메뉴 건너뛰기




Volumn 20, Issue 14, 2006, Pages 1959-1973

Drosophila ribosomal proteins are associated with linker histone H1 and suppress gene transcription

Author keywords

Chromatin; Histone H1; L22; Ribosomal protein; Transcription

Indexed keywords

HISTONE H1; INSECT PROTEIN; RIBOSOME PROTEIN;

EID: 33746041435     PISSN: 08909369     EISSN: 15495477     Source Type: Journal    
DOI: 10.1101/gad.390106     Document Type: Article
Times cited : (78)

References (79)
  • 1
    • 0002470839 scopus 로고    scopus 로고
    • Preparation of nuclear and cytoplasmic extracts from mammalian cells
    • (eds. S.J. Enna et al.), Unit 12.3. John WIley & Sons, NY
    • Abmayr, S.M., Carrozza, M.J., and Workman, J.L. 2003. Preparation of nuclear and cytoplasmic extracts from mammalian cells. In Current protocols in pharmacology (eds. S.J. Enna et al.), Unit 12.3. John WIley & Sons, NY.
    • (2003) Current Protocols in Pharmacology
    • Abmayr, S.M.1    Carrozza, M.J.2    Workman, J.L.3
  • 2
    • 0018075458 scopus 로고
    • Does protein synthesis occur within the nucleus? Unambiguous evidence is still needed
    • Allen, W. 1978. Does protein synthesis occur within the nucleus? Unambiguous evidence is still needed. Trends Biol. Sci. 3: N225-N228.
    • (1978) Trends Biol. Sci. , vol.3
    • Allen, W.1
  • 3
    • 2342456308 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay: Terminating erroneous gene expression
    • Baker, K.E. and Parker, R. 2004. Nonsense-mediated mRNA decay: Terminating erroneous gene expression. Curr. Opin. Cell Biol. 16: 293-299.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 293-299
    • Baker, K.E.1    Parker, R.2
  • 4
    • 0033986861 scopus 로고    scopus 로고
    • Histone H1 is dispensable for methylation-associated gene silencing in Ascobolus immersus and essential for long life span
    • Barra, J.L., Rhounim, L., Rossignol, J.L., and Faugeron, G. 2000. Histone H1 is dispensable for methylation-associated gene silencing in Ascobolus immersus and essential for long life span. Mol. Cell. Biol. 20: 61-69.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 61-69
    • Barra, J.L.1    Rhounim, L.2    Rossignol, J.L.3    Faugeron, G.4
  • 5
    • 0037112790 scopus 로고    scopus 로고
    • Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm
    • Bohnsack, M.T., Regener, K., Schwappach, B., Saffrich, R., Paraskeva, E., Hartmann, E., and Gorlich, D. 2002. Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm. EMBO J. 21: 6205-6215.
    • (2002) EMBO J. , vol.21 , pp. 6205-6215
    • Bohnsack, M.T.1    Regener, K.2    Schwappach, B.3    Saffrich, R.4    Paraskeva, E.5    Hartmann, E.6    Gorlich, D.7
  • 6
    • 0021771057 scopus 로고
    • Splicing of Xenopus laevis ribosomal protein RNAs is inhibited in vivo by antisera to ribonucleoproteins containing U1 small nuclear RNA
    • Bozzoni, I., Annesi, F., Beccari, E., Fragapane, P., Pierandrei-Amaldi, P., and Amaldi, F. 1984. Splicing of Xenopus laevis ribosomal protein RNAs is inhibited in vivo by antisera to ribonucleoproteins containing U1 small nuclear RNA. J. Mol. Biol. 180: 1173-1178.
    • (1984) J. Mol. Biol. , vol.180 , pp. 1173-1178
    • Bozzoni, I.1    Annesi, F.2    Beccari, E.3    Fragapane, P.4    Pierandrei-Amaldi, P.5    Amaldi, F.6
  • 7
    • 0036781068 scopus 로고    scopus 로고
    • Ribosome components are associated with sites of transcription
    • Brogna, S., Sato, T.A., and Rosbash, M. 2002. Ribosome components are associated with sites of transcription. Mol. Cell 10: 93-104.
