메뉴 건너뛰기




Volumn 33, Issue 23, 2014, Pages 2829-2846

The exosome-binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase

Author keywords

nuclear exosome; RNA degradation; X ray crystallography; yeast genetics

Indexed keywords

EXORIBONUCLEASE; GREEN FLUORESCENT PROTEIN; HELICASE; RIBONUCLEASE; RIBONUCLEASE RRP47; RIBONUCLEASE RRP6; RNA; UNCLASSIFIED DRUG; ANAZOLENE SODIUM; DEAD BOX PROTEIN; DNA BINDING PROTEIN; EXOSOME MULTIENZYME RIBONUCLEASE COMPLEX; FUCHSINE; LRP1 PROTEIN, S CEREVISIAE; MTR4 PROTEIN, S CEREVISIAE; MULTIPROTEIN COMPLEX; NUCLEAR PROTEIN; OLIGONUCLEOTIDE PROBE; RNA BINDING PROTEIN; RRP6 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84919337863     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.15252/embj.201488757     Document Type: Article
Times cited : (90)

References (70)
  • 5
    • 0000577868 scopus 로고    scopus 로고
    • The 3 to 5 degradation of yeast mRNAs is a general mechanism for mRNA turnover that requires the SKI2 DEVH box protein and 3 to 5 exonucleases of the exosome complex
    • Anderson JS, Parker RP, (1998) The 3 to 5 degradation of yeast mRNAs is a general mechanism for mRNA turnover that requires the SKI2 DEVH box protein and 3 to 5 exonucleases of the exosome complex. EMBO J 17: 1497-1506
    • (1998) EMBO J , vol.17 , pp. 1497-1506
    • Anderson, J.S.1    Parker, R.P.2
  • 6
    • 0035801392 scopus 로고    scopus 로고
    • Ski7p G protein interacts with the exosome and the Ski complex for 3-to-5 mRNA decay in yeast
    • Araki Y, Takahashi S, Kobayashi T, Kajiho H, Hoshino S, Katada T, (2001) Ski7p G protein interacts with the exosome and the Ski complex for 3-to-5 mRNA decay in yeast. EMBO J 20: 4684-4693
    • (2001) EMBO J , vol.20 , pp. 4684-4693
    • Araki, Y.1    Takahashi, S.2    Kobayashi, T.3    Kajiho, H.4    Hoshino, S.5    Katada, T.6
  • 7
    • 84895882408 scopus 로고    scopus 로고
    • RRP6 from Trypanosoma brucei: Crystal structure of the catalytic domain, association with EAP3 and activity towards structured and non-structured RNA substrates
    • Barbosa RL, Legrand P, Wien F, Pineau B, Thompson A, Guimarães BG, (2014) RRP6 from Trypanosoma brucei: crystal structure of the catalytic domain, association with EAP3 and activity towards structured and non-structured RNA substrates. PLoS One 9: e89138
    • (2014) PLoS One , vol.9 , pp. e89138
    • Barbosa, R.L.1    Legrand, P.2    Wien, F.3    Pineau, B.4    Thompson, A.5    Guimarães, B.G.6
  • 9
    • 70350336247 scopus 로고    scopus 로고
    • The yeast exosome functions as a macromolecular cage to channel RNA substrates for degradation
    • Bonneau F, Basquin J, Ebert J, Lorentzen E, Conti E, (2009) The yeast exosome functions as a macromolecular cage to channel RNA substrates for degradation. Cell 139: 547-559
    • (2009) Cell , vol.139 , pp. 547-559
    • Bonneau, F.1    Basquin, J.2    Ebert, J.3    Lorentzen, E.4    Conti, E.5
  • 10
    • 0034664803 scopus 로고    scopus 로고
    • Identification of a regulated pathway for nuclear pre-mRNA turnover
    • Bousquet-Antonelli C, Presutti C, Tollervey D, (2000) Identification of a regulated pathway for nuclear pre-mRNA turnover. Cell 102: 765-775
