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Volumn 43, Issue 9, 2015, Pages 4746-4757

Structural and functional analysis of the Rpf2-Rrs1 complex in ribosome biogenesis

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL PROTEIN; RNA 5S; RPF2 PROTEIN; RRS1 PROTEIN; UNCLASSIFIED DRUG; PROTEIN BINDING; RIBOSOME PROTEIN;

EID: 84936760336     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkv305     Document Type: Article
Times cited : (39)

References (41)
  • 1
    • 0038738334 scopus 로고    scopus 로고
    • Pre-ribosomes on the road from the nucleolus to the cytoplasm
    • Tschochner, H. and Hurt, E. (2003) Pre-ribosomes on the road from the nucleolus to the cytoplasm. Trends Cell Biol., 13, 255-263.
    • (2003) Trends Cell Biol , vol.13 , pp. 255-263
    • Tschochner, H.1    Hurt, E.2
  • 2
    • 0033509092 scopus 로고    scopus 로고
    • Protein trans-acting factors involved in ribosome biogenesis in Saccharomyces cerevisiae
    • Kressler, D., Linder, P. and de La Cruz, J. (1999) Protein trans-acting factors involved in ribosome biogenesis in Saccharomyces cerevisiae. Mol. Cell. Biol., 19, 7897-7912.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 7897-7912
    • Kressler, D.1    Linder, P.2    De La Cruz, J.3
  • 3
    • 0033367325 scopus 로고    scopus 로고
    • Ribosome synthesis in Saccharomyces cerevisiae
    • Venema, J. and Tollervey, D. (1999) Ribosome synthesis in Saccharomyces cerevisiae. Annu. Rev. Genet., 33, 261-311.
    • (1999) Annu. Rev. Genet , vol.33 , pp. 261-311
    • Venema, J.1    Tollervey, D.2
  • 5
    • 0037054550 scopus 로고    scopus 로고
    • Rlp7p is associated with 60S preribosomes, restricted to the granular component of the nucleolus, and required for pre-rRNA processing
    • Gadal, O., Strauss, D., Petfalski, E., Gleizes, P.E., Gas, N., Tollervey, D. and Hurt, E. (2002) Rlp7p is associated with 60S preribosomes, restricted to the granular component of the nucleolus, and required for pre-rRNA processing. J. Cell Biol., 157, 941-951.
    • (2002) J. Cell Biol , vol.157 , pp. 941-951
    • Gadal, O.1    Strauss, D.2    Petfalski, E.3    Gleizes, P.E.4    Gas, N.5    Tollervey, D.6    Hurt, E.7
  • 6
    • 0033485458 scopus 로고    scopus 로고
    • Ribosomal internal transcribed spacer 2 (ITS2) exhibits a common core of secondary structure in vertebrates and yeast
    • Joseph, N., Krauskopf, E., Vera, M.I. and Michot, B. (1999) Ribosomal internal transcribed spacer 2 (ITS2) exhibits a common core of secondary structure in vertebrates and yeast. Nucleic Acids Res., 27, 4533-4540.
    • (1999) Nucleic Acids Res , vol.27 , pp. 4533-4540
    • Joseph, N.1    Krauskopf, E.2    Vera, M.I.3    Michot, B.4
  • 7
    • 0025266635 scopus 로고
    • Structural analysis of the internal transcribed spacer 2 of the precursor ribosomal RNA from Saccharomyces cerevisiae
    • Yeh, L.C. and Lee, J.C. (1990) Structural analysis of the internal transcribed spacer 2 of the precursor ribosomal RNA from Saccharomyces cerevisiae. J. Mol. Biol., 211, 699-712.
    • (1990) J. Mol. Biol , vol.211 , pp. 699-712
    • Yeh, L.C.1    Lee, J.C.2
  • 8
    • 84887113964 scopus 로고    scopus 로고
    • Ribosome biogenesis in the yeast Saccharomyces cerevisiae
    • Woolford, J.L. Jr and Baserga, S.J. (2013) Ribosome biogenesis in the yeast Saccharomyces cerevisiae. Genetics, 195, 643-681.
    • (2013) Genetics , vol.195 , pp. 643-681
    • Woolford, J.L.1    Baserga, S.J.2
  • 9
    • 0035370085 scopus 로고    scopus 로고
    • The Brix domain protein family-a key to the ribosomal biogenesis pathway?
