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Volumn 23, Issue 1, 2016, Pages 37-44

Architecture of the Rix1-Rea1 checkpoint machinery during pre-60S-ribosome remodeling

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DYNEIN ADENOSINE TRIPHOSPHATASE; REA1 PROTEIN; RIBONUCLEOPROTEIN; RIBOSOME PROTEIN; RIX1 PROTEIN; RNA 5.8S; UNCLASSIFIED DRUG; MDN1 PROTEIN, S CEREVISIAE; RIX1 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84954244690     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.3132     Document Type: Article
Times cited : (91)

References (90)
  • 1
    • 0038738334 scopus 로고    scopus 로고
    • Pre-ribosomes on the road from the nucleolus to the cytoplasm
    • Tschochner, H., Hurt, E. Pre-ribosomes on the road from the nucleolus to the cytoplasm. Trends Cell Biol. 13, 255-263 (2003).
    • (2003) Trends Cell Biol. , vol.13 , pp. 255-263
    • Tschochner, H.1    Hurt, E.2
  • 2
    • 84930708678 scopus 로고    scopus 로고
    • Functions of ribosomal proteins in assembly of eukaryotic ribosomes in vivo
    • de la Cruz, J., Karbstein, K., Woolford, J.L. Jr. Functions of ribosomal proteins in assembly of eukaryotic ribosomes in vivo. Annu. Rev. Biochem. 84, 93-129 (2015).
    • (2015) Annu. Rev. Biochem. , vol.84 , pp. 93-129
    • De La Cruz, J.1    Karbstein, K.2    Woolford, J.L.3
  • 3
    • 49249139050 scopus 로고    scopus 로고
    • The post-transcriptional steps of eukaryotic ribosome biogenesis
    • Henras, A.K. et al. The post-transcriptional steps of eukaryotic ribosome biogenesis. Cell. Mol. Life Sci. 65, 2334-2359 (2008).
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 2334-2359
    • Henras, A.K.1
  • 4
    • 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
  • 5
    • 84865837598 scopus 로고    scopus 로고
    • The box C/D and H/ACA snoRNPs: Key players in the modification, processing and the dynamic folding of ribosomal RNA Wiley Interdiscip
    • Watkins, N.J., Bohnsack, M.T. The box C/D and H/ACA snoRNPs: key players in the modification, processing and the dynamic folding of ribosomal RNA. Wiley Interdiscip. Rev. RNA 3, 397-414 (2012).
    • (2012) Rev. RNA , vol.3 , pp. 397-414
    • Watkins, N.J.1    Bohnsack, M.T.2
  • 6
    • 0029939247 scopus 로고    scopus 로고
    • The 3 end of yeast 5.8S rRNA is generated by an exonuclease processing mechanism
    • Mitchell, P., Petfalski, E., Tollervey, D. The 3 end of yeast 5.8S rRNA is generated by an exonuclease processing mechanism. Genes Dev. 10, 502-513 (1996).
    • (1996) Genes Dev. , vol.10 , pp. 502-513
    • Mitchell, P.1    Petfalski, E.2    Tollervey, D.3
  • 7
    • 71149112138 scopus 로고    scopus 로고
    • Rrp17p is a eukaryotic exonuclease required for 5 end processing of Pre-60S ribosomal RNA
    • Oeffinger, M. et al. Rrp17p is a eukaryotic exonuclease required for 5 end processing of Pre-60S ribosomal RNA. Mol. Cell 36, 768-781 (2009).
    • (2009) Mol. Cell , vol.36 , pp. 768-781
    • Oeffinger, M.1
  • 8
    • 0028342849 scopus 로고
    • The 5 end of yeast 5.8S rRNA is generated by exonucleases from an upstream cleavage site
    • Henry, Y. et al. The 5 end of yeast 5.8S rRNA is generated by exonucleases from an upstream cleavage site. EMBO J. 13, 2452-2463 (1994).
    • (1994) EMBO J. , vol.13 , pp. 2452-2463
    • Henry, Y.1
  • 9
    • 80053196804 scopus 로고    scopus 로고
    • Rcl1 protein, a novel nuclease for 18 S ribosomal RNA production
    • Horn, D.M., Mason, S.L., Karbstein, K. Rcl1 protein, a novel nuclease for 18 S ribosomal RNA production. J. Biol. Chem. 286, 34082-34087 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 34082-34087
    • Horn, D.M.1    Mason, S.L.2    Karbstein, K.3
  • 10
    • 0037182878 scopus 로고    scopus 로고
    • A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA biogenesis
    • Dragon, F. et al. A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA biogenesis. Nature 417, 967-970 (2002).
