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Volumn 8, Issue 1, 2017, Pages

Reconstitution of the complete pathway of ITS2 processing at the pre-ribosome

Author keywords

[No Author keywords available]

Indexed keywords

INTERNAL TRANSCRIBED SPACER 2; RIBONUCLEASE; RIBOSOME RNA; DIS3 PROTEIN, S CEREVISIAE; EXOSOME MULTIENZYME RIBONUCLEASE COMPLEX; LAS1 PROTEIN, S CEREVISIAE; NUCLEAR PROTEIN; RIBOSOME PROTEIN; RNA 5.8S; RNA PRECURSOR; RNA, RIBOSOMAL, 25S; RRP6 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 85035353973     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/s41467-017-01786-9     Document Type: Article
Times cited : (62)

References (53)
  • 1
    • 84925286904 scopus 로고    scopus 로고
    • Noncoding RNAs in eukaryotic ribosome biogenesis and function
    • Lafontaine, D. L. Noncoding RNAs in eukaryotic ribosome biogenesis and function. Nat. Struct. Mol. Biol. 22, 11-19 (2015).
    • (2015) Nat. Struct. Mol. Biol. , vol.22 , pp. 11-19
    • Lafontaine, D.L.1
  • 2
    • 85020177727 scopus 로고    scopus 로고
    • Comparison of pre-ribosomal RNA processing pathways in yeast, plant and human cells: Focus on coordinated action of endo-and exoribonucleases
    • Tomecki, R., Sikorski, P. J. & Zakrzewska-Placzek, M. Comparison of pre-ribosomal RNA processing pathways in yeast, plant and human cells: focus on coordinated action of endo-and exoribonucleases. FEBS Lett. 591, 1801-1850 (2017).
    • (2017) FEBS Lett. , vol.591 , pp. 1801-1850
    • Tomecki, R.1    Sikorski, P.J.2    Zakrzewska-Placzek, M.3
  • 3
    • 84992623378 scopus 로고    scopus 로고
    • Mechanistic insight into eukaryotic 60S ribosomal subunit biogenesis by cryo-electron microscopy
    • Greber, B. J. Mechanistic insight into eukaryotic 60S ribosomal subunit biogenesis by cryo-electron microscopy. RNA 22, 1643-1662 (2016).
    • (2016) RNA , vol.22 , pp. 1643-1662
    • Greber, B.J.1
  • 4
    • 84855230073 scopus 로고    scopus 로고
    • The power of AAA-ATPases on the road of pre-60S ribosome maturation-Molecular machines that strip pre-ribosomal particles
    • Kressler, D., Hurt, E., Bergler, H. & Bassler, J. The power of AAA-ATPases on the road of pre-60S ribosome maturation-molecular machines that strip pre-ribosomal particles. Biochim. Biophys. Acta. 1823, 92-100 (2012).
    • (2012) Biochim. Biophys. Acta. , vol.1823 , pp. 92-100
    • Kressler, D.1    Hurt, E.2    Bergler, H.3    Bassler, J.4
  • 5
    • 84887113964 scopus 로고    scopus 로고
    • Ribosome biogenesis in the yeast Saccharomyces cerevisiae
    • Woolford, J. L. Jr & Baserga, S. J. Ribosome biogenesis in the yeast Saccharomyces cerevisiae. Genetics 195, 643-681 (2013).
    • (2013) Genetics , vol.195 , pp. 643-681
    • Woolford, J.L.1    Baserga, S.J.2
  • 6
    • 0031731302 scopus 로고    scopus 로고
    • The structure of the ITS2-proximal stem is required for pre-rRNA processing in yeast
    • Peculis, B. A. & Greer, C. L. The structure of the ITS2-proximal stem is required for pre-rRNA processing in yeast. RNA 4, 1610-1622 (1998).