    • (2002) Mol. Cell , vol.10 , pp. 93-104
    • Brogna, S.1    Sato, T.A.2    Rosbash, M.3
  • 8
    • 14644388222 scopus 로고    scopus 로고
    • The dynamics of histone H1 function in chromatin
    • Bustin, M. 2005. The dynamics of histone H1 function in chromatin. Mol. Cell 17: 617-620.
    • (2005) Mol. Cell , vol.17 , pp. 617-620
    • Bustin, M.1
  • 9
    • 2342640073 scopus 로고    scopus 로고
    • Does protein synthesis occur in the nucleus?
    • Dahlberg, J.E. and Lund, E. 2004. Does protein synthesis occur in the nucleus? Curr. Opin. Cell Biol. 16: 335-338.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 335-338
    • Dahlberg, J.E.1    Lund, E.2
  • 10
    • 0034707668 scopus 로고    scopus 로고
    • Nuclear eukaryotic initiation factor 4E (eIF4E) colocalizes with splicing factors in speckles
    • Dostie, J., Lejbkowicz, F., and Sonenberg, N. 2000. Nuclear eukaryotic initiation factor 4E (eIF4E) colocalizes with splicing factors in speckles. J. Cell Biol. 148: 239-247.
    • (2000) J. Cell Biol. , vol.148 , pp. 239-247
    • Dostie, J.1    Lejbkowicz, F.2    Sonenberg, N.3
  • 11
    • 0037490067 scopus 로고    scopus 로고
    • Suppression of homologous recombination by the Saccharomyces cerevisiae linker histone
    • Downs, J.A., Kosmidou, E., Morgan, A., and Jackson, S.P. 2003. Suppression of homologous recombination by the Saccharomyces cerevisiae linker histone. Mol. Cell 11: 1685-1692.
    • (2003) Mol. Cell , vol.11 , pp. 1685-1692
    • Downs, J.A.1    Kosmidou, E.2    Morgan, A.3    Jackson, S.P.4
  • 12
    • 0037188922 scopus 로고    scopus 로고
    • Yph1p, an ORC-interacting protein: Potential links between cell proliferation control, DNA replication, and ribosome biogenesis
    • Du, Y.C. and Stillman, B. 2002. Yph1p, an ORC-interacting protein: Potential links between cell proliferation control, DNA replication, and ribosome biogenesis. Cell 109: 835-848.
    • (2002) Cell , vol.109 , pp. 835-848
    • Du, Y.C.1    Stillman, B.2
  • 15
    • 0032939495 scopus 로고    scopus 로고
    • Ribosomal protein S14 of Saccharomyces cerevisiae regulates its expression by binding to RPS14B pre-mRNA and to 18S rRNA
    • Fewell, S.W. and Woolford Jr., J.L. 1999. Ribosomal protein S14 of Saccharomyces cerevisiae regulates its expression by binding to RPS14B pre-mRNA and to 18S rRNA. Mol. Cell. Biol. 19: 826-834.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 826-834
    • Fewell, S.W.1    Woolford Jr., J.L.2
  • 17
    • 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
  • 18
    • 0018075458 scopus 로고
    • Does protein synthesis occur within the nucleus? Good evidence that it does
    • Goidl, J.A. 1978. Does protein synthesis occur within the nucleus? Good evidence that it does. Trends Biochem. Sci. 3: N225-N228.
    • (1978) Trends Biochem. Sci. , vol.3
    • Goidl, J.A.1
  • 19
    • 0000253250 scopus 로고
    • On the question of protein synthesis by cell nuclei
    • eds. D.M. Prescott et al. Appleton-Century-Crofts, New York
    • Goldstein, L. 1970. On the question of protein synthesis by cell nuclei. In Advances in cell biology (eds. D.M. Prescott et al.), Vol. 1, pp. 187-210. Appleton-Century-Crofts, New York.
