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Volumn 38, Issue 4, 2009, Pages 1261-1272

Yeast strains with N-terminally truncated ribosomal protein S5: Implications for the evolution, structure and function of the Rps5/Rps7 proteins

Author keywords

[No Author keywords available]

Indexed keywords

INITIATION FACTOR 2; INITIATION FACTOR 3; PROTEIN S 5; PROTEIN S7; RIBOSOME PROTEIN; RIBOSOME RNA; UNCLASSIFIED DRUG; ESCHERICHIA COLI PROTEIN; RIBOSOMAL PROTEIN S5; RIBOSOMAL PROTEIN S7; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 77950349471     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkp1113     Document Type: Article
Times cited : (24)

References (45)
  • 1
    • 0037115872 scopus 로고    scopus 로고
    • Comparative analysis of ribosomal proteins in complete genomes: an example of reductive evolution at the domain scale
    • Lecompte, O., Ripp, R., Thierry, J.C., Moras, D. and Poch, O. (2002) Comparative analysis of ribosomal proteins in complete genomes: an example of reductive evolution at the domain scale. Nucleic Acids Res., 30, 5382-5390.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 5382-5390
    • Lecompte, O.1    Ripp, R.2    Thierry, J.C.3    Moras, D.4    Poch, O.5
  • 3
    • 33645467060 scopus 로고    scopus 로고
    • Eukaryotic ribosomal proteins lacking a eubacterial counterpart: important players in ribosomal function
    • Dresios, J., Panopoulos, P. and Synetos, D. (2006) Eukaryotic ribosomal proteins lacking a eubacterial counterpart: important players in ribosomal function. Mol. Microbiol., 59, 1651-1663.
    • (2006) Mol. Microbiol. , vol.59 , pp. 1651-1663
    • Dresios, J.1    Panopoulos, P.2    Synetos, D.3
  • 4
    • 0029402642 scopus 로고
    • Structure and evolution of mammalian ribosomal proteins
    • Wool, I.G., Chan, Y.L. and Gluck, A. (1995) Structure and evolution of mammalian ribosomal proteins. Biochem. Cell Biol., 73, 933-947.
    • (1995) Biochem. Cell Biol. , vol.73 , pp. 933-947
    • Wool, I.G.1    Chan, Y.L.2    Gluck, A.3
  • 5
    • 0028863027 scopus 로고
    • Cloning and characterisation of the gene encoding the ribosomal protein S5 (also known as rp14, S2, YS8) of Saccharomyces cerevisiae
    • Ignatovich, O., Cooper, M., Kulesza, H.M. and Beggs, J.D. (1995) Cloning and characterisation of the gene encoding the ribosomal protein S5 (also known as rp14, S2, YS8) of Saccharomyces cerevisiae. Nucleic Acids Res., 23, 4616-4619.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 4616-4619
    • Ignatovich, O.1    Cooper, M.2    Kulesza, H.M.3    Beggs, J.D.4
  • 6
    • 36248983727 scopus 로고    scopus 로고
    • Roles of the negatively charged N-terminal extension of Saccharomyces cerevisiae ribosomal protein S5 revealed by characterization of a yeast strain containing human ribosomal protein S5
    • Galkin, O., Bentley, A.A., Gupta, S., Compton, B.A., Mazumder, B., Kinzy, T.G., Merrick, W.C., Hatzoglou, M., Pestova, T.V., Hellen, C.U. et al. (2007) Roles of the negatively charged N-terminal extension of Saccharomyces cerevisiae ribosomal protein S5 revealed by characterization of a yeast strain containing human ribosomal protein S5. RNA, 13, 2116-2128.
    • (2007) RNA , vol.13 , pp. 2116-2128
    • Galkin, O.1    Bentley, A.A.2    Gupta, S.3    Compton, B.A.4    Mazumder, B.5    Kinzy, T.G.6    Merrick, W.C.7    Hatzoglou, M.8    Pestova, T.V.9    Hellen, C.U.10
  • 8
    • 0035798380 scopus 로고    scopus 로고
    • Structure of the 80S ribosome from Saccharomyces cerevisiae-tRNA-ribosome and subunit-subunit interactions
    • Spahn, C.M., Beckmann, R., Eswar, N., Penczek, P.A., Sali, A., Blobel, G. and Frank, J. (2001) Structure of the 80S ribosome from Saccharomyces cerevisiae-tRNA-ribosome and subunit-subunit interactions. Cell, 107, 373-386.