    • (1998) RNA , vol.4 , pp. 1610-1622
    • Peculis, B.A.1    Greer, C.L.2
  • 7
    • 84857198777 scopus 로고    scopus 로고
    • LAS1L interacts with the mammalian Rix1 complex to regulate ribosome biogenesis
    • Castle, C. D., Cassimere, E. K. & Denicourt, C. LAS1L interacts with the mammalian Rix1 complex to regulate ribosome biogenesis. Mol. Biol. Cell 23, 716-728 (2012).
    • (2012) Mol. Biol. Cell , vol.23 , pp. 716-728
    • Castle, C.D.1    Cassimere, E.K.2    Denicourt, C.3
  • 8
    • 84856807167 scopus 로고    scopus 로고
    • The evolutionarily conserved protein Las1 is required for pre-rRNA processing at both ends of ITS2
    • Schillewaert, S., Wacheul, L., Lhomme, F. & Lafontaine, D. L. The evolutionarily conserved protein Las1 is required for pre-rRNA processing at both ends of ITS2. Mol. Cell Biol. 32, 430-444 (2012).
    • (2012) Mol. Cell Biol. , vol.32 , pp. 430-444
    • Schillewaert, S.1    Wacheul, L.2    Lhomme, F.3    Lafontaine, D.L.4
  • 9
    • 0037370443 scopus 로고    scopus 로고
    • Intersection of the Kap123p-mediated nuclear import and ribosome export pathways
    • Sydorskyy, Y. et al. Intersection of the Kap123p-mediated nuclear import and ribosome export pathways. Mol. Cell Biol. 23, 2042-2054 (2003).
    • (2003) Mol. Cell Biol. , vol.23 , pp. 2042-2054
    • Sydorskyy, Y.1
  • 10
    • 0030702085 scopus 로고    scopus 로고
    • The exosome: A conserved eukaryotic RNA processing complex containing multiple 3′->5′ exoribonucleases
    • Mitchell, P., Petfalski, E., Shevchenko, A., Mann, M. & Tollervey, D. The exosome: A conserved eukaryotic RNA processing complex containing multiple 3′->5′ exoribonucleases. Cell 91, 457-466 (1997).
    • (1997) Cell , vol.91 , pp. 457-466
    • Mitchell, P.1    Petfalski, E.2    Shevchenko, A.3    Mann, M.4    Tollervey, D.5
  • 11
    • 84875471381 scopus 로고    scopus 로고
    • Las1 interacts with Grc3 polynucleotide kinase and is required for ribosome synthesis in Saccharomyces cerevisiae
    • Castle, C. D. et al. Las1 interacts with Grc3 polynucleotide kinase and is required for ribosome synthesis in Saccharomyces cerevisiae. Nucleic Acids Res. 41, 1135-1150 (2013).
    • (2013) Nucleic Acids Res. , vol.41 , pp. 1135-1150
    • Castle, C.D.1
  • 12
    • 84951286397 scopus 로고    scopus 로고
    • Coordinated ribosomal ITS2 RNA processing by the las1 complex integrating endonuclease, polynucleotide kinase, and exonuclease activities
    • Gasse, L., Flemming, D. & Hurt, E. Coordinated ribosomal ITS2 RNA processing by the las1 complex integrating endonuclease, polynucleotide kinase, and exonuclease activities. Mol. Cell 60, 808-815 (2015).
    • (2015) Mol. Cell , vol.60 , pp. 808-815
    • Gasse, L.1    Flemming, D.2    Hurt, E.3
  • 13
    • 84938809545 scopus 로고    scopus 로고
    • RNA degradation paths in a 12-subunit nuclear exosome complex
    • Makino, D. L. et al. RNA degradation paths in a 12-subunit nuclear exosome complex. Nature 524, 54-58 (2015).