    • (2002) Nature , vol.417 , pp. 967-970
    • Dragon, F.1
  • 11
    • 18544371820 scopus 로고    scopus 로고
    • 90S pre-ribosomes include the 35S pre-rRNA, the U3 snoRNP, and 40S subunit processing factors but predominantly lack 60S synthesis factors
    • Grandi, P. et al. 90S pre-ribosomes include the 35S pre-rRNA, the U3 snoRNP, and 40S subunit processing factors but predominantly lack 60S synthesis factors. Mol. Cell 10, 105-115 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 105-115
    • Grandi, P.1
  • 12
    • 0037536219 scopus 로고    scopus 로고
    • The path from nucleolar 90S to cytoplasmic 40S pre-ribosomes
    • Schäfer, T., Strauss, D., Petfalski, E., Tollervey, D., Hurt, E. The path from nucleolar 90S to cytoplasmic 40S pre-ribosomes. EMBO J. 22, 1370-1380 (2003).
    • (2003) EMBO J. , vol.22 , pp. 1370-1380
    • Schäfer, T.1    Strauss, D.2    Petfalski, E.3    Tollervey, D.4    Hurt, E.5
  • 13
    • 70149120737 scopus 로고    scopus 로고
    • Nob1 binds the single-stranded cleavage site D at the 3-end of 18S rRNA with its PIN domain
    • Lamanna, A.C., Karbstein, K. Nob1 binds the single-stranded cleavage site D at the 3-end of 18S rRNA with its PIN domain. Proc. Natl. Acad. Sci. USA 106, 14259-14264 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 14259-14264
    • Lamanna, A.C.1    Karbstein, K.2
  • 14
    • 70449656291 scopus 로고    scopus 로고
    • RNA helicase Prp43 and its co-factor Pfa1 promote 20 to 18 S rRNA processing catalyzed by the endonuclease Nob1
    • Pertschy, B. et al. RNA helicase Prp43 and its co-factor Pfa1 promote 20 to 18 S rRNA processing catalyzed by the endonuclease Nob1. J. Biol. Chem. 284, 35079-35091 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 35079-35091
    • Pertschy, B.1
  • 15
    • 0027367147 scopus 로고
    • Nuclear RNase MRP is required for correct processing of pre-5.8S rRNA in Saccharomyces cerevisiae
    • Schmitt, M.E., Clayton, D.A. Nuclear RNase MRP is required for correct processing of pre-5.8S rRNA in Saccharomyces cerevisiae. Mol. Cell. Biol. 13, 7935-7941 (1993).
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7935-7941
    • Schmitt, M.E.1    Clayton, D.A.2
  • 16
    • 0028054796 scopus 로고
    • The RNA of RNase MRP is required for normal processing of ribosomal RNA
    • Chu, S., Archer, R.H., Zengel, J.M., Lindahl, L. The RNA of RNase MRP is required for normal processing of ribosomal RNA. Proc. Natl. Acad. Sci. USA 91, 659-663 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 659-663
    • Chu, S.1    Archer, R.H.2    Zengel, J.M.3    Lindahl, L.4
  • 17
    • 35348939066 scopus 로고    scopus 로고
    • Assembly factors Rpf2 and Rrs1 recruit 5S rRNA and ribosomal proteins rpL5 and rpL11 into nascent ribosomes
    • Zhang, J. et al. Assembly factors Rpf2 and Rrs1 recruit 5S rRNA and ribosomal proteins rpL5 and rpL11 into nascent ribosomes. Genes Dev. 21, 2580-2592 (2007).
    • (2007) Genes Dev. , vol.21 , pp. 2580-2592
    • Zhang, J.1
  • 18
    • 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
  • 19
    • 69649102579 scopus 로고    scopus 로고
    • Mechanochemical removal of ribosome biogenesis factors from nascent 60S ribosomal subunits
    • Ulbrich, C. et al. Mechanochemical removal of ribosome biogenesis factors from nascent 60S ribosomal subunits. Cell 138, 911-922 (2009).
    • (2009) Cell , vol.138 , pp. 911-922
    • Ulbrich, C.1
  • 20
    • 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 , pp. 3491
    • Leidig, C.1
  • 21
    • 18644372079 scopus 로고    scopus 로고
    • 60S pre-ribosome formation viewed from assembly in the nucleolus until export to the cytoplasm
    • Nissan, T.A., Bassler, J., Petfalski, E., Tollervey, D., Hurt, E. 60S pre-ribosome formation viewed from assembly in the nucleolus until export to the cytoplasm. EMBO J. 21, 5539-5547 (2002).