    • (2000) Cell , vol.102 , pp. 765-775
    • Bousquet-Antonelli, C.1    Presutti, C.2    Tollervey, D.3
  • 11
    • 0032557455 scopus 로고    scopus 로고
    • Rrp6p, the yeast homologue of the human PM-Scl 100-kDa autoantigen, is essential for efficient 5.8 S rRNA 3 end formation
    • Briggs MW, Burkard KT, Butler JS, (1998) Rrp6p, the yeast homologue of the human PM-Scl 100-kDa autoantigen, is essential for efficient 5.8 S rRNA 3 end formation. J Biol Chem 273: 13255-13263
    • (1998) J Biol Chem , vol.273 , pp. 13255-13263
    • Briggs, M.W.1    Burkard, K.T.2    Butler, J.S.3
  • 12
    • 0033960962 scopus 로고    scopus 로고
    • A nuclear 3-5 exonuclease involved in mRNA degradation interacts with Poly(A) polymerase and the hnRNA protein Npl3p
    • Burkard KT, Butler JS, (2000) A nuclear 3-5 exonuclease involved in mRNA degradation interacts with Poly(A) polymerase and the hnRNA protein Npl3p. Mol Cell Biol 20: 604-616
    • (2000) Mol Cell Biol , vol.20 , pp. 604-616
    • Burkard, K.T.1    Butler, J.S.2
  • 13
    • 79960681216 scopus 로고    scopus 로고
    • Rrp6, rrp47 and cofactors of the nuclear exosome
    • Butler JS, Mitchell P, (2011) Rrp6, rrp47 and cofactors of the nuclear exosome. Adv Exp Med Biol 702: 91-104
    • (2011) Adv Exp Med Biol , vol.702 , pp. 91-104
    • Butler, J.S.1    Mitchell, P.2
  • 14
    • 57149094672 scopus 로고    scopus 로고
    • Evidence for core exosome independent function of the nuclear exoribonuclease Rrp6p
    • Callahan KP, Butler JS, (2008) Evidence for core exosome independent function of the nuclear exoribonuclease Rrp6p. Nucleic Acids Res 36: 6645-6655
    • (2008) Nucleic Acids Res , vol.36 , pp. 6645-6655
    • Callahan, K.P.1    Butler, J.S.2
  • 16
    • 79953017227 scopus 로고    scopus 로고
    • The C-terminal region of the exosome-associated protein Rrp47 is specifically required for box C/D small nucleolar RNA 3-maturation
    • Costello JL, Stead JA, Feigenbutz M, Jones RM, Mitchell P, (2011) The C-terminal region of the exosome-associated protein Rrp47 is specifically required for box C/D small nucleolar RNA 3-maturation. J Biol Chem 286: 4535-4543
    • (2011) J Biol Chem , vol.286 , pp. 4535-4543
    • Costello, J.L.1    Stead, J.A.2    Feigenbutz, M.3    Jones, R.M.4    Mitchell, P.5
  • 17
    • 41549133010 scopus 로고    scopus 로고
    • The Leishmania tarentolae exosome: Purification and structural analysis by electron microscopy
    • Cristodero M, Böttcher B, Diepholz M, Scheffzek K, Clayton C, (2008) The Leishmania tarentolae exosome: purification and structural analysis by electron microscopy. Mol Biochem Parasitol 159: 24-29
    • (2008) Mol Biochem Parasitol , vol.159 , pp. 24-29
    • Cristodero, M.1    Böttcher, B.2    Diepholz, M.3    Scheffzek, K.4    Clayton, C.5
  • 18
    • 0032481316 scopus 로고    scopus 로고
    • Dob1p (Mtr4p) is a putative ATP-dependent RNA helicase required for the 3 end formation of 5.8S rRNA in Saccharomyces cerevisiae
    • de la Cruz J, Kressler D, Tollervey D, Linder P, (1998) Dob1p (Mtr4p) is a putative ATP-dependent RNA helicase required for the 3 end formation of 5.8S rRNA in Saccharomyces cerevisiae. EMBO J 17: 1128-1140