    • (2015) Nature , vol.524 , pp. 54-58
    • Makino, D.L.1
  • 14
    • 84874742223 scopus 로고    scopus 로고
    • Crystal structure of an RNA-bound 11-subunit eukaryotic exosome complex
    • Makino, D. L., Baumgartner, M. & Conti, E. Crystal structure of an RNA-bound 11-subunit eukaryotic exosome complex. Nature 495, 70-75 (2013).
    • (2013) Nature , vol.495 , pp. 70-75
    • Makino, D.L.1    Baumgartner, M.2    Conti, E.3
  • 15
    • 84995545531 scopus 로고    scopus 로고
    • Nuclear RNA exosome at 3.1 A reveals substrate specificities, RNA paths, and allosteric inhibition of Rrp44/Dis3
    • Zinder, J. C., Wasmuth, E. V. & Lima, C. D. Nuclear RNA exosome at 3.1 A reveals substrate specificities, RNA paths, and allosteric inhibition of Rrp44/Dis3. Mol. Cell 64, 734-745 (2016).
    • (2016) Mol. Cell , vol.64 , pp. 734-745
    • Zinder, J.C.1    Wasmuth, E.V.2    Lima, C.D.3
  • 16
    • 57049152286 scopus 로고    scopus 로고
    • Structural organization of the RNA-degrading exosome
    • Lorentzen, E., Basquin, J. & Conti, E. Structural organization of the RNA-degrading exosome. Curr. Opin. Struct. Biol. 18, 709-713 (2008).
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 709-713
    • Lorentzen, E.1    Basquin, J.2    Conti, E.3
  • 17
    • 84952683219 scopus 로고    scopus 로고
    • The regulation and functions of the nuclear RNA exosome complex
    • Kilchert, C., Wittmann, S. & Vasiljeva, L. The regulation and functions of the nuclear RNA exosome complex. Nat. Rev. Mol. Cell Biol. 17, 227-239 (2016).
    • (2016) Nat. Rev. Mol. Cell Biol. , vol.17 , pp. 227-239
    • Kilchert, C.1    Wittmann, S.2    Vasiljeva, L.3
  • 18
    • 79960681216 scopus 로고    scopus 로고
    • Rrp6, rrp47 and cofactors of the nuclear exosome
    • Butler, J. S. & Mitchell, P. Rrp6, rrp47 and cofactors of the nuclear exosome. Adv. Exp. Med. Biol. 702, 91-104 (2011).
    • (2011) Adv. Exp. Med. Biol. , vol.702 , pp. 91-104
    • Butler, J.S.1    Mitchell, P.2
  • 19
    • 84875128302 scopus 로고    scopus 로고
    • Ski2-like RNA helicase structures: Common themes and complex assemblies
    • Johnson, S. J. & Jackson, R. N. Ski2-like RNA helicase structures: common themes and complex assemblies. RNA. Biol. 10, 33-43 (2013).
    • (2013) RNA. Biol. , vol.10 , pp. 33-43
    • Johnson, S.J.1    Jackson, R.N.2
  • 20
    • 84919337863 scopus 로고    scopus 로고
    • The exosome-binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase
    • Schuch, B. et al. The exosome-binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase. EMBO J 33, 2829-2846 (2014).
    • (2014) EMBO J , vol.33 , pp. 2829-2846
    • Schuch, B.1
  • 21
    • 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. 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).
    • (1998) EMBO J , vol.17 , pp. 1128-1140
    • De La Cruz, J.1    Kressler, D.2    Tollervey, D.3    Linder, P.4
  • 22
    • 33749130843 scopus 로고    scopus 로고
    • Remodeling of ribonucleoprotein complexes with DExH/D RNA helicases
    • Jankowsky, E. & Bowers, H. Remodeling of ribonucleoprotein complexes with DExH/D RNA helicases. Nucleic Acids Res. 34, 4181-4188 (2006).