    • (2002) EMBO J. , vol.21 , pp. 5539-5547
    • Nissan, T.A.1    Bassler, J.2    Petfalski, E.3    Tollervey, D.4    Hurt, E.5
  • 22
    • 84880005858 scopus 로고    scopus 로고
    • Studies on the assembly characteristics of large subunit ribosomal proteins in S. Cerevisae
    • Ohmayer, U. et al. Studies on the assembly characteristics of large subunit ribosomal proteins in S. cerevisae. PLoS One 8, e68412 (2013).
    • (2013) PLoS One , vol.8 , pp. e68412
    • Ohmayer, U.1
  • 23
    • 84892365661 scopus 로고    scopus 로고
    • Coupled GTPase and remodelling ATPase activities form a checkpoint for ribosome export
    • Matsuo, Y. et al. Coupled GTPase and remodelling ATPase activities form a checkpoint for ribosome export. Nature 505, 112-116 (2014).
    • (2014) Nature , vol.505 , pp. 112-116
    • Matsuo, Y.1
  • 24
    • 84918586987 scopus 로고    scopus 로고
    • A network of assembly factors is involved in remodeling rRNA elements during preribosome maturation
    • Baßler, J. et al. A network of assembly factors is involved in remodeling rRNA elements during preribosome maturation. J. Cell Biol. 207, 481-498 (2014).
    • (2014) J. Cell Biol. , vol.207 , pp. 481-498
    • Baßler, J.1
  • 25
    • 70349924070 scopus 로고    scopus 로고
    • Yvh1 is required for a late maturation step in the 60S biogenesis pathway
    • Kemmler, S., Occhipinti, L., Veisu, M., Panse, V.G. Yvh1 is required for a late maturation step in the 60S biogenesis pathway. J. Cell Biol. 186, 863-880 (2009).
    • (2009) J. Cell Biol. , vol.186 , pp. 863-880
    • Kemmler, S.1    Occhipinti, L.2    Veisu, M.3    Panse, V.G.4
  • 26
    • 70349901353 scopus 로고    scopus 로고
    • Ribosome stalk assembly requires the dual-specificity phosphatase Yvh1 for the exchange of Mrt4 with P0
    • Lo, K.Y., Li, Z., Wang, F., Marcotte, E.M., Johnson, A.W. Ribosome stalk assembly requires the dual-specificity phosphatase Yvh1 for the exchange of Mrt4 with P0. J. Cell Biol. 186, 849-862 (2009).
    • (2009) J. Cell Biol. , vol.186 , pp. 849-862
    • Lo, K.Y.1    Li, Z.2    Wang, F.3    Marcotte, E.M.4    Johnson, A.W.5
  • 27
    • 75749112585 scopus 로고    scopus 로고
    • Role and dynamics of the ribosomal protein P0 and its related trans-acting factor Mrt4 during ribosome assembly in Saccharomyces cerevisiae
    • Rodríguez-Mateos, M. et al. Role and dynamics of the ribosomal protein P0 and its related trans-acting factor Mrt4 during ribosome assembly in Saccharomyces cerevisiae. Nucleic Acids Res. 37, 7519-7532 (2009).
    • (2009) Nucleic Acids Res. , vol.37 , pp. 7519-7532
    • Rodríguez-Mateos, M.1
  • 28
    • 84871965556 scopus 로고    scopus 로고
    • Rlp24 activates the AAA-ATPase Drg1 to initiate cytoplasmic pre-60S maturation
    • Kappel, L. et al. Rlp24 activates the AAA-ATPase Drg1 to initiate cytoplasmic pre-60S maturation. J. Cell Biol. 199, 771-782 (2012).
    • (2012) J. Cell Biol. , vol.199 , pp. 771-782
    • Kappel, L.1
  • 29
    • 34748819901 scopus 로고    scopus 로고
    • Cytoplasmic recycling of 60S preribosomal factors depends on the AAA protein Drg1
    • Pertschy, B. et al. Cytoplasmic recycling of 60S preribosomal factors depends on the AAA protein Drg1. Mol. Cell. Biol. 27, 6581-6592 (2007).
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 6581-6592
    • Pertschy, B.1
  • 30
    • 34548341809 scopus 로고    scopus 로고
    • The Hsp40 chaperone Jjj1 is required for the nucleo-cytoplasmic recycling of preribosomal factors in Saccharomyces cerevisiae
    • Demoinet, E., Jacquier, A., Lutfalla, G., Fromont-Racine, M. The Hsp40 chaperone Jjj1 is required for the nucleo-cytoplasmic recycling of preribosomal factors in Saccharomyces cerevisiae. RNA 13, 1570-1581 (2007).