    • Eisenhaber, F., Wechselberger, C. and Kreil, G. (2001) The Brix domain protein family-a key to the ribosomal biogenesis pathway? Trends Biochem. Sci., 26, 345-347.
    • (2001) Trends Biochem, Sci , vol.26 , pp. 345-347
    • Eisenhaber, F.1    Wechselberger, C.2    Kreil, G.3
  • 10
    • 0036183980 scopus 로고    scopus 로고
    • The sigma(70)-like motif: A eukaryotic RNA binding domain unique to a superfamily of proteins required for ribosome biogenesis
    • Wehner, K.A. and Baserga, S.J. (2002) The sigma(70)-like motif: a eukaryotic RNA binding domain unique to a superfamily of proteins required for ribosome biogenesis. Mol. Cell, 9, 329-339.
    • (2002) Mol. Cell , vol.9 , pp. 329-339
    • Wehner, K.A.1    Baserga, S.J.2
  • 11
    • 0032808151 scopus 로고    scopus 로고
    • Imp3p and Imp4p two specific components of the U3 small nucleolar ribonucleoprotein that are essential for pre-18S rRNA processing
    • Lee, S.J. and Baserga, S.J. (1999) Imp3p and Imp4p, two specific components of the U3 small nucleolar ribonucleoprotein that are essential for pre-18S rRNA processing. Mol. Cell. Biol., 19, 5441-5452.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 5441-5452
    • Lee, S.J.1    Baserga, S.J.2
  • 12
    • 0037386438 scopus 로고    scopus 로고
    • The human Imp3 and Imp4 proteins form a ternary complex with hMpp10, which only interacts with the U3 snoRNA in 60-80S ribonucleoprotein complexes
    • Granneman, S., Gallagher, J.E., Vogelzangs, J., Horstman, W., van Venrooij, W.J., Baserga, S.J. and Pruijn, G.J. (2003) The human Imp3 and Imp4 proteins form a ternary complex with hMpp10, which only interacts with the U3 snoRNA in 60-80S ribonucleoprotein complexes. Nucleic Acids Res., 31, 1877-1887.
    • (2003) Nucleic Acids Res , vol.31 , pp. 1877-1887
    • Granneman, S.1    Gallagher, J.E.2    Vogelzangs, J.3    Horstman, W.4    Van Venrooij, W.J.5    Baserga, S.J.6    Pruijn, G.J.7
  • 13
    • 37549012958 scopus 로고    scopus 로고
    • The U3 small nucleolar ribonucleoprotein component Imp4p is a telomeric DNA-binding protein
    • Hsieh, Y.C., Tu, P.J., Lee, Y.Y., Kuo, C.C., Lin, Y.C., Wu, C.F. and Lin, J.J. (2007) The U3 small nucleolar ribonucleoprotein component Imp4p is a telomeric DNA-binding protein. Biochem. J., 408, 387-393.
    • (2007) Biochem. J , vol.408 , pp. 387-393
    • Hsieh, Y.C.1    Tu, P.J.2    Lee, Y.Y.3    Kuo, C.C.4    Lin, Y.C.5    Wu, C.F.6    Lin, J.J.7
  • 14
    • 14644393728 scopus 로고    scopus 로고
    • Crystal structure of Mil (Mth680): Internal duplication and similarity between the Imp4/Brix domain and the anticodon-binding domain of class IIa aminoacyl-tRNA synthetases
    • Ng, C.L., Waterman, D., Koonin, E.V., Antson, A.A. and Ortiz-Lombardia, M. (2005) Crystal structure of Mil (Mth680): internal duplication and similarity between the Imp4/Brix domain and the anticodon-binding domain of class IIa aminoacyl-tRNA synthetases. EMBO Rep., 6, 140-146.