    • (2006) Nucleic Acids Res. , vol.34 , pp. 4181-4188
    • Jankowsky, E.1    Bowers, H.2
  • 23
    • 84940378977 scopus 로고    scopus 로고
    • The exosome is recruited to RNA substrates through specific adaptor proteins
    • Thoms, M. et al. The exosome is recruited to RNA substrates through specific adaptor proteins. Cell 162, 1029-1038 (2015).
    • (2015) Cell , vol.162 , pp. 1029-1038
    • Thoms, M.1
  • 24
    • 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, M. W., Burkard, K. T. & Butler, J. S. 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).
    • (1998) J. Biol. Chem. , vol.273 , pp. 13255-13263
    • Briggs, M.W.1    Burkard, K.T.2    Butler, J.S.3
  • 25
    • 84870834419 scopus 로고    scopus 로고
    • Structure of the pre-60S ribosomal subunit with nuclear export factor Arx1 bound at the exit tunnel
    • Bradatsch, B. et al. Structure of the pre-60S ribosomal subunit with nuclear export factor Arx1 bound at the exit tunnel. Nat. Struct. Mol. Biol. 19, 1234-1241 (2012).
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 1234-1241
    • Bradatsch, B.1
  • 26
    • 84918590647 scopus 로고    scopus 로고
    • 60S ribosome biogenesis requires rotation of the 5S ribonucleoprotein particle
    • Leidig, C. et al. 60S ribosome biogenesis requires rotation of the 5S ribonucleoprotein particle. Nat. Commun. 5, 3491 (2014).
    • (2014) Nat. Commun. , vol.5
    • Leidig, C.1
  • 27
    • 84991056230 scopus 로고    scopus 로고
    • Atomic modeling of the ITS2 ribosome assembly subcomplex from cryo-EM together with mass spectrometry-identified protein-protein crosslinks
    • Wu, S., Tan, D., Woolford, J. L. Jr, Dong, M. Q. & Gao, N. Atomic modeling of the ITS2 ribosome assembly subcomplex from cryo-EM together with mass spectrometry-identified protein-protein crosslinks. Protein Sci. 26, 103-112 (2017).
    • (2017) Protein Sci. , vol.26 , pp. 103-112
    • Wu, S.1    Tan, D.2    Woolford, J.L.3    Dong, M.Q.4    Gao, N.5
  • 28
    • 80053594862 scopus 로고    scopus 로고
    • A cluster of ribosome synthesis factors regulate pre-rRNA folding and 5.8S rRNA maturation by the Rat1 exonuclease
    • Granneman, S., Petfalski, E. & Tollervey, D. A cluster of ribosome synthesis factors regulate pre-rRNA folding and 5.8S rRNA maturation by the Rat1 exonuclease. EMBO. J. 30, 4006-4019 (2011).
    • (2011) EMBO. J. , vol.30 , pp. 4006-4019
    • Granneman, S.1    Petfalski, E.2    Tollervey, D.3
  • 29
    • 84888413916 scopus 로고    scopus 로고
    • Identification of the binding site of Rlp7 on assembling 60S ribosomal subunits in Saccharomyces cerevisiae
    • Dembowski, J. A., Ramesh, M., McManus, C. J. & Woolford, J. L. Jr. Identification of the binding site of Rlp7 on assembling 60S ribosomal subunits in Saccharomyces cerevisiae. RNA 19, 1639-1647 (2013).
    • (2013) RNA , vol.19 , pp. 1639-1647
    • Dembowski, J.A.1    Ramesh, M.2    McManus, C.J.3    Woolford, J.L.4
  • 30
    • 84973664344 scopus 로고    scopus 로고
    • Diverse roles of assembly factors revealed by structures of late nuclear pre-60S ribosomes
    • Wu, S. et al. Diverse roles of assembly factors revealed by structures of late nuclear pre-60S ribosomes. Nature 534, 133-137 (2016).