    • (1970) Advances in Cell Biology , vol.1 , pp. 187-210
    • Goldstein, L.1
  • 20
    • 0035793640 scopus 로고    scopus 로고
    • Core histone acetylation is regulated by linker histone stoichiometry in vivo
    • Gunjan, A., Sittman, D.B., and Brown, D.T. 2001. Core histone acetylation is regulated by linker histone stoichiometry in vivo. J. Biol. Chem. 276: 3635-3640.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3635-3640
    • Gunjan, A.1    Sittman, D.B.2    Brown, D.T.3
  • 21
    • 33746038201 scopus 로고    scopus 로고
    • Staining cells
    • eds. E.D. Harlow and D. Lane. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Harlow, E.D. and Lane, D. 1999. Staining cells. In Using antibodies (eds. E.D. Harlow and D. Lane), pp. 103-149. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1999) Using Antibodies , pp. 103-149
    • Harlow, E.D.1    Lane, D.2
  • 22
    • 0033975839 scopus 로고    scopus 로고
    • Histone H1 is a specific repressor of core histone acetylation in chromatin
    • Herrera, J.E., West, K.L., Schiltz, R.L., Nakatani, Y., and Bustin, M. 2000. Histone H1 is a specific repressor of core histone acetylation in chromatin. Mol. Cell. Biol. 20: 523-529.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 523-529
    • Herrera, J.E.1    West, K.L.2    Schiltz, R.L.3    Nakatani, Y.4    Bustin, M.5
  • 23
    • 0035958006 scopus 로고    scopus 로고
    • Decreased expression of specific genes in yeast cells lacking histone H1
    • Hellauer, K., Sirard, E., and Turcotte, B. 2001. Decreased expression of specific genes in yeast cells lacking histone H1. J. Biol. Chem. 276: 13587-13592.
    • (2001) J. Biol. Chem. , vol.276 , pp. 13587-13592
    • Hellauer, K.1    Sirard, E.2    Turcotte, B.3
  • 24
    • 0025764058 scopus 로고
    • Histone-DNA interactions and their modulation by phosphorylation of -Ser-Pro-X-Lys/Arg- motifs
    • Hill, C.S., Rimmer, J.M., Green, B.N., Finch, J.T., and Thomas, J.O. 1991. Histone-DNA interactions and their modulation by phosphorylation of -Ser-Pro-X-Lys/Arg- motifs. EMBO J. 10: 1939-1948.
    • (1991) EMBO J. , vol.10 , pp. 1939-1948
    • Hill, C.S.1    Rimmer, J.M.2    Green, B.N.3    Finch, J.T.4    Thomas, J.O.5
  • 25
    • 0033375911 scopus 로고    scopus 로고
    • Mechanisms of mRNA surveillance in eukaryotes
    • Hilleren, P. and Parker, R. 1999. Mechanisms of mRNA surveillance in eukaryotes. Annu. Rev. Genet. 33: 229-260.
    • (1999) Annu. Rev. Genet. , vol.33 , pp. 229-260
    • Hilleren, P.1    Parker, R.2
  • 26
    • 0035839002 scopus 로고    scopus 로고
    • Coupled transcription and translation within nuclei of mammalian cells
    • Iborra, F.J., Jackson, D.A., and Cook, P.R. 2001. Coupled transcription and translation within nuclei of mammalian cells. Science 293: 1139-1142.
    • (2001) Science , vol.293 , pp. 1139-1142
    • Iborra, F.J.1    Jackson, D.A.2    Cook, P.R.3
  • 27
    • 13444251381 scopus 로고    scopus 로고
    • Human ribosomal protein S26 suppresses the splicing of its premRNA
    • Ivanov, A.V., Malygin, A.A., and Karpova, G.G. 2005. Human ribosomal protein S26 suppresses the splicing of its premRNA. Biochim. Biophys. Acta 1727: 134-140.
    • (2005) Biochim. Biophys. Acta , vol.1727 , pp. 134-140
    • Ivanov, A.V.1    Malygin, A.A.2    Karpova, G.G.3
  • 28
    • 0037965571 scopus 로고    scopus 로고
    • Telomeric position effect variegation in Saccharomyces cerevisiae by Caenorhabditis elegans linker histones suggests a mechanistic connection between germ line and telomeric silencing
    • Jedrusik, M.A. and Schulze, E. 2003. Telomeric position effect variegation in Saccharomyces cerevisiae by Caenorhabditis elegans linker histones suggests a mechanistic connection between germ line and telomeric silencing. Mol. Cell. Biol. 23: 3681-3691.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3681-3691
    • Jedrusik, M.A.1    Schulze, E.2
  • 29
    • 0037716756 scopus 로고    scopus 로고
    • Early formation of mRNP: License for export or quality control?