    • (1998) EMBO J , vol.17 , pp. 1128-1140
    • De La Cruz, J.1    Kressler, D.2    Tollervey, D.3    Linder, P.4
  • 19
    • 33644784770 scopus 로고    scopus 로고
    • Accumulation of unstable promoter-associated transcripts upon loss of the nuclear exosome subunit Rrp6p in Saccharomyces cerevisiae
    • Davis CA, Ares M, (2006) Accumulation of unstable promoter-associated transcripts upon loss of the nuclear exosome subunit Rrp6p in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 103: 3262-3267
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 3262-3267
    • Davis, C.A.1    Ares, M.2
  • 21
    • 33846068920 scopus 로고    scopus 로고
    • A single subunit, Dis3, is essentially responsible for yeast exosome core activity
    • Dziembowski A, Lorentzen E, Conti E, Séraphin B, (2007) A single subunit, Dis3, is essentially responsible for yeast exosome core activity. Nat Struct Mol Biol 14: 15-22
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 15-22
    • Dziembowski, A.1    Lorentzen, E.2    Conti, E.3    Séraphin, B.4
  • 24
    • 84892399891 scopus 로고    scopus 로고
    • The exosome cofactor Rrp47 is critical for the stability and normal expression of its associated exoribonuclease Rrp6 in Saccharomyces cerevisiae
    • Feigenbutz M, Garland W, Turner M, Mitchell P, (2013a) The exosome cofactor Rrp47 is critical for the stability and normal expression of its associated exoribonuclease Rrp6 in Saccharomyces cerevisiae. PLoS One 8: e80752
    • (2013) PLoS One , vol.8 , pp. e80752
    • Feigenbutz, M.1    Garland, W.2    Turner, M.3    Mitchell, P.4
  • 25
    • 84878388270 scopus 로고    scopus 로고
    • Assembly of the yeast exoribonuclease Rrp6 with its associated cofactor Rrp47 occurs in the nucleus and is critical for the controlled expression of Rrp47
    • Feigenbutz M, Jones R, Besong TMD, Harding SE, Mitchell P, (2013b) Assembly of the yeast exoribonuclease Rrp6 with its associated cofactor Rrp47 occurs in the nucleus and is critical for the controlled expression of Rrp47. J Biol Chem 288: 15959-15970
    • (2013) J Biol Chem , vol.288 , pp. 15959-15970
    • Feigenbutz, M.1    Jones, R.2    Besong, T.M.D.3    Harding, S.E.4    Mitchell, P.5
  • 26
    • 84888401056 scopus 로고    scopus 로고
    • Rrp47 functions in RNA surveillance and stable RNA processing when divorced from the exoribonuclease and exosome-binding domains of Rrp6
    • Garland W, Feigenbutz M, Turner M, Mitchell P, (2013) Rrp47 functions in RNA surveillance and stable RNA processing when divorced from the exoribonuclease and exosome-binding domains of Rrp6. RNA 19: 1659-1668
    • (2013) RNA , vol.19 , pp. 1659-1668
    • Garland, W.1    Feigenbutz, M.2    Turner, M.3    Mitchell, P.4
  • 29
    • 84055217962 scopus 로고    scopus 로고
    • The crystal structure of S. Cerevisiae Ski2, a DExH helicase associated with the cytoplasmic functions of the exosome
    • Halbach F, Rode M, Conti E, (2012) The crystal structure of S. cerevisiae Ski2, a DExH helicase associated with the cytoplasmic functions of the exosome. RNA 18: 124-134
    • (2012) RNA , vol.18 , pp. 124-134
    • Halbach, F.1    Rode, M.2    Conti, E.3
  • 30
