a general procedure of protein complex purification. Methods 24:218-229. http://dx.doi.org/10.1006/meth.2001.1183.
    • (2001) Methods , vol.24 , pp. 218-229
    • Puig, O.1    Caspary, F.2    Rigaut, G.3    Rutz, B.4    Bouveret, E.5    Bragado-Nilsson, E.6    Wilm, M.7    Seraphin, B.8
  • 46
    • 40149109321 scopus 로고    scopus 로고
    • A systematic library for comprehensive overexpression screens in Saccharomyces cerevisiae
    • Jones GM, Stalker J, Humphray S, West A, Cox T, Rogers J, Dunham I, Prelich G. 2008. A systematic library for comprehensive overexpression screens in Saccharomyces cerevisiae. Nat. Methods 5:239-241. http://dx.doi.org/10.1038/nmeth.1181.
    • (2008) Nat. Methods , vol.5 , pp. 239-241
    • Jones, G.M.1    Stalker, J.2    Humphray, S.3    West, A.4    Cox, T.5    Rogers, J.6    Dunham, I.7    Prelich, G.8
  • 47
    • 64649086745 scopus 로고    scopus 로고
    • The essential N terminus of the Pta1 scaffold protein is required for snoRNA transcription termination and Ssu72 function but is dispensable for pre-mRNA 3'-end processing
    • Ghazy MA, He X, Singh BN, Hampsey M, Moore C. 2009. The essential N terminus of the Pta1 scaffold protein is required for snoRNA transcription termination and Ssu72 function but is dispensable for pre-mRNA 3'-end processing. Mol. Cell. Biol. 29:2296-2307. http://dx.doi.org/10.1128/MCB.01514-08.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 2296-2307
    • Ghazy, M.A.1    He, X.2    Singh, B.N.3    Hampsey, M.4    Moore, C.5
  • 48
    • 84859900820 scopus 로고    scopus 로고
    • Novel interactions at the essential N-terminus of poly(A) polymerase that could regulate poly(A) addition in Saccharomyces cerevisiae
    • Ezeokonkwo C, Ghazy MA, Zhelkovsky A, Yeh PC, Moore C. 2012. Novel interactions at the essential N-terminus of poly(A) polymerase that could regulate poly(A) addition in Saccharomyces cerevisiae. FEBS Lett. 586:1173-1178. http://dx.doi.org/10.1016/j.febslet.2012.03.036.
    • (2012) FEBS Lett , vol.586 , pp. 1173-1178
    • Ezeokonkwo, C.1    Ghazy, M.A.2    Zhelkovsky, A.3    Yeh, P.C.4    Moore, C.5
  • 49
    • 2242469712 scopus 로고    scopus 로고
    • Structure of the HIV-1 nucleocapsid protein bound to the SL3 psi-RNA recognition element
    • De Guzman RN, Wu ZR, Stalling CC, Pappalardo L, Borer PN, Summers MF. 1998. Structure of the HIV-1 nucleocapsid protein bound to the SL3 psi-RNA recognition element. Science 279:384-388. http://dx.doi.org/10.1126/science.279.5349.384.
    • (1998) Science , vol.279 , pp. 384-388
    • De Guzman, R.N.1    Wu, Z.R.2    Stalling, C.C.3    Pappalardo, L.4    Borer, P.N.5    Summers, M.F.6
  • 50
    • 0034679803 scopus 로고    scopus 로고
    • Distinct roles of two Yth1p domains in 3'-end cleavage and polyadenylation of yeast pre-mRNAs
    • Barabino SM, Ohnacker M, Keller W. 2000. Distinct roles of two Yth1p domains in 3'-end cleavage and polyadenylation of yeast pre-mRNAs. EMBO J. 19:3778-3787. http://dx.doi.org/10.1093/emboj/19.14.3778.
    • (2000) EMBO J , vol.19 , pp. 3778-3787
    • Barabino, S.M.1    Ohnacker, M.2    Keller, W.3
  • 51
    • 0036682601 scopus 로고    scopus 로고
    • Yhh1p/Cft1p directly links poly(A) site recognition and RNA polymerase II transcription termination
    • Dichtl B, Blank D, Sadowski M, Hubner W, Weiser S, Keller W. 2002. Yhh1p/Cft1p directly links poly(A) site recognition and RNA polymerase II transcription termination. EMBO J. 21:4125-4135. http://dx.doi.org /10.1093/emboj/cdf390.