    • Jensen, T.H., Dower, K., Libri, D., and Rosbash, M. 2003. Early formation of mRNP: License for export or quality control? Mol. Cell 11: 1129-1138.
    • (2003) Mol. Cell , vol.11 , pp. 1129-1138
    • Jensen, T.H.1    Dower, K.2    Libri, D.3    Rosbash, M.4
  • 30
    • 0031022333 scopus 로고    scopus 로고
    • H1-mediated repression of transcription factor binding to a stably positioned nucleosome
    • Juan, L.J., Utley, R.T., Vignali, M., Bohm, L., and Workman, J.L. 1997. H1-mediated repression of transcription factor binding to a stably positioned nucleosome. J. Biol. Chem. 272: 3635-3640.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3635-3640
    • Juan, L.J.1    Utley, R.T.2    Vignali, M.3    Bohm, L.4    Workman, J.L.5
  • 32
    • 0033153348 scopus 로고    scopus 로고
    • RNP complexes: Composition, structure, and function
    • Krecic, A.M. and Swanson, M.S. 1999. hnRNP complexes: Composition, structure, and function. Curr. Opin. Cell Biol. 11: 363-371.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 363-371
    • Krecic, A.M.1    Swanson, M.S.2
  • 33
    • 0033509092 scopus 로고    scopus 로고
    • Protein transacting factors involved in ribosome biogenesis in Saccharomyces cerevisiae
    • Kressler, D., Linder, P., and De La Cruz, J. 1999. Protein transacting 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
  • 34
    • 9344248397 scopus 로고    scopus 로고
    • Nonsense-mediated decay does not occur within the yeast nucleus
    • Kuperwasser, N., Brogna, S., Dower, K., and Rosbash, M. 2004. Nonsense-mediated decay does not occur within the yeast nucleus. RNA 10: 1907-1915.
    • (2004) RNA , vol.10 , pp. 1907-1915
    • Kuperwasser, N.1    Brogna, S.2    Dower, K.3    Rosbash, M.4
  • 35
    • 0026095663 scopus 로고
    • Role of nucleosomal cores and histone H1 in regulation of transcription by RNA polymerase II
    • Laybourn, P.J. and Kadonaga, J.T. 1991. Role of nucleosomal cores and histone H1 in regulation of transcription by RNA polymerase II. Science 254: 238-245.
    • (1991) Science , vol.254 , pp. 238-245
    • Laybourn, P.J.1    Kadonaga, J.T.2
  • 36
    • 2942696668 scopus 로고    scopus 로고
    • MSX1 cooperates with histone H1b for inhibition of transcription and myogenesis
    • Lee, H., Habas, R., and Abate-Shen, C. 2004. MSX1 cooperates with histone H1b for inhibition of transcription and myogenesis. Science 304: 1675-1678.
    • (2004) Science , vol.304 , pp. 1675-1678
    • Lee, H.1    Habas, R.2    Abate-Shen, C.3
  • 37
    • 0026705268 scopus 로고
    • A fraction of the mRNA 5′ cap-binding protein, eukaryotic initiation factor 4E, localizes to the nucleus
    • Lejbkowicz, F., Goyer, C., Darveau, A., Neron, S., Lemieux, R., and Sonenberg, N. 1992. A fraction of the mRNA 5′ cap-binding protein, eukaryotic initiation factor 4E, localizes to the nucleus. Proc. Natl. Acad. Sci. 89: 9612-9616.
    • (1992) Proc. Natl. Acad. Sci. , vol.89 , pp. 9612-9616
    • Lejbkowicz, F.1    Goyer, C.2    Darveau, A.3    Neron, S.4    Lemieux, R.5    Sonenberg, N.6
  • 38
    • 0027220589 scopus 로고
    • Protein traffic on the heat shock promoter: Parking, stalling, and trucking along
    • Lis, J. and Wu, C. 1993. Protein traffic on the heat shock promoter: Parking, stalling, and trucking along. Cell 74: 1-4.
    • (1993) Cell , vol.74 , pp. 1-4
    • Lis, J.1    Wu, C.2
  • 39
    • 0037381213 scopus 로고    scopus 로고
    • Structure and dynamic behavior of nucleosomes
    • Luger, K. 2003. Structure and dynamic behavior of nucleosomes. Curr. Opin. Genet. Dev. 13: 127-135.