    • 84882796823 scopus 로고    scopus 로고
    • The yeast ski complex: Crystal structure and RNA channeling to the exosome complex
    • Halbach F, Reichelt P, Rode M, Conti E, (2013) The yeast ski complex: crystal structure and RNA channeling to the exosome complex. Cell 154: 814-826
    • (2013) Cell , vol.154 , pp. 814-826
    • Halbach, F.1    Reichelt, P.2    Rode, M.3    Conti, E.4
  • 31
    • 0035807308 scopus 로고    scopus 로고
    • Quality control of mRNA 3-end processing is linked to the nuclear exosome
    • Hilleren P, McCarthy T, Rosbash M, Parker R, Jensen TH, (2001) Quality control of mRNA 3-end processing is linked to the nuclear exosome. Nature 413: 538-542
    • (2001) Nature , vol.413 , pp. 538-542
    • Hilleren, P.1    McCarthy, T.2    Rosbash, M.3    Parker, R.4    Jensen, T.H.5
  • 32
    • 0037155584 scopus 로고    scopus 로고
    • Exosome-mediated recognition and degradation of mRNAs lacking a termination codon
    • van Hoof A, Frischmeyer PA, Dietz HC, Parker R, (2002) Exosome-mediated recognition and degradation of mRNAs lacking a termination codon. Science 295: 2262-2264
    • (2002) Science , vol.295 , pp. 2262-2264
    • Van Hoof, A.1    Frischmeyer, P.A.2    Dietz, H.C.3    Parker, R.4
  • 34
    • 77954952539 scopus 로고    scopus 로고
    • The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing
    • Jackson RN, Klauer AA, Hintze BJ, Robinson H, van Hoof A, Johnson SJ, (2010) The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing. EMBO J 29: 2205-2216
    • (2010) EMBO J , vol.29 , pp. 2205-2216
    • Jackson, R.N.1    Klauer, A.A.2    Hintze, B.J.3    Robinson, H.4    Van Hoof, A.5    Johnson, S.J.6
  • 35
    • 79960473450 scopus 로고    scopus 로고
    • Activities of human RRP6 and structure of the human RRP6 catalytic domain
    • Januszyk K, Liu Q, Lima CD, (2011) Activities of human RRP6 and structure of the human RRP6 catalytic domain. RNA 17: 1566-1577
    • (2011) RNA , vol.17 , pp. 1566-1577
    • Januszyk, K.1    Liu, Q.2    Lima, C.D.3
  • 36
    • 76449106188 scopus 로고    scopus 로고
    • Integration, scaling, space-group assignment and post-refinement
    • Kabsch W, (2010) Integration, scaling, space-group assignment and post-refinement. Acta Crystallogr D Biol Crystallogr 66: 133-144
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 133-144
    • Kabsch, W.1
  • 37
    • 2642574393 scopus 로고    scopus 로고
    • Nuclear surveillance and degradation of hypomodified initiator tRNAMet in S. Cerevisiae
    • Kadaba S, Krueger A, Trice T, Krecic AM, Hinnebusch AG, Anderson J, (2004) Nuclear surveillance and degradation of hypomodified initiator tRNAMet in S. cerevisiae. Genes Dev 18: 1227-1240
    • (2004) Genes Dev , vol.18 , pp. 1227-1240
    • Kadaba, S.1    Krueger, A.2    Trice, T.3    Krecic, A.M.4    Hinnebusch, A.G.5    Anderson, J.6
  • 38
    • 84871736707 scopus 로고    scopus 로고
    • Genetic interactions suggest multiple distinct roles of the arch and core helicase domains of Mtr4 in Rrp6 and exosome function
    • Klauer AA, van Hoof A, (2013) Genetic interactions suggest multiple distinct roles of the arch and core helicase domains of Mtr4 in Rrp6 and exosome function. Nucleic Acids Res 41: 533-541