    • (2007) RNA , vol.13 , pp. 1570-1581
    • Demoinet, E.1    Jacquier, A.2    Lutfalla, G.3    Fromont-Racine, M.4
  • 31
    • 33646582609 scopus 로고    scopus 로고
    • Nuclear recycling of the pre-60S ribosomal subunit-associated factor Arx1 depends on Rei1 in Saccharomyces cerevisiae
    • Hung, N.J., Johnson, A.W. Nuclear recycling of the pre-60S ribosomal subunit-associated factor Arx1 depends on Rei1 in Saccharomyces cerevisiae. Mol. Cell. Biol. 26, 3718-3727 (2006).
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3718-3727
    • Hung, N.J.1    Johnson, A.W.2
  • 32
    • 33646391661 scopus 로고    scopus 로고
    • A functional network involved in the recycling of nucleocytoplasmic pre-60S factors
    • Lebreton, A. et al. A functional network involved in the recycling of nucleocytoplasmic pre-60S factors. J. Cell Biol. 173, 349-360 (2006).
    • (2006) J. Cell Biol. , vol.173 , pp. 349-360
    • Lebreton, A.1
  • 33
    • 14844327974 scopus 로고    scopus 로고
    • Release of the export adapter, Nmd3p, from the 60S ribosomal subunit requires Rpl10p and the cytoplasmic GTPase Lsg1p
    • Hedges, J., West, M., Johnson, A.W. Release of the export adapter, Nmd3p, from the 60S ribosomal subunit requires Rpl10p and the cytoplasmic GTPase Lsg1p. EMBO J. 24, 567-579 (2005).
    • (2005) EMBO J. , vol.24 , pp. 567-579
    • Hedges, J.1    West, M.2    Johnson, A.W.3
  • 34
    • 17644379370 scopus 로고    scopus 로고
    • Defining the order in which Nmd3p and Rpl10p load onto nascent 60S ribosomal subunits
    • West, M., Hedges, J.B., Chen, A., Johnson, A.W. Defining the order in which Nmd3p and Rpl10p load onto nascent 60S ribosomal subunits. Mol. Cell. Biol. 25, 3802-3813 (2005).
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 3802-3813
    • West, M.1    Hedges, J.B.2    Chen, A.3    Johnson, A.W.4
  • 35
    • 0035027807 scopus 로고    scopus 로고
    • Nuclear export of 60s ribosomal subunits depends on Xpo1p and requires a nuclear export sequence-containing factor, Nmd3p, that associates with the large subunit protein Rpl10p
    • Gadal, O. et al. Nuclear export of 60s ribosomal subunits depends on Xpo1p and requires a nuclear export sequence-containing factor, Nmd3p, that associates with the large subunit protein Rpl10p. Mol. Cell. Biol. 21, 3405-3415 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3405-3415
    • Gadal, O.1
  • 36
    • 18244408555 scopus 로고    scopus 로고
    • The nucle(ol)ar Tif6p and Efl1p are required for a late cytoplasmic step of ribosome synthesis
    • Senger, B. et al. The nucle(ol)ar Tif6p and Efl1p are required for a late cytoplasmic step of ribosome synthesis. Mol. Cell 8, 1363-1373 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 1363-1373
    • Senger, B.1
  • 37
    • 77954404581 scopus 로고    scopus 로고
    • Defining the pathway of cytoplasmic maturation of the 60S ribosomal subunit
    • Lo, K.Y. et al. Defining the pathway of cytoplasmic maturation of the 60S ribosomal subunit. Mol. Cell 39, 196-208 (2010).
    • (2010) Mol. Cell , vol.39 , pp. 196-208
    • Lo, K.Y.1
  • 38
    • 3242694353 scopus 로고    scopus 로고
    • A pre-ribosome with a tadpole-like structure functions in ATP-dependent maturation of 60S subunits
    • Nissan, T.A. et al. A pre-ribosome with a tadpole-like structure functions in ATP-dependent maturation of 60S subunits. Mol. Cell 15, 295-301 (2004).
    • (2004) Mol. Cell , vol.15 , pp. 295-301
    • Nissan, T.A.1
  • 39
    • 11244304243 scopus 로고    scopus 로고
    • Rea1 a dynein-related nuclear AAA-ATPase, is involved in late rRNA processing and nuclear export of 60 S subunits
    • Galani, K., Nissan, T.A., Petfalski, E., Tollervey, D., Hurt, E. Rea1, a dynein-related nuclear AAA-ATPase, is involved in late rRNA processing and nuclear export of 60 S subunits. J. Biol. Chem. 279, 55411-55418 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 55411-55418
    • Galani, K.1    Nissan, T.A.2    Petfalski, E.3    Tollervey, D.4    Hurt, E.5
  • 40
    • 79952254224 scopus 로고    scopus 로고
    • Crystal structure of the dynein motor domain
    • Carter, A.P., Cho, C., Jin, L., Vale, R.D. Crystal structure of the dynein motor domain. Science 331, 1159-1165 (2011).