    • (2002) EMBO J , vol.21 , pp. 4125-4135
    • Dichtl, B.1    Blank, D.2    Sadowski, M.3    Hubner, W.4    Weiser, S.5    Keller, W.6
  • 52
    • 0037089139 scopus 로고    scopus 로고
    • Probabilistic prediction of Saccharomyces cerevisiae mRNA 3'-processing sites
    • Graber JH, McAllister GD, Smith TF. 2002. Probabilistic prediction of Saccharomyces cerevisiae mRNA 3'-processing sites. Nucleic Acids Res. 30:1851-1858. http://dx.doi.org/10.1093/nar/30.8.1851.
    • (2002) Nucleic Acids Res , vol.30 , pp. 1851-1858
    • Graber, J.H.1    McAllister, G.D.2    Smith, T.F.3
  • 53
    • 34748870917 scopus 로고    scopus 로고
    • Polyadenylation site choice in yeast is affected by competition between Npl3 and polyadenylation factor CFI
    • Bucheli ME, He X, Kaplan CD, Moore CL, Buratowski S. 2007. Polyadenylation site choice in yeast is affected by competition between Npl3 and polyadenylation factor CFI. RNA 13:1756-1764. http://dx.doi.org/10.1261/rna.607207.
    • (2007) RNA , vol.13 , pp. 1756-1764
    • Bucheli, M.E.1    He, X.2    Kaplan, C.D.3    Moore, C.L.4    Buratowski, S.5
  • 54
    • 0345373987 scopus 로고    scopus 로고
    • Functional interactions between the transcription and mRNA 3' end processing machineries mediated by Ssu72 and Sub1
    • He X, Khan AU, Cheng H, Pappas DL, Jr, Hampsey M, Moore CL. 2003. Functional interactions between the transcription and mRNA 3' end processing machineries mediated by Ssu72 and Sub1. Genes Dev. 17:1030-1042. http://dx.doi.org/10.1101/gad.1075203.
    • (2003) Genes Dev , vol.17 , pp. 1030-1042
    • He, X.1    Khan, A.U.2    Cheng, H.3    Pappas, D.L.4    Hampsey, M.5    Moore, C.L.6
  • 55
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley D. 2009. Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu. Rev. Biochem. 78:477-513. http://dx.doi.org/10.1146/annurev.biochem.78.081507.101607.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 477-513
    • Finley, D.1
  • 56
    • 1842790562 scopus 로고    scopus 로고
    • Role of C-terminal extensions of subunits 2 and 7 in assembly and activity of eukaryotic proteasomes
    • Ramos PC, Marques AJ, London MK, Dohmen RJ. 2004. Role of C-terminal extensions of subunits 2 and 7 in assembly and activity of eukaryotic proteasomes. J. Biol. Chem. 279:14323-14330. http://dx.doi.org/10.1074/jbc.M308757200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14323-14330
    • Ramos, P.C.1    Marques, A.J.2    London, M.K.3    Dohmen, R.J.4
  • 57
    • 70349441058 scopus 로고    scopus 로고
    • Ubiquitin-binding domains- from structures to functions
    • Dikic I, Wakatsuki S, Walters KJ. 2009. Ubiquitin-binding domains- from structures to functions. Nat. Rev. Mol. Cell Biol. 10:659-671. http: //dx.doi.org/10.1038/nrm2767.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 659-671
    • Dikic, I.1    Wakatsuki, S.2    Walters, K.J.3
  • 59
    • 0002858113 scopus 로고    scopus 로고
    • Proteasome inhibitors cause induction of heat shock proteins and trehalose, which together confer thermotolerance in Saccharomyces cerevisiae
    • Lee DH, Goldberg AL. 1998. Proteasome inhibitors cause induction of heat shock proteins and trehalose, which together confer thermotolerance in Saccharomyces cerevisiae. Mol. Cell. Biol. 18:30-38.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 30-38
    • Lee, D.H.1    Goldberg, A.L.2
  • 60
    • 4744339306 scopus 로고    scopus 로고
    • Ubiquitylation of nascent globin chains in a cell-free system
    • Adachi K, Lakka V, Zhao Y, Surrey S. 2004. Ubiquitylation of nascent globin chains in a cell-free system. J. Biol. Chem. 279:41767-41774. http: //dx.doi.org/10.1074/jbc.M405059200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 41767-41774
    • Adachi, K.1    Lakka, V.2    Zhao, Y.3    Surrey, S.4
  • 61
    • 77949538037 scopus 로고    scopus 로고
    • Discovery of novel proteasome inhibitors using a high-content cell-based screening system
    • Lavelin I, Beer A, Kam Z, Rotter V, Oren M, Navon A, Geiger B. 2009. Discovery of novel proteasome inhibitors using a high-content cell-based screening system. PLoS One 4:e8503. http://dx.doi.org/10.1371/journal.pone.0008503.