    • (2001) Cell , vol.107 , pp. 373-386
    • Spahn, C.M.1    Beckmann, R.2    Eswar, N.3    Penczek, P.A.4    Sali, A.5    Blobel, G.6    Frank, J.7
  • 9
    • 0242414021 scopus 로고    scopus 로고
    • A functional interaction between ribosomal proteins S7 and S11 within the bacterial ribosome
    • Robert, F. and Brakier-Gingras, L. (2003) A functional interaction between ribosomal proteins S7 and S11 within the bacterial ribosome. J. Biol. Chem., 278, 44913-44920.
    • (2003) J. Biol. Chem. , vol.278 , pp. 44913-44920
    • Robert, F.1    Brakier-Gingras, L.2
  • 10
    • 0028953840 scopus 로고
    • Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds
    • Mumberg, D., Muller, R. and Funk, M. (1995) Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds. Gene, 156, 119-122.
    • (1995) Gene , vol.156 , pp. 119-122
    • Mumberg, D.1    Muller, R.2    Funk, M.3
  • 12
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Fukuda, Y., Murata, K. and Kimura, A. (1983) Transformation of intact yeast cells treated with alkali cations. J. Bacteriol., 53, 163-168.
    • (1983) J. Bacteriol. , vol.53 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 13
    • 0023341242 scopus 로고
    • A segment of GCN4 mRNA containing the upstream AUG codons confers translational control upon a heterologous yeast transcript
    • Mueller, P.P., Harashima, S. and Hinnebusch, A.G. (1987) A segment of GCN4 mRNA containing the upstream AUG codons confers translational control upon a heterologous yeast transcript. Proc. Natl Acad. Sci. USA, 84, 2863-2867.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 2863-2867
    • Mueller, P.P.1    Harashima, S.2    Hinnebusch, A.G.3
  • 14
    • 0037416198 scopus 로고    scopus 로고
    • Internal initiation drives the synthesis of Ure2 protein lacking the prion domain and affects [URE3] propagation in yeast cells
    • Komar, A.A., Lesnik, T., Cullin, C., Merrick, W.C., Trachsel, H. and Altmann, M. (2003) Internal initiation drives the synthesis of Ure2 protein lacking the prion domain and affects [URE3] propagation in yeast cells. EMBO J., 22, 1199-1209.
    • (2003) EMBO J. , vol.22 , pp. 1199-1209
    • Komar, A.A.1    Lesnik, T.2    Cullin, C.3    Merrick, W.C.4    Trachsel, H.5    Altmann, M.6
  • 15
    • 18144363165 scopus 로고    scopus 로고
    • Novel characteristics of the biological properties of the yeast Saccharomyces cerevisiae eukaryotic initiation factor 2A
    • Komar, A.A., Gross, S.R., Barth-Baus, D., Strachan, R., Hensold, J.O., Goss Kinzy, T. and Merrick, W.C. (2005) Novel characteristics of the biological properties of the yeast Saccharomyces cerevisiae eukaryotic initiation factor 2A. J. Biol. Chem., 280, 15601-15611.
    • (2005) J. Biol. Chem. , vol.280 , pp. 15601-15611
    • Komar, A.A.1    Gross, S.R.2    Barth-Baus, D.3    Strachan, R.4    Hensold, J.O.5    Goss Kinzy, T.6    Merrick, W.C.7
  • 16
    • 0042703890 scopus 로고    scopus 로고
    • An in vivo dual-luciferase assay system for studying translational recoding in the yeast Saccharomyces cerevisiae
    • Harger, J.W. and Dinman, J.D. (2003) An in vivo dual-luciferase assay system for studying translational recoding in the yeast Saccharomyces cerevisiae. RNA, 9, 1019-1024.