    • (2016) Nature , vol.534 , pp. 133-137
    • Wu, S.1
  • 31
    • 84954244690 scopus 로고    scopus 로고
    • Architecture of the Rix1-Rea1 checkpoint machinery during pre-60S-ribosome remodeling
    • Barrio-Garcia, C. et al. Architecture of the Rix1-Rea1 checkpoint machinery during pre-60S-ribosome remodeling. Nat. Struct. Mol. Biol. 23, 37-44 (2016).
    • (2016) Nat. Struct. Mol. Biol. , vol.23 , pp. 37-44
    • Barrio-Garcia, C.1
  • 32
    • 32044449843 scopus 로고    scopus 로고
    • Comprehensive mutational analysis of yeast DEXD/H box RNA helicases involved in large ribosomal subunit biogenesis
    • Bernstein, K. A., Granneman, S., Lee, A. V., Manickam, S. & Baserga, S. J. Comprehensive mutational analysis of yeast DEXD/H box RNA helicases involved in large ribosomal subunit biogenesis. Mol. Cell Biol. 26, 1195-1208 (2006).
    • (2006) Mol. Cell Biol. , vol.26 , pp. 1195-1208
    • Bernstein, K.A.1    Granneman, S.2    Lee, A.V.3    Manickam, S.4    Baserga, S.J.5
  • 33
    • 58149236691 scopus 로고    scopus 로고
    • The exosome contains domains with specific endoribonuclease, exoribonuclease and cytoplasmic mRNA decay activities
    • Schaeffer, D. et al. The exosome contains domains with specific endoribonuclease, exoribonuclease and cytoplasmic mRNA decay activities. Nat. Struct. Mol. Biol. 16, 56-62 (2009).
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 56-62
    • Schaeffer, D.1
  • 34
    • 33846068920 scopus 로고    scopus 로고
    • A single subunit, Dis3, is essentially responsible for yeast exosome core activity
    • Dziembowski, A., Lorentzen, E., Conti, E. & Seraphin, B. A single subunit, Dis3, is essentially responsible for yeast exosome core activity. Nat. Struct. Mol. Biol. 14, 15-22 (2007).
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 15-22
    • Dziembowski, A.1    Lorentzen, E.2    Conti, E.3    Seraphin, B.4
  • 35
    • 0042834089 scopus 로고    scopus 로고
    • Contribution of domain structure to the RNA 3′ end processing and degradation functions of the nuclear exosome subunit Rrp6p
    • Phillips, S. & Butler, J. S. Contribution of domain structure to the RNA 3′ end processing and degradation functions of the nuclear exosome subunit Rrp6p. RNA 9, 1098-1107 (2003).
    • (2003) RNA , vol.9 , pp. 1098-1107
    • Phillips, S.1    Butler, J.S.2
  • 36
    • 84883377142 scopus 로고    scopus 로고
    • A transcriptome-wide atlas of RNP composition reveals diverse classes of mRNAs and lncRNAs
    • Tuck, A. C. & Tollervey, D. A transcriptome-wide atlas of RNP composition reveals diverse classes of mRNAs and lncRNAs. Cell 154, 996-1009 (2013).
    • (2013) Cell , vol.154 , pp. 996-1009
    • Tuck, A.C.1    Tollervey, D.2
  • 37
    • 84992364760 scopus 로고    scopus 로고
    • Ribosome-stalk biogenesis is coupled with recruitment of nuclear export factor to the nascent 60S subunit
    • Sarkar, A., Pech, M., Thoms, M., Beckmann, R. & Hurt, E. Ribosome-stalk biogenesis is coupled with recruitment of nuclear export factor to the nascent 60S subunit. Nat. Struct. Mol. Biol. 23, 1074-1082 (2016).