    • (2009) PLoS One , vol.4 , pp. e8503
    • Lavelin, I.1    Beer, A.2    Kam, Z.3    Rotter, V.4    Oren, M.5    Navon, A.6    Geiger, B.7
  • 62
    • 0034074948 scopus 로고    scopus 로고
    • Posttranslational phosphorylation and ubiquitination of the Saccharomyces cerevisiae poly(A) polymerase at the S/G2 stage of the cell cycle
    • Mizrahi N, Moore C. 2000. Posttranslational phosphorylation and ubiquitination of the Saccharomyces cerevisiae poly(A) polymerase at the S/G2 stage of the cell cycle. Mol. Cell. Biol. 20:2794-2802. http://dx.doi.org/10.1128/MCB.20.8.2794-2802.2000.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2794-2802
    • Mizrahi, N.1    Moore, C.2
  • 63
    • 84860516339 scopus 로고    scopus 로고
    • Novel E3 ubiquitin ligases that regulate histone protein levels in the budding yeast Saccharomyces cerevisiae
    • Singh RK, Gonzalez M, Kabbaj MH, Gunjan A. 2012. Novel E3 ubiquitin ligases that regulate histone protein levels in the budding yeast Saccharomyces cerevisiae. PLoS One 7:e36295. http://dx.doi.org/10.1371/journal.pone.0036295.
    • (2012) PLoS One , vol.7 , pp. e36295
    • Singh, R.K.1    Gonzalez, M.2    Kabbaj, M.H.3    Gunjan, A.4
  • 64
    • 0035836765 scopus 로고    scopus 로고
    • A comprehensive two-hybrid analysis to explore the yeast protein interactome
    • Ito T, Chiba T, Ozawa R, Yoshida M, Hattori M, Sakaki Y. 2001. A comprehensive two-hybrid analysis to explore the yeast protein interactome. Proc. Natl. Acad. Sci. U. S. A. 98:4569-4574. http://dx.doi.org/10.1073/pnas.061034498.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 4569-4574
    • Ito, T.1    Chiba, T.2    Ozawa, R.3    Yoshida, M.4    Hattori, M.5    Sakaki, Y.6
  • 66
    • 33846137688 scopus 로고    scopus 로고
    • Hse1, a component of the yeast Hrs-STAM ubiquitin-sorting complex, associates with ubiquitin peptidases and a ligase to control sorting efficiency into multivesicular bodies
    • Ren J, Kee Y, Huibregtse JM, Piper RC. 2007. Hse1, a component of the yeast Hrs-STAM ubiquitin-sorting complex, associates with ubiquitin peptidases and a ligase to control sorting efficiency into multivesicular bodies. Mol. Biol. Cell 18:324-335. http://dx.doi.org/10.1091/mbc.E06 -06-0557.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 324-335
    • Ren, J.1    Kee, Y.2    Huibregtse, J.M.3    Piper, R.C.4
  • 68
    • 0030835542 scopus 로고    scopus 로고
    • The Uba2 and Ufd1 proteins of Saccharomyces cerevisiae interact with poly(A) polymerase and affect the polyadenylation activity of cell extracts
    • del Olmo M, Mizrahi N, Gross S, Moore CL. 1997. The Uba2 and Ufd1 proteins of Saccharomyces cerevisiae interact with poly(A) polymerase and affect the polyadenylation activity of cell extracts. Mol. Gen. Genet. 255: 209-218. http://dx.doi.org/10.1007/s004380050491.
    • (1997) Mol. Gen. Genet. , vol.255 , pp. 209-218
    • del Olmo, M.1    Mizrahi, N.2    Gross, S.3    Moore, C.L.4
  • 69
    • 37549012161 scopus 로고    scopus 로고
    • Sumoylation modulates the assembly and activity of the pre-mRNA 3' processing complex
    • Vethantham V, Rao N, Manley JL. 2007. Sumoylation modulates the assembly and activity of the pre-mRNA 3' processing complex. Mol. Cell. Biol. 27:8848-8858. http://dx.doi.org/10.1128/MCB.01186-07.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 8848-8858
    • Vethantham, V.1    Rao, N.2    Manley, J.L.3
  • 70
    • 39449103526 scopus 로고    scopus 로고
    • Sumoylation regulates multiple aspects of mammalian poly(A) polymerase function
    • Vethantham V, Rao N, Manley JL. 2008. Sumoylation regulates multiple aspects of mammalian poly(A) polymerase function. Genes Dev. 22:499- 511. http://dx.doi.org/10.1101/gad.1628208.