    • (2013) Nucleic Acids Res , vol.41 , pp. 533-541
    • Klauer, A.A.1    Van Hoof, A.2
  • 40
    • 33845407784 scopus 로고    scopus 로고
    • Reconstitution, activities, and structure of the eukaryotic RNA exosome
    • Liu Q, Greimann JC, Lima CD, (2006) Reconstitution, activities, and structure of the eukaryotic RNA exosome. Cell 127: 1223-1237
    • (2006) Cell , vol.127 , pp. 1223-1237
    • Liu, Q.1    Greimann, J.C.2    Lima, C.D.3
  • 42
    • 40849106786 scopus 로고    scopus 로고
    • Structure of the active subunit of the yeast exosome core, Rrp44: Diverse modes of substrate recruitment in the RNase II nuclease family
    • Lorentzen E, Basquin J, Tomecki R, Dziembowski A, Conti E, (2008) Structure of the active subunit of the yeast exosome core, Rrp44: diverse modes of substrate recruitment in the RNase II nuclease family. Mol Cell 29: 717-728
    • (2008) Mol Cell , vol.29 , pp. 717-728
    • Lorentzen, E.1    Basquin, J.2    Tomecki, R.3    Dziembowski, A.4    Conti, E.5
  • 44
    • 84874742223 scopus 로고    scopus 로고
    • Crystal structure of an RNA-bound 11-subunit eukaryotic exosome complex
    • Makino DL, Baumgärtner M, Conti E, (2013a) Crystal structure of an RNA-bound 11-subunit eukaryotic exosome complex. Nature 495: 70-75
    • (2013) Nature , vol.495 , pp. 70-75
    • Makino, D.L.1    Baumgärtner, M.2    Conti, E.3
  • 45
    • 84886405949 scopus 로고    scopus 로고
    • The RNA exosome and proteasome: Common principles of degradation control
    • Makino DL, Halbach F, Conti E, (2013b) The RNA exosome and proteasome: common principles of degradation control. Nat Rev Mol Cell Biol 14: 654-660
    • (2013) Nat Rev Mol Cell Biol , vol.14 , pp. 654-660
    • Makino, D.L.1    Halbach, F.2    Conti, E.3
  • 48
    • 33747041640 scopus 로고    scopus 로고
    • Structure of the nuclear exosome component Rrp6p reveals an interplay between the active site and the HRDC domain
    • Midtgaard SF, Assenholt J, Jonstrup AT, Van LB, Jensen TH, Brodersen DE, (2006) Structure of the nuclear exosome component Rrp6p reveals an interplay between the active site and the HRDC domain. Proc Natl Acad Sci USA 103: 11898-11903
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 11898-11903
    • Midtgaard, S.F.1    Assenholt, J.2    Jonstrup, A.T.3    Van, L.B.4    Jensen, T.H.5    Brodersen, D.E.6
  • 49
    • 50249112157 scopus 로고    scopus 로고
    • A yeast exosome cofactor, Mpp6, functions in RNA surveillance and in the degradation of noncoding RNA transcripts
    • Milligan L, Decourty L, Saveanu C, Rappsilber J, Ceulemans H, Jacquier A, Tollervey D, (2008) A yeast exosome cofactor, Mpp6, functions in RNA surveillance and in the degradation of noncoding RNA transcripts. Mol Cell Biol 28: 5446-5457
    • (2008) Mol Cell Biol , vol.28 , pp. 5446-5457
    • Milligan, L.1    Decourty, L.2    Saveanu, C.3    Rappsilber, J.4    Ceulemans, H.5    Jacquier, A.6    Tollervey, D.7
  • 51
    • 0037762554 scopus 로고    scopus 로고
    • An NMD pathway in yeast involving accelerated deadenylation and exosome-mediated 3->5 degradation
    • Mitchell P, Tollervey D, (2003) An NMD pathway in yeast involving accelerated deadenylation and exosome-mediated 3->5 degradation. Mol Cell 11: 1405-1413
