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Volumn 22, Issue 1, 2008, Pages 50-65

Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5′ to 3′ and 3′ to 5′

Author keywords

Cell cycle; Decapping; Exosome; Histone; mRNA stability; Oligouridylation

Indexed keywords

HISTONE; MESSENGER RNA; URIDINE;

EID: 38149023239     PISSN: 08909369     EISSN: 15495477     Source Type: Journal    
DOI: 10.1101/gad.1622708     Document Type: Article
Times cited : (279)

References (67)
  • 1
    • 0033567131 scopus 로고    scopus 로고
    • The yeast exosome and human PM-Scl are related complexes of 3′ → 5′ exonucleases
    • Allmang, C., Petfalski, E., Podtelejnikov, A., Mann, M., Tollervey, D., and Mitchell, P. 1999. The yeast exosome and human PM-Scl are related complexes of 3′ → 5′ exonucleases. Genes & Dev. 13: 2148-2158.
    • (1999) Genes & Dev , vol.13 , pp. 2148-2158
    • Allmang, C.1    Petfalski, E.2    Podtelejnikov, A.3    Mann, M.4    Tollervey, D.5    Mitchell, P.6
  • 2
    • 8544253956 scopus 로고    scopus 로고
    • A faux 3′-UTR promotes aberrant termination and triggers nonsense-mediated mRNA decay
    • Amrani, N., Ganesan, R., Kervestin, S., Mangus, D.A., Ghosh, S., and Jacobson, A. 2004. A faux 3′-UTR promotes aberrant termination and triggers nonsense-mediated mRNA decay. Nature 432: 112-118.
    • (2004) Nature , vol.432 , pp. 112-118
    • Amrani, N.1    Ganesan, R.2    Kervestin, S.3    Mangus, D.A.4    Ghosh, S.5    Jacobson, A.6
  • 3
    • 0033548140 scopus 로고    scopus 로고
    • Polyadenylation promotes degradation of 3′-structured RNA by the Escherichia coli mRNA degradosome in vitro
    • Blum, E., Carpousis, A.J., and Higgins, C.F. 1999. Polyadenylation promotes degradation of 3′-structured RNA by the Escherichia coli mRNA degradosome in vitro. J. Biol. Chem. 274: 4009-4016.
    • (1999) J. Biol. Chem , vol.274 , pp. 4009-4016
    • Blum, E.1    Carpousis, A.J.2    Higgins, C.F.3
  • 4
    • 38549117402 scopus 로고    scopus 로고
    • SLIP1, a factor required for activation of histone mRNA translation by the stem-loop binding protein
    • doi:10.1128/MCB.01500- 07
    • Cakmakci, N.G., Lerner, R.S., Wagner, E.J., Zheng, L.-X., and Marzluff, W.F. 2007. SLIP1, a factor required for activation of histone mRNA translation by the stem-loop binding protein. Mol. Cell. Biol. doi:10.1128/MCB.01500- 07.
    • (2007) Mol. Cell. Biol
    • Cakmakci, N.G.1    Lerner, R.S.2    Wagner, E.J.3    Zheng, L.-X.4    Marzluff, W.F.5
  • 5
    • 0029871812 scopus 로고    scopus 로고
    • Mechanisms and control of mRNA turnover in Saccharomyces cerevisiae
    • Caponigro, G. and Parker, R. 1996. Mechanisms and control of mRNA turnover in Saccharomyces cerevisiae. Microbiol. Rev. 60: 233-249.
    • (1996) Microbiol. Rev , vol.60 , pp. 233-249
    • Caponigro, G.1    Parker, R.2
  • 6
    • 25144482816 scopus 로고    scopus 로고
    • General translational repression by activators of mRNA decapping
    • Coller, J. and Parker, R. 2005. General translational repression by activators of mRNA decapping. Cell 122: 875-886.
    • (2005) Cell , vol.122 , pp. 875-886
    • Coller, J.1    Parker, R.2
  • 7
    • 0035674477 scopus 로고    scopus 로고
    • The DEAD box helicase, Dhh1p, functions in mRNA decapping and interacts with both the decapping and deadenylase complexes
    • Coller, J.M., Tucker, M., Sheth, U., Valencia-Sanchez, M.A., and Parker, R. 2001. The DEAD box helicase, Dhh1p, functions in mRNA decapping and interacts with both the decapping and deadenylase complexes. RNA 7: 1717-1727.
    • (2001) RNA , vol.7 , pp. 1717-1727
    • Coller, J.M.1    Tucker, M.2    Sheth, U.3    Valencia-Sanchez, M.A.4    Parker, R.5
  • 9
    • 0141888419 scopus 로고    scopus 로고
    • A 3′ exonuclease that specifically interacts with the 3′ end of histone mRNA
    • Dominski, Z., Yang, X., Kaygun, H., and Marzluff, W.F. 2003. A 3′ exonuclease that specifically interacts with the 3′ end of histone mRNA. Mol. Cell 12: 295-305.
    • (2003) Mol. Cell , vol.12 , pp. 295-305
    • Dominski, Z.1    Yang, X.2    Kaygun, H.3    Marzluff, W.F.4
  • 10
    • 26244452759 scopus 로고    scopus 로고
    • The polyadenylation factor CPSF-73 is involved in histone pre-mRNA processing
    • Dominski, Z., Yang, X.C., and Marzluff, W.F. 2005. The polyadenylation factor CPSF-73 is involved in histone pre-mRNA processing. Cell 123: 37-48.
    • (2005) Cell , vol.123 , pp. 37-48