    • (2003) Curr. Opin. Genet. Dev. , vol.13 , pp. 127-135
    • Luger, K.1
  • 40
    • 0032509304 scopus 로고    scopus 로고
    • Proofreading and aminoacylation of tRNAs before export from the nucleus
    • Lund, E. and Dahlberg, J.E. 1998. Proofreading and aminoacylation of tRNAs before export from the nucleus. Science 282: 2082-2085.
    • (1998) Science , vol.282 , pp. 2082-2085
    • Lund, E.1    Dahlberg, J.E.2
  • 41
    • 0035125142 scopus 로고    scopus 로고
    • mRNA quality control: Marking the message for life or death
    • Lykke-Andersen, J. 2001. mRNA quality control: Marking the message for life or death. Curr. Biol. 11: R88-R91.
    • (2001) Curr. Biol. , vol.11
    • Lykke-Andersen, J.1
  • 42
    • 0037041395 scopus 로고    scopus 로고
    • An extensive network of coupling among gene expression machines
    • Maniatis, T. and Reed, R. 2002. An extensive network of coupling among gene expression machines. Nature 416: 499-506.
    • (2002) Nature , vol.416 , pp. 499-506
    • Maniatis, T.1    Reed, R.2
  • 43
    • 0029330286 scopus 로고
    • When cells stop making sense: Effects of nonsense codons on RNA metabolism in vertebrate cells
    • Maquat, L.E. 1995. When cells stop making sense: Effects of nonsense codons on RNA metabolism in vertebrate cells. RNA 1: 453-465.
    • (1995) RNA , vol.1 , pp. 453-465
    • Maquat, L.E.1
  • 44
    • 0027416787 scopus 로고
    • Association of individual hnRNP proteins and snRNPs with nascent transcripts
    • Matunis, E.L., Matunis, M.J., and Dreyfuss, G. 1993. Association of individual hnRNP proteins and snRNPs with nascent transcripts. J. Cell Biol. 121: 219-228.
    • (1993) J. Cell Biol. , vol.121 , pp. 219-228
    • Matunis, E.L.1    Matunis, M.J.2    Dreyfuss, G.3
  • 46
    • 0034649663 scopus 로고    scopus 로고
    • Dynamic binding of histone H1 to chromatin in living cells
    • Misteli, T., Gunjan, A., Hock, R., Bustin, M., and Brown, D.T. 2000. Dynamic binding of histone H1 to chromatin in living cells. Nature 408: 877-881.
    • (2000) Nature , vol.408 , pp. 877-881
    • Misteli, T.1    Gunjan, A.2    Hock, R.3    Bustin, M.4    Brown, D.T.5
  • 48
    • 0027183945 scopus 로고
    • The 3;21 translocation in myelodysplasia results in a fusion transcript between the AML1 gene and the gene for EAP, a highly conserved protein associated with the Epstein-Barr virus small RNA EBER 1
    • Nucifora, G., Begy, C.R., Erickson, P., Drabkin, H.A., and Rowley, J.D. 1993. The 3;21 translocation in myelodysplasia results in a fusion transcript between the AML1 gene and the gene for EAP, a highly conserved protein associated with the Epstein-Barr virus small RNA EBER 1. Proc. Natl. Acad. Sci. 90: 7784-7788.
    • (1993) Proc. Natl. Acad. Sci. , vol.90 , pp. 7784-7788
    • Nucifora, G.1    Begy, C.R.2    Erickson, P.3    Drabkin, H.A.4    Rowley, J.D.5
  • 49
    • 0025053965 scopus 로고
    • The ultrastructure of imaginal disc cells in primary cultures and during cell aggregation in continuous cell lines
    • Peel, D.J., Johnson, S.A., and Milner, M.J. 1990. The ultrastructure of imaginal disc cells in primary cultures and during cell aggregation in continuous cell lines. Tissue Cell 22: 749-758.