    • (2003) Mol Cell , vol.11 , pp. 1405-1413
    • Mitchell, P.1    Tollervey, D.2
  • 52
    • 60549114880 scopus 로고    scopus 로고
    • Widespread bidirectional promoters are the major source of cryptic transcripts in yeast
    • Neil H, Malabat C, d'Aubenton-Carafa Y, Xu Z, Steinmetz LM, Jacquier A, (2009) Widespread bidirectional promoters are the major source of cryptic transcripts in yeast. Nature 457: 1038-1042
    • (2009) Nature , vol.457 , pp. 1038-1042
    • Neil, H.1    Malabat, C.2    D'Aubenton-Carafa, Y.3    Xu, Z.4    Steinmetz, L.M.5    Jacquier, A.6
  • 53
    • 4644366388 scopus 로고    scopus 로고
    • HKL2MAP: A graphical user interface for macromolecular phasing with SHELX programs
    • Pape T, Schneider TR, (2004) HKL2MAP: a graphical user interface for macromolecular phasing with SHELX programs. J Appl Crystallogr 37: 843-844
    • (2004) J Appl Crystallogr , vol.37 , pp. 843-844
    • Pape, T.1    Schneider, T.R.2
  • 55
    • 0027310271 scopus 로고
    • Improvements in the numerical analysis of thermodynamic data from biomolecular complexes
    • Royer CA, (1993) Improvements in the numerical analysis of thermodynamic data from biomolecular complexes. Anal Biochem 210: 91-97
    • (1993) Anal Biochem , vol.210 , pp. 91-97
    • Royer, C.A.1
  • 57
    • 34250339672 scopus 로고    scopus 로고
    • C1D and hMtr4p associate with the human exosome subunit PM/Scl-100 and are involved in pre-rRNA processing
    • Schilders G, van Dijk E, Pruijn GJM, (2007) C1D and hMtr4p associate with the human exosome subunit PM/Scl-100 and are involved in pre-rRNA processing. Nucleic Acids Res 35: 2564-2572
    • (2007) Nucleic Acids Res , vol.35 , pp. 2564-2572
    • Schilders, G.1    Van Dijk, E.2    Pruijn, G.J.M.3
  • 58
    • 52949089292 scopus 로고    scopus 로고
    • The exosome: A multipurpose RNA-decay machine
    • Schmid M, Jensen TH, (2008) The exosome: a multipurpose RNA-decay machine. Trends Biochem Sci 33: 501-510
    • (2008) Trends Biochem Sci , vol.33 , pp. 501-510
    • Schmid, M.1    Jensen, T.H.2
  • 59
    • 84884592355 scopus 로고    scopus 로고
    • Threading the barrel of the RNA exosome
    • Schneider C, Tollervey D, (2013) Threading the barrel of the RNA exosome. Trends Biochem Sci 38: 485-493
    • (2013) Trends Biochem Sci , vol.38 , pp. 485-493
    • Schneider, C.1    Tollervey, D.2
  • 60
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick GM, (2008) A short history of SHELX. Acta Crystallogr A 64: 112-122
    • (2008) Acta Crystallogr A , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 61
    • 34548712987 scopus 로고    scopus 로고
    • The PMC2NT domain of the catalytic exosome subunit Rrp6p provides the interface for binding with its cofactor Rrp47p, a nucleic acid-binding protein
    • Stead JA, Costello JL, Livingstone MJ, Mitchell P, (2007) The PMC2NT domain of the catalytic exosome subunit Rrp6p provides the interface for binding with its cofactor Rrp47p, a nucleic acid-binding protein. Nucleic Acids Res 35: 5556-5567
    • (2007) Nucleic Acids Res , vol.35 , pp. 5556-5567