    • (2016) Nat. Struct. Mol. Biol. , vol.23 , pp. 1074-1082
    • Sarkar, A.1    Pech, M.2    Thoms, M.3    Beckmann, R.4    Hurt, E.5
  • 38
    • 62049085366 scopus 로고    scopus 로고
    • The N-Terminal PIN domain of the exosome subunit Rrp44 harbors endonuclease activity and tethers Rrp44 to the yeast core exosome
    • Schneider, C., Leung, E., Brown, J. & Tollervey, D. The N-Terminal PIN domain of the exosome subunit Rrp44 harbors endonuclease activity and tethers Rrp44 to the yeast core exosome. Nucleic Acids Res. 37, 1127-1140 (2009).
    • (2009) Nucleic Acids Res. , vol.37 , pp. 1127-1140
    • Schneider, C.1    Leung, E.2    Brown, J.3    Tollervey, D.4
  • 39
    • 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, E. V. & Lima, C. D. 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).
    • (2012) Mol. Cell , vol.48 , pp. 133-144
    • Wasmuth, E.V.1    Lima, C.D.2
  • 40
    • 84876040204 scopus 로고    scopus 로고
    • The RNA exosome complex central channel controls both exonuclease and endonuclease Dis3 activities in vivo and in vitro
    • Drazkowska, K. et al. The RNA exosome complex central channel controls both exonuclease and endonuclease Dis3 activities in vivo and in vitro. Nucleic Acids Res. 41, 3845-3858 (2013).
    • (2013) Nucleic Acids Res. , vol.41 , pp. 3845-3858
    • Drazkowska, K.1
  • 41
    • 84992358935 scopus 로고    scopus 로고
    • Structure of a cytoplasmic 11-subunit RNA exosome complex
    • Kowalinski, E. et al. Structure of a cytoplasmic 11-subunit RNA exosome complex. Mol. Cell 63, 125-134 (2016).
    • (2016) Mol. Cell , vol.63 , pp. 125-134
    • Kowalinski, E.1
  • 42
    • 57749189164 scopus 로고    scopus 로고
    • Endonucleolytic RNA cleavage by a eukaryotic exosome
    • Lebreton, A., Tomecki, R., Dziembowski, A. & Seraphin, B. Endonucleolytic RNA cleavage by a eukaryotic exosome. Nature 456, 993-996 (2008).
    • (2008) Nature , vol.456 , pp. 993-996
    • Lebreton, A.1    Tomecki, R.2    Dziembowski, A.3    Seraphin, B.4
  • 43
    • 77953105480 scopus 로고    scopus 로고
    • The AAA-ATPase Rea1 drives removal of biogenesis factors during multiple stages of 60S ribosome assembly
    • Bassler, J. et al. The AAA-ATPase Rea1 drives removal of biogenesis factors during multiple stages of 60S ribosome assembly. Mol. Cell 38, 712-721 (2010).
    • (2010) Mol. Cell , vol.38 , pp. 712-721
    • Bassler, J.1
  • 44
    • 84946792425 scopus 로고    scopus 로고
    • The structure of Rpf2-Rrs1 explains its role in ribosome biogenesis
    • Kharde, S., Calvino, F. R., Gumiero, A., Wild, K. & Sinning, I. The structure of Rpf2-Rrs1 explains its role in ribosome biogenesis. Nucleic Acids Res. 43, 7083-7095 (2015).
    • (2015) Nucleic Acids Res. , vol.43 , pp. 7083-7095
    • Kharde, S.1    Calvino, F.R.2    Gumiero, A.3    Wild, K.4    Sinning, I.5
  • 45
    • 85022193634 scopus 로고    scopus 로고
    • Insights into remodeling events during eukaryotic large ribosomal subunit assembly provided by high resolution cryo-EM structures
    • Biedka, S., Wu, S., LaPeruta, A. J., Gao, N. & Woolford, J. L., Jr. Insights into remodeling events during eukaryotic large ribosomal subunit assembly provided by high resolution cryo-EM structures. RNA Biol. 7, 1-8 (2017).