    • (1990) Tissue Cell , vol.22 , pp. 749-758
    • Peel, D.J.1    Johnson, S.A.2    Milner, M.J.3
  • 50
    • 0031878107 scopus 로고    scopus 로고
    • The host gene for intronic U17 small nucleolar RNAs in mammals has no protein-coding potential and is a member of the 5-terminal oligopyrimidine gene family
    • Pelczar, P. and Filipowicz, W. 1998. The host gene for intronic U17 small nucleolar RNAs in mammals has no protein-coding potential and is a member of the 5-terminal oligopyrimidine gene family. Mol. Cell. Biol. 18: 4509-4518.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4509-4518
    • Pelczar, P.1    Filipowicz, W.2
  • 51
    • 0028130301 scopus 로고
    • Linker histones H1 and H5 prevent the mobility of positioned nucleosomes
    • Pennings, S., Meersseman, G., and Bradbury, E.M. 1994. Linker histones H1 and H5 prevent the mobility of positioned nucleosomes. Proc. Natl. Acad. Sci. 91: 10275-10279.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 10275-10279
    • Pennings, S.1    Meersseman, G.2    Bradbury, E.M.3
  • 52
    • 0028791330 scopus 로고
    • Mechanism of protein access to specific DNA sequences in chromatin: A dynamic equilibrium model for gene regulation
    • Polach, K.J. and Widom, J. 1995. Mechanism of protein access to specific DNA sequences in chromatin: A dynamic equilibrium model for gene regulation. J. Mol. Biol. 254: 130-149.
    • (1995) J. Mol. Biol. , vol.254 , pp. 130-149
    • Polach, K.J.1    Widom, J.2
  • 53
    • 0025770052 scopus 로고
    • The ribosomal protein L2 in S. cerevisiae controls the level of accumulation of its own mRNA
    • Presutti, C., Ciafre, S.A., and Bozzoni, I. 1991. The ribosomal protein L2 in S. cerevisiae controls the level of accumulation of its own mRNA. EMBO J. 10: 2215-2221.
    • (1991) EMBO J. , vol.10 , pp. 2215-2221
    • Presutti, C.1    Ciafre, S.A.2    Bozzoni, I.3
  • 54
    • 0014827830 scopus 로고
    • Evidence for transport of preribosomal RNA from the nucleolus to the chromosomes in Chironomus tentans salivary gland cells
    • Ringborg, U., Daneholt, B., Edstrom, J.E., Egyhazi, E., and Rydlander, L. 1970. Evidence for transport of preribosomal RNA from the nucleolus to the chromosomes in Chironomus tentans salivary gland cells. J. Mol. Biol. 51: 679-686.
    • (1970) J. Mol. Biol. , vol.51 , pp. 679-686
    • Ringborg, U.1    Daneholt, B.2    Edstrom, J.E.3    Egyhazi, E.4    Rydlander, L.5
  • 55
    • 0029951860 scopus 로고    scopus 로고
    • Immunofluorescence studies of human fibroblasts demonstrate the presence of the complex of elongation factor-1 βγδ in the endoplasmic reticulum
    • Sanders, J., Brandsma, M., Janssen, G.M., Dijk, J., and Moller, W. 1996. Immunofluorescence studies of human fibroblasts demonstrate the presence of the complex of elongation factor-1 βγδ in the endoplasmic reticulum. J. Cell Sci. 109: 1113-1117.
    • (1996) J. Cell Sci. , vol.109 , pp. 1113-1117
    • Sanders, J.1    Brandsma, M.2    Janssen, G.M.3    Dijk, J.4    Moller, W.5
  • 56
    • 0035960726 scopus 로고    scopus 로고
    • A yeast homolog of chromatin assembly factor 1 is involved in early ribosome assembly
    • Schaper, S., Fromont-Racine, M., Linder, P., de la Cruz, J., Namane, A., and Yaniv, M. 2001. A yeast homolog of chromatin assembly factor 1 is involved in early ribosome assembly. Curr. Biol. 11: 1885-1890.
    • (2001) Curr. Biol. , vol.11 , pp. 1885-1890
    • Schaper, S.1    Fromont-Racine, M.2    Linder, P.3    De La Cruz, J.4    Namane, A.5    Yaniv, M.6
  • 57
    • 0036204810 scopus 로고    scopus 로고
    • Integration of splicing, transport and translation to achieve mRNA quality control by the nonsense-mediated decay pathway
    • REVIEWS1006
    • Schell, T., Kulozik, A.E., and Hentze, M.W. 2002. Integration of splicing, transport and translation to achieve mRNA quality control by the nonsense-mediated decay pathway. Genome Biol. 3: REVIEWS1006.