    • (2003) RNA , vol.9 , pp. 1019-1024
    • Harger, J.W.1    Dinman, J.D.2
  • 17
    • 7044260452 scopus 로고    scopus 로고
    • Evidence against a direct role for the Upf proteins in frameshifting or nonsense codon readthrough
    • Harger, J.W. and Dinman, J.D. (2004) Evidence against a direct role for the Upf proteins in frameshifting or nonsense codon readthrough. RNA, 10, 1721-1729.
    • (2004) RNA , vol.10 , pp. 1721-1729
    • Harger, J.W.1    Dinman, J.D.2
  • 18
    • 0025869164 scopus 로고
    • GCD2, a translational repressor of the GCN4 gene, has a general function in the initiation of protein synthesis in Saccharomyces cerevisiae
    • Foiani, M., Cigan, A.M., Paddon, C.J., Harashima, S. and Hinnebusch, A.G. (1991) GCD2, a translational repressor of the GCN4 gene, has a general function in the initiation of protein synthesis in Saccharomyces cerevisiae. Mol. Cell. Biol., 11, 3203-3216.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3203-3216
    • Foiani, M.1    Cigan, A.M.2    Paddon, C.J.3    Harashima, S.4    Hinnebusch, A.G.5
  • 19
    • 34249857603 scopus 로고    scopus 로고
    • Salicylates trigger protein synthesis inhibition in a protein kinase R-like endoplasmic reticulum kinase-dependent manner
    • Silva, A.M., Wang, D., Komar, A.A., Castilho, B.A. and Williams, B.R. (2007) Salicylates trigger protein synthesis inhibition in a protein kinase R-like endoplasmic reticulum kinase-dependent manner. J. Biol. Chem., 282, 10164-10171.
    • (2007) J. Biol. Chem. , vol.282 , pp. 10164-10171
    • Silva, A.M.1    Wang, D.2    Komar, A.A.3    Castilho, B.A.4    Williams, B.R.5
  • 20
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin, H., Staehelin, T. and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl Acad. Sci. USA, 76, 4350-4354.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 21
    • 0028971194 scopus 로고
    • Modulation of tRNA(iMet), eIF-2, and eIF-2B expression shows that GCN4 translation is inversely coupled to the level of eIF-2.GTP. Met-tRNA(iMet) ternary complexes
    • Dever, T.E., Yang, W., Aström, S., Byström, A.S. and Hinnebusch, A.G. (1995) Modulation of tRNA(iMet), eIF-2, and eIF-2B expression shows that GCN4 translation is inversely coupled to the level of eIF-2.GTP.Met-tRNA(iMet) ternary complexes. Mol. Cell. Biol., 15, 6351-6363.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6351-6363
    • Dever, T.E.1    Yang, W.2    Aström, S.3    Byström, A.S.4    Hinnebusch, A.G.5
  • 22
    • 0031876171 scopus 로고    scopus 로고
    • Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5
    • Phan, L., Zhang, X., Asano, K., Anderson, J., Vornlocher, H.P., Greenberg, J.R., Qin, J. and Hinnebusch, A.G. (1998) Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5. Mol. Cell. Biol., 18, 4935-4946.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4935-4946
    • Phan, L.1    Zhang, X.2    Asano, K.3    Anderson, J.4    Vornlocher, H.P.5    Greenberg, J.R.6    Qin, J.7    Hinnebusch, A.G.8
  • 23
    • 0017690216 scopus 로고
    • Method for detection of specific RNAs in agarose gels by transfer to diazobenzyloxymethyl-paper and hybridization with DNA probes
    • Alwine, J.C., Kemp, D.J. and Stark, G.R. (1977) Method for detection of specific RNAs in agarose gels by transfer to diazobenzyloxymethyl-paper and hybridization with DNA probes. Proc. Natl Acad. Sci. USA, 74, 5350-5354.
    • (1977) Proc. Natl Acad. Sci. USA , vol.74 , pp. 5350-5354
    • Alwine, J.C.1    Kemp, D.J.2    Stark, G.R.3
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 16544392668 scopus 로고    scopus 로고
    • Systematic analysis of bicistronic reporter assay data
    • Jacobs, J.L. and Dinman, J.D. (2004) Systematic analysis of bicistronic reporter assay data. Nucleic Acids Res., 32, e160.