    • (2011) Science , vol.331 , pp. 1159-1165
    • Carter, A.P.1    Cho, C.2    Jin, L.3    Vale, R.D.4
  • 41
    • 84859918439 scopus 로고    scopus 로고
    • The 2.8 Å crystal structure of the dynein motor domain
    • Kon, T. et al. The 2.8 Å crystal structure of the dynein motor domain. Nature 484, 345-350 (2012).
    • (2012) Nature , vol.484 , pp. 345-350
    • Kon, T.1
  • 42
    • 79952756302 scopus 로고    scopus 로고
    • The SUMO system controls nucleolar partitioning of a novel mammalian ribosome biogenesis complex
    • Finkbeiner, E., Haindl, M., Muller, S. The SUMO system controls nucleolar partitioning of a novel mammalian ribosome biogenesis complex. EMBO J. 30, 1067-1078 (2011).
    • (2011) EMBO J. , vol.30 , pp. 1067-1078
    • Finkbeiner, E.1    Haindl, M.2    Muller, S.3
  • 43
    • 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
  • 44
    • 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
  • 45
    • 73349085934 scopus 로고    scopus 로고
    • An auxin-based degron system for the rapid depletion of proteins in nonplant cells
    • Nishimura, K., Fukagawa, T., Takisawa, H., Kakimoto, T., Kanemaki, M. An auxin-based degron system for the rapid depletion of proteins in nonplant cells. Nat. Methods 6, 917-922 (2009).
    • (2009) Nat. Methods , vol.6 , pp. 917-922
    • Nishimura, K.1    Fukagawa, T.2    Takisawa, H.3    Kakimoto, T.4    Kanemaki, M.5
  • 46
    • 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
  • 47
    • 84936760336 scopus 로고    scopus 로고
    • Structural and functional analysis of the Rpf2-Rrs1 complex in ribosome biogenesis
    • Asano, N. et al. Structural and functional analysis of the Rpf2-Rrs1 complex in ribosome biogenesis. Nucleic Acids Res. 43, 4746-4757 (2015).
    • (2015) Nucleic Acids Res. , vol.43 , pp. 4746-4757
    • Asano, N.1
  • 48
    • 84946792425 scopus 로고    scopus 로고
    • The structure of Rpf2-Rrs1 explains its role in ribosome biogenesis
    • Kharde, S., Calvinõ, 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    Calvinõ, F.R.2    Gumiero, A.3    Wild, K.4    Sinning, I.5
  • 49
    • 84936990413 scopus 로고    scopus 로고
    • Chaperoning 5S RNA assembly
    • Madru, C. et al. Chaperoning 5S RNA assembly. Genes Dev. 29, 1432-1446 (2015).
    • (2015) Genes Dev. , vol.29 , pp. 1432-1446
    • Madru, C.1
  • 50
    • 84870855677 scopus 로고    scopus 로고
    • Targeted proteomics reveals compositional dynamics of 60S pre-ribosomes after nuclear export
    • Altvater, M. et al. Targeted proteomics reveals compositional dynamics of 60S pre-ribosomes after nuclear export. Mol. Syst. Biol. 8, 628 (2012).
    • (2012) Mol. Syst. Biol. , vol.8 , pp. 628
    • Altvater, M.1
  • 51
    • 0034099781 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae SDA1 gene is required for actin cytoskeleton organization and cell cycle progression
    • Buscemi, G., Saracino, F., Masnada, D., Carbone, M.L. The Saccharomyces cerevisiae SDA1 gene is required for actin cytoskeleton organization and cell cycle progression. J. Cell Sci. 113, 1199-1211 (2000).
    • (2000) J. Cell Sci. , vol.113 , pp. 1199-1211
    • Buscemi, G.1    Saracino, F.2    Masnada, D.3    Carbone, M.L.4
  • 52
    • 33645727798 scopus 로고    scopus 로고
    • Surveillance of nuclear-restricted pre-ribosomes within a subnucleolar region of Saccharomyces cerevisiae
    • Dez, C., Houseley, J., Tollervey, D. Surveillance of nuclear-restricted pre-ribosomes within a subnucleolar region of Saccharomyces cerevisiae. EMBO J. 25, 1534-1546 (2006).