    • (2017) RNA Biol , vol.7 , pp. 1-8
    • Biedka, S.1    Wu, S.2    LaPeruta, A.J.3    Gao, N.4    Woolford, J.L.5
  • 46
    • 84866914596 scopus 로고    scopus 로고
    • Hierarchical recruitment into nascent ribosomes of assembly factors required for 27SB pre-rRNA processing in Saccharomyces cerevisiae
    • Talkish, J., Zhang, J., Jakovljevic, J., Horsey, E. W. & Woolford, J. L. Jr. Hierarchical recruitment into nascent ribosomes of assembly factors required for 27SB pre-rRNA processing in Saccharomyces cerevisiae. Nucleic Acids Res. 40, 8646-8661 (2012).
    • (2012) Nucleic Acids Res. , vol.40 , pp. 8646-8661
    • Talkish, J.1    Zhang, J.2    Jakovljevic, J.3    Horsey, E.W.4    Woolford, J.L.5
  • 47
    • 84983283607 scopus 로고    scopus 로고
    • The N-Terminal extension of yeast ribosomal protein L8 is involved in two major remodeling events during late nuclear stages of 60S ribosomal subunit assembly
    • Tutuncuoglu, B., Jakovljevic, J., Wu, S., Gao, N. & Woolford, J. L. Jr. The N-Terminal extension of yeast ribosomal protein L8 is involved in two major remodeling events during late nuclear stages of 60S ribosomal subunit assembly. RNA 22, 1386-1399 (2016).
    • (2016) RNA , vol.22 , pp. 1386-1399
    • Tutuncuoglu, B.1    Jakovljevic, J.2    Wu, S.3    Gao, N.4    Woolford, J.L.5
  • 48
    • 25844461364 scopus 로고    scopus 로고
    • Rat1p and Rai1p function with the nuclear exosome in the processing and degradation of rRNA precursors
    • Fang, F., Phillips, S. & Butler, J. S. Rat1p and Rai1p function with the nuclear exosome in the processing and degradation of rRNA precursors. RNA 11, 1571-1578 (2005).
    • (2005) RNA , vol.11 , pp. 1571-1578
    • Fang, F.1    Phillips, S.2    Butler, J.S.3
  • 49
    • 85020178014 scopus 로고    scopus 로고
    • The assembly factor Erb1 functions in multiple remodeling events during 60S ribosomal subunit assembly in S. Cerevisiae
    • Konikkat, S., Biedka, S. & Woolford, J. L. Jr. The assembly factor Erb1 functions in multiple remodeling events during 60S ribosomal subunit assembly in S. cerevisiae. Nucleic Acids Res 45, 4853-4865 (2017).
    • (2017) Nucleic Acids Res , vol.45 , pp. 4853-4865
    • Konikkat, S.1    Biedka, S.2    Woolford, J.L.3
  • 50
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensible image processing suite for electron microscopy
    • Tang, G. et al. EMAN2: An extensible image processing suite for electron microscopy. J. Struct. Biol. 157, 38-46 (2007).
    • (2007) J. Struct. Biol. , vol.157 , pp. 38-46
    • Tang, G.1
  • 52
    • 80355128077 scopus 로고    scopus 로고
    • Single particle electron microscopy reconstruction of the exosome complex using the random conical tilt method
    • Liu, X. & Wang, H. W. Single particle electron microscopy reconstruction of the exosome complex using the random conical tilt method. J. Vis. Exp. 28, 2574 (2011).
    • (2011) J. Vis. Exp. , vol.28 , pp. 2574
    • Liu, X.1    Wang, H.W.2
  • 53
    • 76949097340 scopus 로고    scopus 로고
    • Quantitative proteomics reveals subset-specific viral recognition in dendritic cells
    • Luber, C. A. et al. Quantitative proteomics reveals subset-specific viral recognition in dendritic cells. Immunity 32, 279-289 (2010).
    • (2010) Immunity , vol.32 , pp. 279-289
    • Luber, C.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.