    • (2002) Genome Biol. , vol.3
    • Schell, T.1    Kulozik, A.E.2    Hentze, M.W.3
  • 58
    • 25844434760 scopus 로고    scopus 로고
    • Association of ribosomal proteins with nascent transcripts in S. cerevisiae
    • Schroder, P.A. and Moore, M.J. 2005. Association of ribosomal proteins with nascent transcripts in S. cerevisiae. RNA 11: 1521-1529.
    • (2005) RNA , vol.11 , pp. 1521-1529
    • Schroder, P.A.1    Moore, M.J.2
  • 59
    • 0030576509 scopus 로고    scopus 로고
    • Linker histone H1 regulates specific gene expression but not global transcription in vivo
    • Shen, X. and Gorovsky, M.A. 1996. Linker histone H1 regulates specific gene expression but not global transcription in vivo. Cell 86: 475-483.
    • (1996) Cell , vol.86 , pp. 475-483
    • Shen, X.1    Gorovsky, M.A.2
  • 60
    • 0033730418 scopus 로고    scopus 로고
    • Factors affecting nuclear export of the 60S ribosomal subunit in vivo
    • Stage-Zimmermann, T., Schmidt, U., and Silver, P.A. 2000. Factors affecting nuclear export of the 60S ribosomal subunit in vivo. Mol. Biol. Cell 11: 3777-3789.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3777-3789
    • Stage-Zimmermann, T.1    Schmidt, U.2    Silver, P.A.3
  • 61
    • 0030824599 scopus 로고    scopus 로고
    • Somatic linker histones cause loss of mesodermal competence in Xenopus
    • Steinbach, O.C., Wolffe, A.P., and Rupp, R.A. 1997. Somatic linker histones cause loss of mesodermal competence in Xenopus. Nature 389: 395-399.
    • (1997) Nature , vol.389 , pp. 395-399
    • Steinbach, O.C.1    Wolffe, A.P.2    Rupp, R.A.3
  • 62
    • 0028949203 scopus 로고
    • Regulation of human RPS14 transcription by intronic antisense RNAs and ribosomal protein S14
    • Tasheva, E.S. and Roufa, D.J. 1995. Regulation of human RPS14 transcription by intronic antisense RNAs and ribosomal protein S14. Genes & Dev. 9: 304-316.
    • (1995) Genes & Dev. , vol.9 , pp. 304-316
    • Tasheva, E.S.1    Roufa, D.J.2
  • 63
    • 0033151772 scopus 로고    scopus 로고
    • Histone H1: Location and role
    • Thomas, J.O. 1999. Histone H1: Location and role. Curr. Opin. Cell Biol. 11: 312-317.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 312-317
    • Thomas, J.O.1
  • 64
    • 0026021681 scopus 로고
    • EAP, a highly conserved cellular protein associated with Epstein-Barr virus small RNAs (EBERs)
    • Toczyski, D.P. and Steitz, J.A. 1991. EAP, a highly conserved cellular protein associated with Epstein-Barr virus small RNAs (EBERs). EMBO J. 10: 459-466.
    • (1991) EMBO J. , vol.10 , pp. 459-466
    • Toczyski, D.P.1    Steitz, J.A.2
  • 65
    • 0022129510 scopus 로고
    • Sequences required for in vitro transcriptional activation of a Drosophila hsp 70 gene
    • Topol, J., Ruden, D.M., and Parker, C.S. 1985. Sequences required for in vitro transcriptional activation of a Drosophila hsp 70 gene. Cell 42: 527-537.
    • (1985) Cell , vol.42 , pp. 527-537
    • Topol, J.1    Ruden, D.M.2    Parker, C.S.3
  • 66
    • 0028200980 scopus 로고
    • Localization of Saccharomyces cerevisiae ribosomal protein L16 on the surface of 60 S ribosomal subunits by immunoelectron microscopy
    • Tsay, Y.F., Shankweiler, G., Lake, J., and Woolford Jr., J.L. 1994. Localization of Saccharomyces cerevisiae ribosomal protein L16 on the surface of 60 S ribosomal subunits by immunoelectron microscopy. J. Biol. Chem. 269: 7579-7586.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7579-7586
    • Tsay, Y.F.1    Shankweiler, G.2    Lake, J.3    Woolford Jr., J.L.4
  • 67
    • 4944245398 scopus 로고    scopus 로고
    • Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin
    • Vaquero, A., Scher, M., Lee, D., Erdjument-Bromage, H., Tempst, P., and Reinberg, D. 2004. Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin. Mol. Cell 16: 93-105.