    • (2006) EMBO J. , vol.25 , pp. 1534-1546
    • Dez, C.1    Houseley, J.2    Tollervey, D.3
  • 53
    • 84927142939 scopus 로고    scopus 로고
    • Symportin 1 chaperones 5S RNP assembly during ribosome biogenesis by occupying an essential rRNA-binding site
    • Calvinõ, F.R. et al. Symportin 1 chaperones 5S RNP assembly during ribosome biogenesis by occupying an essential rRNA-binding site. Nat. Commun. 6, 6510 (2015).
    • (2015) Nat. Commun. , vol.6 , pp. 6510
    • Calvinõ, F.R.1
  • 54
    • 84868223667 scopus 로고    scopus 로고
    • Synchronizing nuclear import of ribosomal proteins with ribosome assembly
    • Kressler, D. et al. Synchronizing nuclear import of ribosomal proteins with ribosome assembly. Science 338, 666-671 (2012).
    • (2012) Science , vol.338 , pp. 666-671
    • Kressler, D.1
  • 55
    • 84892443134 scopus 로고    scopus 로고
    • 5S ribosomal RNA is an essential component of a nascent ribosomal precursor complex that regulates the Hdm2-p53 checkpoint
    • Donati, G., Peddigari, S., Mercer, C.A., Thomas, G. 5S ribosomal RNA is an essential component of a nascent ribosomal precursor complex that regulates the Hdm2-p53 checkpoint. Cell Rep. 4, 87-98 (2013).
    • (2013) Cell Rep. , vol.4 , pp. 87-98
    • Donati, G.1    Peddigari, S.2    Mercer, C.A.3    Thomas, G.4
  • 56
    • 84938073179 scopus 로고    scopus 로고
    • Structure of human MDM2 complexed with RPL11 reveals the molecular basis of p53 activation
    • Zheng, J. et al. Structure of human MDM2 complexed with RPL11 reveals the molecular basis of p53 activation. Genes Dev. 29, 1524-1534 (2015).
    • (2015) Genes Dev. , vol.29 , pp. 1524-1534
    • Zheng, J.1
  • 57
    • 4444271170 scopus 로고    scopus 로고
    • A versatile toolbox for PCR-based tagging of yeast genes: New fluorescent proteins, more markers and promoter substitution cassettes
    • Janke, C. et al. A versatile toolbox for PCR-based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettes. Yeast 21, 947-962 (2004).
    • (2004) Yeast , vol.21 , pp. 947-962
    • Janke, C.1
  • 58
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine, M.S. et al. Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14, 953-961 (1998).
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1
  • 59
    • 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, E.A. Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast. Genetics 144, 1425-1436 (1996).
    • (1996) Genetics , vol.144 , pp. 1425-1436
    • James, P.1    Halladay, J.2    Craig, E.A.3
  • 60
    • 0024977417 scopus 로고
    • Elevated recombination rates in transcriptionally active DNA
    • Thomas, B.J., Rothstein, R. Elevated recombination rates in transcriptionally active DNA. Cell 56, 619-630 (1989).
    • (1989) Cell , vol.56 , pp. 619-630
    • Thomas, B.J.1    Rothstein, R.2
  • 61
    • 0029790980 scopus 로고    scopus 로고
    • The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl-and glutamyl-tRNA synthetases
    • Simos, G. et al. The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl-and glutamyl-tRNA synthetases. EMBO J. 15, 5437-5448 (1996).
    • (1996) EMBO J. , vol.15 , pp. 5437-5448
    • Simos, G.1
  • 62
    • 0038044717 scopus 로고    scopus 로고
    • Sequential protein association with nascent 60S ribosomal particles
    • Saveanu, C. et al. Sequential protein association with nascent 60S ribosomal particles. Mol. Cell. Biol. 23, 4449-4460 (2003).
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4449-4460
    • Saveanu, C.1
  • 63
    • 0037188922 scopus 로고    scopus 로고
    • Yph1p an ORC-interacting protein: Potential links between cell proliferation control DNA replication, and ribosome biogenesis
    • Du, Y.C., Stillman, B. Yph1p, an ORC-interacting protein: potential links between cell proliferation control, DNA replication, and ribosome biogenesis. Cell 109, 835-848 (2002).