    • (2005) EMBO Rep , vol.6 , pp. 140-146
    • Ng, C.L.1    Waterman, D.2    Koonin, E.V.3    Antson, A.A.4    Ortiz-Lombardia, M.5
  • 15
    • 0033994223 scopus 로고    scopus 로고
    • RRS1, a conserved essential gene, encodes a novel regulatory protein required for ribosome biogenesis in Saccharomyces cerevisiae
    • Tsuno, A., Miyoshi, K., Tsujii, R., Miyakawa, T. and Mizuta, K. (2000) RRS1, a conserved essential gene, encodes a novel regulatory protein required for ribosome biogenesis in Saccharomyces cerevisiae. Mol. Cell. Biol., 20, 2066-2074.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 2066-2074
    • Tsuno, A.1    Miyoshi, K.2    Tsujii, R.3    Miyakawa, T.4    Mizuta, K.5
  • 16
    • 80052767367 scopus 로고    scopus 로고
    • Ribosome biogenesis factors bind a nuclear envelope SUN domain protein to cluster yeast telomeres
    • Horigome, C., Okada, T., Shimazu, K., Gasser, S.M. and Mizuta, K. (2011) Ribosome biogenesis factors bind a nuclear envelope SUN domain protein to cluster yeast telomeres. EMBO J., 30, 3799-3811.
    • (2011) EMBO J. , vol.30 , pp. 3799-3811
    • Horigome, C.1    Okada, T.2    Shimazu, K.3    Gasser, S.M.4    Mizuta, K.5
  • 18
    • 0037047270 scopus 로고    scopus 로고
    • Rpf2p, an evolutionarily conserved protein, interacts with ribosomal protein L11 and is essential for the processing of 27 SB Pre-rRNA to 25 S rRNA and the 60 S ribosomal subunit assembly in Saccharomyces cerevisiae
    • Morita, D., Miyoshi, K., Matsui, Y., Toh, E.A., Shinkawa, H., Miyakawa, T. and Mizuta, K. (2002) Rpf2p, an evolutionarily conserved protein, interacts with ribosomal protein L11 and is essential for the processing of 27 SB Pre-rRNA to 25 S rRNA and the 60 S ribosomal subunit assembly in Saccharomyces cerevisiae. J. Biol. Chem., 277, 28780-28786.
    • (2002) J. Biol. Chem , vol.277 , pp. 28780-28786
    • Morita, D.1    Miyoshi, K.2    Matsui, Y.3    Toh, E.A.4    Shinkawa, H.5    Miyakawa, T.6    Mizuta, K.7
  • 19
    • 0037166233 scopus 로고    scopus 로고
    • Normal assembly of 60 S ribosomal subunits is required for the signaling in response to a secretory defect in Saccharomyces cerevisiae
    • Miyoshi, K., Tsujii, R., Yoshida, H., Maki, Y., Wada, A., Matsui, Y., Toh, E.A. and Mizuta, K. (2002) Normal assembly of 60 S ribosomal subunits is required for the signaling in response to a secretory defect in Saccharomyces cerevisiae. J. Biol. Chem., 277, 18334-18339.
    • (2002) J. Biol. Chem , vol.277 , pp. 18334-18339
    • Miyoshi, K.1    Tsujii, R.2    Yoshida, H.3    Maki, Y.4    Wada, A.5    Matsui, Y.6    Toh, E.A.7    Mizuta, K.8
  • 20
    • 2342664094 scopus 로고    scopus 로고
    • Rrs1p, a ribosomal protein L11-binding protein, is required for nuclear export of the 60S pre-ribosomal subunit in Saccharomyces cerevisiae
    • Miyoshi, K., Shirai, C., Horigome, C., Takenami, K., Kawasaki, J. and Mizuta, K. (2004) Rrs1p, a ribosomal protein L11-binding protein, is required for nuclear export of the 60S pre-ribosomal subunit in Saccharomyces cerevisiae. FEBS Lett., 565, 106-110.
    • (2004) FEBS Lett , vol.565 , pp. 106-110
    • Miyoshi, K.1    Shirai, C.2    Horigome, C.3    Takenami, K.4    Kawasaki, J.5    Mizuta, K.6
  • 21
    • 23844511660 scopus 로고    scopus 로고
    • Synergistic defect in 60S ribosomal subunit assembly caused by a mutation of Rrs1p, a ribosomal protein L11-binding protein, and 3-extension of 5S rRNA in Saccharomyces cerevisiae
    • Nariai, M., Tanaka, T., Okada, T., Shirai, C., Horigome, C. and Mizuta, K. (2005) Synergistic defect in 60S ribosomal subunit assembly caused by a mutation of Rrs1p, a ribosomal protein L11-binding protein, and 3-extension of 5S rRNA in Saccharomyces cerevisiae. Nucleic Acids Res., 33, 4553-4562.