    • (2008) Genes Dev , vol.22 , pp. 499-511
    • Vethantham, V.1    Rao, N.2    Manley, J.L.3
  • 73
    • 0036889142 scopus 로고    scopus 로고
    • Interactions between mRNA export commitment, 3'-end quality control, and nuclear degradation
    • Libri D, Dower K, Boulay J, Thomsen R, Rosbash M, Jensen TH. 2002. Interactions between mRNA export commitment, 3'-end quality control, and nuclear degradation. Mol. Cell. Biol. 22:8254-8266. http://dx.doi.org /10.1128/MCB.22.23.8254-8266.2002.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8254-8266
    • Libri, D.1    Dower, K.2    Boulay, J.3    Thomsen, R.4    Rosbash, M.5    Jensen, T.H.6
  • 74
    • 80455177038 scopus 로고    scopus 로고
    • The export factor Yra1 modulates mRNA 3' end processing
    • Johnson SA, Kim H, Erickson B, Bentley DL. 2011. The export factor Yra1 modulates mRNA 3' end processing. Nat. Struct. Mol. Biol. 18: 1164-1171. http://dx.doi.org/10.1038/nsmb.2126.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 1164-1171
    • Johnson, S.A.1    Kim, H.2    Erickson, B.3    Bentley, D.L.4
  • 77
    • 42449084129 scopus 로고    scopus 로고
    • Protein factors in pre-mRNA 3'-end processing
    • Mandel CR, Bai Y, Tong L. 2008. Protein factors in pre-mRNA 3'-end processing. Cell. Mol. Life Sci. 65:1099-1122. http://dx.doi.org/10.1007 /s00018-007-7474-3.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 1099-1122
    • Mandel, C.R.1    Bai, Y.2    Tong, L.3
  • 78
    • 84866059126 scopus 로고    scopus 로고
    • The RNA-binding E3 ubiquitin ligase MEX-3C links ubiquitination with MHC-I mRNA degradation
    • Cano F, Bye H, Duncan LM, Buchet-Poyau K, Billaud M, Wills MR, Lehner PJ. 2012. The RNA-binding E3 ubiquitin ligase MEX-3C links ubiquitination with MHC-I mRNA degradation. EMBO J. 31:3596-3606. http://dx.doi.org/10.1038/emboj.2012.218.
    • (2012) EMBO J , vol.31 , pp. 3596-3606
    • Cano, F.1    Bye, H.2    Duncan, L.M.3    Buchet-Poyau, K.4    Billaud, M.5    Wills, M.R.6    Lehner, P.J.7
  • 79
    • 78649752092 scopus 로고    scopus 로고
    • RNA-binding E3 ubiquitin ligases: novel players in nucleic acid regulation
    • Cano F, Miranda-Saavedra D, Lehner PJ. 2010. RNA-binding E3 ubiquitin ligases: novel players in nucleic acid regulation. Biochem. Soc. Trans. 38:1621-1626. http://dx.doi.org/10.1042/BST0381621.
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 1621-1626
    • Cano, F.1    Miranda-Saavedra, D.2    Lehner, P.J.3
  • 80
    • 84875520533 scopus 로고    scopus 로고
    • Mdm2 and MdmX as regulators of gene expression
    • Biderman L, Manley JL, Prives C. 2012. Mdm2 and MdmX as regulators of gene expression. Genes Cancer 3:264-273. http://dx.doi.org/10.1177 /1947601912455331.
    • (2012) Genes Cancer , vol.3 , pp. 264-273
    • Biderman, L.1    Manley, J.L.2    Prives, C.3
  • 82
    • 44949142293 scopus 로고    scopus 로고
    • Systematic approach for validating the ubiquitinated proteome
    • Seyfried NT, Xu P, Duong DM, Cheng D, Hanfelt J, Peng J. 2008. Systematic approach for validating the ubiquitinated proteome. Anal. Chem. 80:4161-4169. http://dx.doi.org/10.1021/ac702516a.
    • (2008) Anal. Chem. , vol.80 , pp. 4161-4169
    • Seyfried, N.T.1    Xu, P.2    Duong, D.M.3    Cheng, D.4    Hanfelt, J.5    Peng, J.6
  • 83
    • 84879613791 scopus 로고    scopus 로고
    • Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation
    • Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villen J. 2013. Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nat. Methods 10:676-682. http://dx.doi.org/10.1038/nmeth.2519.
    • (2013) Nat. Methods , vol.10 , pp. 676-682
    • Swaney, D.L.1    Beltrao, P.2    Starita, L.3    Guo, A.4    Rush, J.5    Fields, S.6    Krogan, N.J.7    Villen, J.8


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