    • (2004) Nucleic Acids Res. , vol.32
    • Jacobs, J.L.1    Dinman, J.D.2
  • 27
    • 0022841695 scopus 로고
    • The cellular level of yeast ribosomal protein L25 is controlled principally by rapid degradation of excess protein
    • elBaradi, T.T., van der Sande, C.A., Mager, W.H., Raue, H.A. and Planta, R.J. (1986) The cellular level of yeast ribosomal protein L25 is controlled principally by rapid degradation of excess protein. Curr. Genet., 10, 733-739.
    • (1986) Curr. Genet. , vol.10 , pp. 733-739
    • elBaradi, T.T.1    van der Sande, C.A.2    Mager, W.H.3    Raue, H.A.4    Planta, R.J.5
  • 28
    • 0023757899 scopus 로고
    • The accumulation of three yeast ribosomal proteins under conditions of excess mRNA is determined primarily by fast protein decay
    • Maicas, E., Pluthero, F.G. and Friesen, J.D. (1988) The accumulation of three yeast ribosomal proteins under conditions of excess mRNA is determined primarily by fast protein decay. Mol. Cell Biol., 8, 169-175.
    • (1988) Mol. Cell Biol. , vol.8 , pp. 169-175
    • Maicas, E.1    Pluthero, F.G.2    Friesen, J.D.3
  • 29
    • 0024024935 scopus 로고
    • Ribosomal protein synthesis is not regulated at the translational level in Saccharomyces cerevisiae: balanced accumulation of ribosomal proteins L16 and rp59 is mediated by turnover of excess protein
    • Tsay, Y.F., Thompson, J.R., Rotenberg, M.O., Larkin, J.C. and Woolford, J.L. Jr (1988) Ribosomal protein synthesis is not regulated at the translational level in Saccharomyces cerevisiae: balanced accumulation of ribosomal proteins L16 and rp59 is mediated by turnover of excess protein. Genes Dev., 6, 664-676.
    • (1988) Genes Dev. , vol.6 , pp. 664-676
    • Tsay, Y.F.1    Thompson, J.R.2    Rotenberg, M.O.3    Larkin, J.C.4    Woolford J.L., Jr.5
  • 30
  • 31
    • 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. and Warner, J.R. (1997) 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) Mol. Cell. Biol. , vol.17 , pp. 1959-1965
    • Vilardell, J.1    Warner, J.R.2
  • 34
    • 26944450063 scopus 로고    scopus 로고
    • Roles of eukaryotic ribosomal proteins in maturation and transport of pre-18S rRNA and ribosome function
    • Ferreira-Cerca, S., Pöll, G., Gleizes, P.E., Tschochner, H. and Milkereit, P. (2005) Roles of eukaryotic ribosomal proteins in maturation and transport of pre-18S rRNA and ribosome function. Mol. Cell, 20, 263-275.
    • (2005) Mol. Cell , vol.20 , pp. 263-275
    • Ferreira-Cerca, S.1    Pöll, G.2    Gleizes, P.E.3    Tschochner, H.4    Milkereit, P.5
  • 35
    • 56049089606 scopus 로고    scopus 로고
    • Nuclear export competence of pre-40S subunits in fission yeast requires the ribosomal protein Rps2
    • Perreault, A., Bellemer, C. and Bachand, F. (2008) Nuclear export competence of pre-40S subunits in fission yeast requires the ribosomal protein Rps2. Nucleic Acids Res., 36, 6132-6142.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 6132-6142
    • Perreault, A.1    Bellemer, C.2    Bachand, F.3
  • 36
    • 33748924333 scopus 로고    scopus 로고
    • eIF3: a versatile scaffold for translation initiation complexes
    • Hinnebusch, A.G. (2006) eIF3: a versatile scaffold for translation initiation complexes. Trends Biochem. Sci., 31, 553-562.
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 553-562
    • Hinnebusch, A.G.1
  • 37
    • 0000091608 scopus 로고    scopus 로고
    • The pathway and mechanism of eukaryotic protein synthesis
    • Sonenberg, N., Hershey, J. W. B. and Mathews, M. B. (eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Hershey, J.W.B. and Merrick, W.C. (2000) The pathway and mechanism of eukaryotic protein synthesis. In Sonenberg, N., Hershey, J.W.B. and Mathews, M.B. (eds), Translational Control of Gene Expression. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 33-38.