    • (2002) Cell , vol.109 , pp. 835-848
    • Du, Y.C.1    Stillman, B.2
  • 64
    • 33748755088 scopus 로고    scopus 로고
    • Nsa2 is an unstable, conserved factor required for the maturation of 27 SB pre-rRNAs
    • Lebreton, A., Saveanu, C., Decourty, L., Jacquier, A., Fromont-Racine, M. Nsa2 is an unstable, conserved factor required for the maturation of 27 SB pre-rRNAs. J. Biol. Chem. 281, 27099-27108 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 27099-27108
    • Lebreton, A.1    Saveanu, C.2    Decourty, L.3    Jacquier, A.4    Fromont-Racine, M.5
  • 65
    • 0035882157 scopus 로고    scopus 로고
    • Cic1 an adaptor protein specifically linking the 26S proteasome to its substrate, the SCF component Cdc4
    • Jäger, S., Strayle, J., Heinemeyer, W., Wolf, D.H. Cic1, an adaptor protein specifically linking the 26S proteasome to its substrate, the SCF component Cdc4. EMBO J. 20, 4423-4431 (2001).
    • (2001) EMBO J. , vol.20 , pp. 4423-4431
    • Jäger, S.1    Strayle, J.2    Heinemeyer, W.3    Wolf, D.H.4
  • 66
    • 0031000833 scopus 로고    scopus 로고
    • Ribosomal protein L32 of Saccharomyces cerevisiae influences both the splicing of its own transcript and the processing of rRNA
    • Vilardell, J., Warner, J.R. Ribosomal protein L32 of Saccharomyces cerevisiae influences both the splicing of its own transcript and the processing of rRNA. Mol. Cell. Biol. 17, 1959-1965 (1997).
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1959-1965
    • Vilardell, J.1    Warner, J.R.2
  • 67
    • 0035844145 scopus 로고    scopus 로고
    • Scp160p, an RNA-binding, polysome-associated protein, localizes to the endoplasmic reticulum of Saccharomyces cerevisiae in a microtubule-dependent manner
    • Frey, S., Pool, M., Seedorf, M. Scp160p, an RNA-binding, polysome-associated protein, localizes to the endoplasmic reticulum of Saccharomyces cerevisiae in a microtubule-dependent manner. J. Biol. Chem. 276, 15905-15912 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 15905-15912
    • Frey, S.1    Pool, M.2    Seedorf, M.3
  • 68
    • 26944459664 scopus 로고    scopus 로고
    • The essential WD-repeat protein Rsa4p is required for rRNA processing and intra-nuclear transport of 60S ribosomal subunits
    • de la Cruz, J., Sanz-Martínez, E., Remacha, M. The essential WD-repeat protein Rsa4p is required for rRNA processing and intra-nuclear transport of 60S ribosomal subunits. Nucleic Acids Res. 33, 5728-5739 (2005).
    • (2005) Nucleic Acids Res. , vol.33 , pp. 5728-5739
    • De La Cruz, J.1    Sanz-Martínez, E.2    Remacha, M.3
  • 69
    • 0000254254 scopus 로고    scopus 로고
    • Identification of a 60S preribosomal particle that is closely linked to nuclear export
    • Bassler, J. et al. Identification of a 60S preribosomal particle that is closely linked to nuclear export. Mol. Cell 8, 517-529 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 517-529
    • Bassler, J.1
  • 70
    • 84883489254 scopus 로고    scopus 로고
    • Protein interfaces of the conserved Nup84 complex from Chaetomium thermophilum shown by crosslinking mass spectrometry and electron microscopy
    • Thierbach, K. et al. Protein interfaces of the conserved Nup84 complex from Chaetomium thermophilum shown by crosslinking mass spectrometry and electron microscopy. Structure 21, 1672-1682 (2013).
    • (2013) Structure , vol.21 , pp. 1672-1682
    • Thierbach, K.1
  • 71
    • 84866118432 scopus 로고    scopus 로고
    • False discovery rate estimation for cross-linked peptides identified by mass spectrometry
    • Walzthoeni, T. et al. False discovery rate estimation for cross-linked peptides identified by mass spectrometry. Nat. Methods 9, 901-903 (2012).
    • (2012) Nat. Methods , vol.9 , pp. 901-903
    • Walzthoeni, T.1
  • 72
    • 41449110185 scopus 로고    scopus 로고
    • Identification of cross-linked peptides from large sequence databases
    • Rinner, O. et al. Identification of cross-linked peptides from large sequence databases. Nat. Methods 5, 315-318 (2008).
    • (2008) Nat. Methods , vol.5 , pp. 315-318
    • Rinner, O.1
  • 73
    • 84926486138 scopus 로고    scopus 로고
    • XiNET: Cross-link network maps with residue resolution
    • Combe, C.W., Fischer, L., Rappsilber, J. xiNET: cross-link network maps with residue resolution. Mol. Cell. Proteomics 14, 1137-1147 (2015).
    • (2015) Mol. Cell. Proteomics , vol.14 , pp. 1137-1147
    • Combe, C.W.1    Fischer, L.2    Rappsilber, J.3
  • 74
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke, S.J., Baldwin, P.R., Chiu, W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128, 82-97 (1999).