    • (2004) Mol. Cell , vol.16 , pp. 93-105
    • Vaquero, A.1    Scher, M.2    Lee, D.3    Erdjument-Bromage, H.4    Tempst, P.5    Reinberg, D.6
  • 68
    • 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
  • 69
    • 0031790607 scopus 로고    scopus 로고
    • Location and function of linker histones
    • Vignali, M. and Workman, J.L. 1998. Location and function of linker histones. Nat. Struct. Biol. 5: 1025-1028.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1025-1028
    • Vignali, M.1    Workman, J.L.2
  • 71
    • 0036677083 scopus 로고    scopus 로고
    • mRNA surveillance: The perfect persist
    • Wagner, E. and Lykke-Andersen, J. 2002. mRNA surveillance: The perfect persist. J. Cell Sci. 115: 3033-3038.
    • (2002) J. Cell Sci. , vol.115 , pp. 3033-3038
    • Wagner, E.1    Lykke-Andersen, J.2
  • 72
    • 0036300610 scopus 로고    scopus 로고
    • RNA surveillance by nuclear scanning?
    • Wilkinson, M.F. and Shyu, A.B. 2002. RNA surveillance by nuclear scanning? Nat. Cell Biol. 4: E144-E147.
    • (2002) Nat. Cell Biol. , vol.4
    • Wilkinson, M.F.1    Shyu, A.B.2
  • 73
    • 0035498978 scopus 로고    scopus 로고
    • Curbing the nonsense: The activation and regulation of mRNA surveillance
    • Wilusz, C.J., Wang, W., and Peltz, S.W. 2001. Curbing the nonsense: The activation and regulation of mRNA surveillance. Genes & Dev. 15: 2781-2785.
    • (2001) Genes & Dev. , vol.15 , pp. 2781-2785
    • Wilusz, C.J.1    Wang, W.2    Peltz, S.W.3
  • 75
    • 0029974453 scopus 로고    scopus 로고
    • Extraribosomal functions of ribosomal proteins
    • Wool, I.G. 1996. Extraribosomal functions of ribosomal proteins. Trends Biochem. Sci. 21: 164-165.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 164-165
    • Wool, I.G.1
  • 76
    • 0026297939 scopus 로고
    • The structure and biogenesis of yeast ribosomes
    • Woolford Jr., J.L. 1991. The structure and biogenesis of yeast ribosomes. Adv. Genet. 29: 63-118.
    • (1991) Adv. Genet. , vol.29 , pp. 63-118
    • Woolford Jr., J.L.1
  • 77
    • 0031707751 scopus 로고    scopus 로고
    • Alteration of nucleosome structure as a mechanism of transcriptional regulation
    • Workman, J.L. and Kingston, R.E. 1998. Alteration of nucleosome structure as a mechanism of transcriptional regulation. Annu. Rev. Biochem. 67: 545-579.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 545-579
    • Workman, J.L.1    Kingston, R.E.2
  • 78
    • 0035883954 scopus 로고    scopus 로고
    • Transcription regulation by histone methylation: Interplay between different covalent modifications of the core histone tails
    • Zhang, Y. and Reinberg, D. 2001. Transcription regulation by histone methylation: Interplay between different covalent modifications of the core histone tails. Genes & Dev. 15: 2343-2360.
    • (2001) Genes & Dev. , vol.15 , pp. 2343-2360
    • Zhang, Y.1    Reinberg, D.2
  • 79
    • 0027082560 scopus 로고
    • Histone H1 and transcription: Still an enigma?
    • Zlatanova, J. and Van Holde, K. 1992. Histone H1 and transcription: Still an enigma? J. Cell Sci. 103: 889-895.
    • (1992) J. Cell Sci. , vol.103 , pp. 889-895
    • Zlatanova, J.1    Van Holde, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.