    • (2000) Translational Control of Gene Expression , pp. 33-38
    • Hershey, J.W.B.1    Merrick, W.C.2
  • 38
    • 34247589630 scopus 로고    scopus 로고
    • The ribosomal peptidyl transferase
    • Beringer, M. and Rodnina, M.V. (2007) The ribosomal peptidyl transferase. Mol. Cell, 26, 311-321.
    • (2007) Mol. Cell , vol.26 , pp. 311-321
    • Beringer, M.1    Rodnina, M.V.2
  • 39
    • 63249107241 scopus 로고    scopus 로고
    • The ribosome returned
    • Moore, P.B. (2009) The ribosome returned. J. Biol., 8, 8.
    • (2009) J. Biol. , vol.8 , pp. 8
    • Moore, P.B.1
  • 40
    • 66049161006 scopus 로고    scopus 로고
    • Recent mechanistic insights into eukaryotic ribosomes
    • Rodnina, M.V. and Wintermeyer, W. (2009) Recent mechanistic insights into eukaryotic ribosomes. Curr. Opin. Cell. Biol., 21, 435-443.
    • (2009) Curr. Opin. Cell. Biol. , vol.21 , pp. 435-443
    • Rodnina, M.V.1    Wintermeyer, W.2
  • 41
    • 33747878071 scopus 로고    scopus 로고
    • Decoding errors and the involvement of the E-site
    • Nierhaus, K.H. (2006) Decoding errors and the involvement of the E-site. Biochimie, 88, 1013-1019.
    • (2006) Biochimie , vol.88 , pp. 1013-1019
    • Nierhaus, K.H.1
  • 42
    • 58149354143 scopus 로고    scopus 로고
    • Quality control by the ribosome following peptide bond formation
    • Zaher, H.S. and Green, R. (2009) Quality control by the ribosome following peptide bond formation. Nature, 457, 161-166.
    • (2009) Nature , vol.457 , pp. 161-166
    • Zaher, H.S.1    Green, R.2
  • 43
    • 28544439977 scopus 로고    scopus 로고
    • Structural roles for human translation factor eIF3 in initiation of protein synthesis
    • Siridechadilok, B., Fraser, C.S., Hall, R.J., Doudna, J.A. and Nogales, E. (2005) Structural roles for human translation factor eIF3 in initiation of protein synthesis. Science, 310, 1513-1515.
    • (2005) Science , vol.310 , pp. 1513-1515
    • Siridechadilok, B.1    Fraser, C.S.2    Hall, R.J.3    Doudna, J.A.4    Nogales, E.5
  • 44
    • 32044467711 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 3 (eIF3) and eIF2 can promote mRNA binding to 40S subunits independently of eIF4G in yeast
    • Jivotovskaya, A.V., Valásek, L., Hinnebusch, A.G. and Nielsen, K.H. (2006) Eukaryotic translation initiation factor 3 (eIF3) and eIF2 can promote mRNA binding to 40S subunits independently of eIF4G in yeast. Mol. Cell. Biol., 26, 1355-1372.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 1355-1372
    • Jivotovskaya, A.V.1    Valásek, L.2    Hinnebusch, A.G.3    Nielsen, K.H.4
  • 45
    • 33644779804 scopus 로고    scopus 로고
    • Specific functional interactions of nucleotides at key -3 and +4 positions flanking the initiation codon with components of the mammalian 48S translation initiation complex
    • Pisarev, A.V., Kolupaeva, V.G., Pisareva, V.P., Merrick, W.C., Hellen, C.U. and Pestova, T.V. (2006) Specific functional interactions of nucleotides at key -3 and +4 positions flanking the initiation codon with components of the mammalian 48S translation initiation complex. Genes Dev., 20, 624-636.
    • (2006) Genes Dev. , vol.20 , pp. 624-636
    • Pisarev, A.V.1    Kolupaeva, V.G.2    Pisareva, V.P.3    Merrick, W.C.4    Hellen, C.U.5    Pestova, T.V.6


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