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 76
    • 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. 49, 2574 (2011).
    • (2011) J. Vis. Exp. , vol.49 , pp. 2574
    • Liu, X.1    Wang, H.W.2
  • 77
    • 24044434272 scopus 로고    scopus 로고
    • Reconstitution of Nup157 and Nup145N into the Nup84 complex
    • Lutzmann, M. et al. Reconstitution of Nup157 and Nup145N into the Nup84 complex. J. Biol. Chem. 280, 18442-18451 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 18442-18451
    • Lutzmann, M.1
  • 78
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera: A visualization system for exploratory research and analysis
    • Pettersen, E.F. et al. UCSF Chimera: a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 79
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
    • Li, X. et al. Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nat. Methods 10, 584-590 (2013).
    • (2013) Nat. Methods , vol.10 , pp. 584-590
    • Li, X.1
  • 80
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank, J. et al. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116, 190-199 (1996).
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1
  • 81
    • 33845449481 scopus 로고    scopus 로고
    • SIGNATURE: A single-particle selection system for molecular electron microscopy
    • Chen, J.Z., Grigorieff, N. SIGNATURE: a single-particle selection system for molecular electron microscopy. J. Struct. Biol. 157, 168-173 (2007).
    • (2007) J. Struct. Biol. , vol.157 , pp. 168-173
    • Chen, J.Z.1    Grigorieff, N.2
  • 82
    • 84894623755 scopus 로고    scopus 로고
    • Quantifying the local resolution of cryo-EM density maps
    • Kucukelbir, A., Sigworth, F.J., Tagare, H.D. Quantifying the local resolution of cryo-EM density maps. Nat. Methods 11, 63-65 (2014).
    • (2014) Nat. Methods , vol.11 , pp. 63-65
    • Kucukelbir, A.1    Sigworth, F.J.2    Tagare, H.D.3
  • 83
    • 83855162728 scopus 로고    scopus 로고
    • The structure of the eukaryotic ribosome at 3.0 Å resolution
    • Ben-Shem, A. et al. The structure of the eukaryotic ribosome at 3.0 Å resolution. Science 334, 1524-1529 (2011).
    • (2011) Science , vol.334 , pp. 1524-1529
    • Ben-Shem, A.1
  • 84
    • 42949089487 scopus 로고    scopus 로고
    • Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics
    • Trabuco, L.G., Villa, E., Mitra, K., Frank, J., Schulten, K. Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics. Structure 16, 673-683 (2008).
    • (2008) Structure , vol.16 , pp. 673-683
    • Trabuco, L.G.1    Villa, E.2    Mitra, K.3    Frank, J.4    Schulten, K.5
  • 85
    • 43749107283 scopus 로고    scopus 로고
    • Comparative protein structure modeling using Modeller
    • Eswar, N. et al. Comparative protein structure modeling using Modeller. Curr. Protoc. Bioinformatics 15, 5.6 (2006).
    • (2006) Curr. Protoc. Bioinformatics , vol.15 , pp. 5-6
    • Eswar, N.1
  • 86
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • Söding, J., Biegert, A., Lupas, A.N. The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res. 33, W244-W248 (2005).
    • (2005) Nucleic Acids Res. , vol.33 , pp. W244-W248
    • Söding, J.1    Biegert, A.2    Lupas, A.N.3
  • 87
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P.D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 88
    • 84897964300 scopus 로고    scopus 로고
    • A new system for naming ribosomal proteins
    • Ban, N. et al. A new system for naming ribosomal proteins. Curr. Opin. Struct. Biol. 24, 165-169 (2014).
    • (2014) Curr. Opin. Struct. Biol. , vol.24 , pp. 165-169
    • Ban, N.1
  • 89
    • 36448991500 scopus 로고    scopus 로고
    • Clustal W and Clustal X version 2.0
    • Larkin, M.A. et al. Clustal W and Clustal X version 2.0. Bioinformatics 23, 2947-2948 (2007).
    • (2007) Bioinformatics , vol.23 , pp. 2947-2948
    • Larkin, M.A.1
  • 90
    • 65449188232 scopus 로고    scopus 로고
    • Jalview Version 2: A multiple sequence alignment editor and analysis workbench
    • Waterhouse, A.M., Procter, J.B., Martin, D.M., Clamp, M., Barton, G.J. Jalview Version 2: a multiple sequence alignment editor and analysis workbench. Bioinformatics 25, 1189-1191 (2009).
    • (2009) Bioinformatics , vol.25 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.3    Clamp, M.4    Barton, G.J.5


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