    • (2005) Nucleic Acids Res , vol.33 , pp. 4553-4562
    • Nariai, M.1    Tanaka, T.2    Okada, T.3    Shirai, C.4    Horigome, C.5    Mizuta, K.6
  • 22
    • 84925884550 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of ribosome assembly factors: The Rpf2-Rrs1 complex
    • Asano, N., Nakamura, A., Komoda, K., Kato, K., Tanaka, I. and Yao, M. (2014) Crystallization and preliminary X-ray crystallographic analysis of ribosome assembly factors: the Rpf2-Rrs1 complex. Acta Crystallogr. F, 70, 1649-1652.
    • (2014) Acta Crystallogr. F , vol.70 , pp. 1649-1652
    • Asano, N.1    Nakamura, A.2    Komoda, K.3    Kato, K.4    Tanaka, I.5    Yao, M.6
  • 27
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. and Cowtan, K. (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr. D, 60, 2126-2132.
    • (2004) Acta Crystallogr D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 28
    • 57049150788 scopus 로고    scopus 로고
    • The ConSurf-DB: Pre-calculated evolutionary conservation profiles of protein structures
    • Goldenberg, O., Erez, E., Nimrod, G. and Ben-Tal, N. (2009) The ConSurf-DB: pre-calculated evolutionary conservation profiles of protein structures. Nucleic Acids Res., 37, D323-D327.
    • (2009) Nucleic Acids Res , vol.37 , pp. D323-D327
    • Goldenberg, O.1    Erez, E.2    Nimrod, G.3    Ben-Tal, N.4
  • 30
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G. and Gibson, T.J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res., 22, 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 31
    • 84904790793 scopus 로고    scopus 로고
    • Deciphering key features in protein structures with the new ENDscript server
    • Robert, X. and Gouet, P. (2014) Deciphering key features in protein structures with the new ENDscript server. Nucleic Acids Res., 42, W320-W324.
    • (2014) Nucleic Acids Res , vol.42 , pp. W320-W324
    • Robert, X.1    Gouet, P.2
  • 33
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm, L. and Rosenstrom, P. (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res., 38, W545-W549.
    • (2010) Nucleic Acids Res. , vol.38 , pp. W545-W549
    • Holm, L.1    Rosenstrom, P.2
  • 34
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin, L.J., Bryson, K. and Jones, D.T. (2000) The PSIPRED protein structure prediction server. Bioinformatics, 16, 404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 35
    • 7444265178 scopus 로고    scopus 로고
    • Imp3p and Imp4p mediate formation of essential U3-precursor rRNA (pre-rRNA) duplexes possibly to recruit the small subunit processome to the pre-rRNA
    • Gerczei, T. and Correll, C.C. (2004) Imp3p and Imp4p mediate formation of essential U3-precursor rRNA (pre-rRNA) duplexes, possibly to recruit the small subunit processome to the pre-rRNA. Proc. Natl. Acad. Sci. U.S.A., 101, 15301-15306.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 15301-15306
    • Gerczei, T.1    Correll, C.C.2
  • 36
    • 0036878154 scopus 로고    scopus 로고
    • An analysis of protein domain linkers: Their classification and role in protein folding
    • George, R.A. and Heringa, J. (2002) An analysis of protein domain linkers: their classification and role in protein folding. Protein Eng., 15, 871-879.
    • (2002) Protein Eng , vol.15 , pp. 871-879
    • George, R.A.1    Heringa, J.2
  • 37
    • 0024403543 scopus 로고
    • The Q-linker: A class of interdomain sequences found in bacterial multidomain regulatory proteins
    • Wootton, J.C. and Drummond, M.H. (1989) The Q-linker: a class of interdomain sequences found in bacterial multidomain regulatory proteins. Protein Eng., 2, 535-543.
    • (1989) Protein Eng , vol.2 , pp. 535-543
    • Wootton, J.C.1    Drummond, M.H.2
  • 39
    • 77953135927 scopus 로고    scopus 로고
    • Neck linker length determines the degree of processivity in kinesin-1 and kinesin-2 motors
    • Shastry, S. and Hancock, W.O. (2010) Neck linker length determines the degree of processivity in kinesin-1 and kinesin-2 motors. Curr. Biol., 20, 939-943.
    • (2010) Curr. Biol. , vol.20 , pp. 939-943
    • Shastry, S.1    Hancock, W.O.2


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