    • Stead, J.A.1    Costello, J.L.2    Livingstone, M.J.3    Mitchell, P.4
  • 62
    • 84887043926 scopus 로고    scopus 로고
    • Cotranscriptional recruitment of RNA exosome cofactors Rrp47p and Mpp6p and two distinct Trf-Air-Mtr4 polyadenylation (TRAMP) complexes assists the exonuclease Rrp6p in the targeting and degradation of an aberrant messenger ribonucleoprotein particle (mRNP) in yeast
    • Stuparevic I, Mosrin-Huaman C, Hervouet-Coste N, Remenaric M, Rahmouni AR, (2013) Cotranscriptional recruitment of RNA exosome cofactors Rrp47p and Mpp6p and two distinct Trf-Air-Mtr4 polyadenylation (TRAMP) complexes assists the exonuclease Rrp6p in the targeting and degradation of an aberrant messenger ribonucleoprotein particle (mRNP) in yeast. J Biol Chem 288: 31816-31829
    • (2013) J Biol Chem , vol.288 , pp. 31816-31829
    • Stuparevic, I.1    Mosrin-Huaman, C.2    Hervouet-Coste, N.3    Remenaric, M.4    Rahmouni, A.R.5
  • 63
    • 58149344947 scopus 로고    scopus 로고
    • Comparative multiplexed mass spectrometric analyses of endogenously expressed yeast nuclear and cytoplasmic exosomes
    • Synowsky SA, van Wijk M, Raijmakers R, Heck AJR, (2009) Comparative multiplexed mass spectrometric analyses of endogenously expressed yeast nuclear and cytoplasmic exosomes. J Mol Biol 385: 1300-1313
    • (2009) J Mol Biol , vol.385 , pp. 1300-1313
    • Synowsky, S.A.1    Van Wijk, M.2    Raijmakers, R.3    Heck, A.J.R.4
  • 66
    • 33749578566 scopus 로고    scopus 로고
    • Substrate recognition and catalysis by the exoribonuclease RNase R
    • Vincent HA, Deutscher MP, (2006) Substrate recognition and catalysis by the exoribonuclease RNase R. J Biol Chem 281: 29769-29775
    • (2006) J Biol Chem , vol.281 , pp. 29769-29775
    • Vincent, H.A.1    Deutscher, M.P.2
  • 67
    • 84867395423 scopus 로고    scopus 로고
    • Exo- and endoribonucleolytic activities of yeast cytoplasmic and nuclear RNA exosomes are dependent on the noncatalytic core and central channel
    • Wasmuth EV, Lima CD, (2012) Exo- and endoribonucleolytic activities of yeast cytoplasmic and nuclear RNA exosomes are dependent on the noncatalytic core and central channel. Mol Cell 48: 133-144
    • (2012) Mol Cell , vol.48 , pp. 133-144
    • Wasmuth, E.V.1    Lima, C.D.2
  • 68
    • 84904821452 scopus 로고    scopus 로고
    • Structure of an Rrp6-RNA exosome complex bound to poly(A) RNA
    • Wasmuth EV, Januszyk K, Lima CD, (2014) Structure of an Rrp6-RNA exosome complex bound to poly(A) RNA. Nature 511: 435-439
    • (2014) Nature , vol.511 , pp. 435-439
    • Wasmuth, E.V.1    Januszyk, K.2    Lima, C.D.3
  • 69
    • 77955453339 scopus 로고    scopus 로고
    • Structural analysis reveals the characteristic features of Mtr4, a DExH helicase involved in nuclear RNA processing and surveillance
    • Weir JR, Bonneau F, Hentschel J, Conti E, (2010) Structural analysis reveals the characteristic features of Mtr4, a DExH helicase involved in nuclear RNA processing and surveillance. Proc Natl Acad Sci USA 107: 12139-12144
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 12139-12144
    • Weir, J.R.1    Bonneau, F.2    Hentschel, J.3    Conti, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.