    • Dominski, Z.1    Yang, X.C.2    Marzluff, W.F.3
  • 11
    • 19644372547 scopus 로고    scopus 로고
    • Nuclear import of the stem-loop binding protein and localization during the cell cycle
    • Erkmann, J.A., Wagner, E.J., Dong, J., Zhang, Y.P., Kutay, U., and Marzluff, W.F. 2005. Nuclear import of the stem-loop binding protein and localization during the cell cycle. Mol. Biol. Cell 16: 2960-2971.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2960-2971
    • Erkmann, J.A.1    Wagner, E.J.2    Dong, J.3    Zhang, Y.P.4    Kutay, U.5    Marzluff, W.F.6
  • 12
    • 0141856112 scopus 로고    scopus 로고
    • The GW182 protein colocalizes with mRNA degradation associated proteins hDcp1 and hLSm4 in cytoplasmic GW bodies
    • Eystathioy, T., Jakymiw, A., Chan, E.K., Seraphin, B., Cougot, N., and Fritzler, M.J. 2003. The GW182 protein colocalizes with mRNA degradation associated proteins hDcp1 and hLSm4 in cytoplasmic GW bodies. RNA 9: 1171-1173.
    • (2003) RNA , vol.9 , pp. 1171-1173
    • Eystathioy, T.1    Jakymiw, A.2    Chan, E.K.3    Seraphin, B.4    Cougot, N.5    Fritzler, M.J.6
  • 13
    • 0027190530 scopus 로고
    • A highly sensitive method for mapping the 5′ termini of mRNAs
    • Fromont-Racine, M., Bertrand, E., Pictet, R., and Grange, T. 1993. A highly sensitive method for mapping the 5′ termini of mRNAs. Nucleic Acids Res. 21: 1683-1684.
    • (1993) Nucleic Acids Res , vol.21 , pp. 1683-1684
    • Fromont-Racine, M.1    Bertrand, E.2    Pictet, R.3    Grange, T.4
  • 15
    • 2942595765 scopus 로고    scopus 로고
    • Nonsense-mediated messenger RNA decay is initiated by endonucleolytic cleavage in Drosophila
    • Gatfield, D. and Izaurralde, E. 2004. Nonsense-mediated messenger RNA decay is initiated by endonucleolytic cleavage in Drosophila. Nature 429: 575-578.
    • (2004) Nature , vol.429 , pp. 575-578
    • Gatfield, D.1    Izaurralde, E.2
  • 16
    • 0023666085 scopus 로고
    • Translation is required for regulation of histone mRNA degradation
    • Graves, R.A., Pandey, N.B., Chodchoy, N., and Marzluff, W.F. 1987. Translation is required for regulation of histone mRNA degradation. Cell 48: 615-626.
    • (1987) Cell , vol.48 , pp. 615-626
    • Graves, R.A.1    Pandey, N.B.2    Chodchoy, N.3    Marzluff, W.F.4
  • 17
    • 33845957402 scopus 로고    scopus 로고
    • Untemplated oligoadenylation promotes degradation of RISC-cleaved transcripts
    • Ibrahim, F., Rohr, J., Jeong, W.J., Hesson, J., and Cerutti, H. 2006. Untemplated oligoadenylation promotes degradation of RISC-cleaved transcripts. Science 314: 1893.
    • (2006) Science , vol.314 , pp. 1893
    • Ibrahim, F.1    Rohr, J.2    Jeong, W.J.3    Hesson, J.4    Cerutti, H.5
  • 18
    • 26944503146 scopus 로고    scopus 로고
    • Regulated degradation of replication-dependent histone mRNAs requires both ATR and Upf1
    • Kaygun, H. and Marzluff, W.F. 2005a. Regulated degradation of replication-dependent histone mRNAs requires both ATR and Upf1. Nat. Struct. Mol. Biol. 12: 794-800.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 794-800
    • Kaygun, H.1    Marzluff, W.F.2
  • 19
    • 23344452109 scopus 로고    scopus 로고
    • Translation termination is involved in histone mRNA degradation when DNA replication is inhibited
    • Kaygun, H. and Marzluff, W.F. 2005b. Translation termination is involved in histone mRNA degradation when DNA replication is inhibited. Mol. Cell. Biol. 25: 6879-6888.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 6879-6888
    • Kaygun, H.1    Marzluff, W.F.2
  • 20
    • 38149005871 scopus 로고    scopus 로고
    • Upf1 functions in regulation of mammalian histone mRNA decay
    • ed. L.E. Maquat, pp, Landes Bioscience, Georgetown, TX
    • Kaygun, H. and Marzluff, W.F. 2006. Upf1 functions in regulation of mammalian histone mRNA decay. In Nonsense-mediated mRNA decay (ed. L.E. Maquat), pp. 237-252. Landes Bioscience, Georgetown, TX.
    • (2006) Nonsense-mediated mRNA decay , pp. 237-252
    • Kaygun, H.1    Marzluff, W.F.2
  • 21
    • 26944459450 scopus 로고    scopus 로고
    • Symplekin and multiple other polyadenylation factors participate in 3′-end maturation of histone mRNAs
    • Kolev, N.G. and Steitz, J.A. 2005. Symplekin and multiple other polyadenylation factors participate in 3′-end maturation of histone mRNAs. Genes & Dev. 19: 2583-2592.
    • (2005) Genes & Dev , vol.19 , pp. 2583-2592
    • Kolev, N.G.1    Steitz, J.A.2
  • 22
    • 33845264383 scopus 로고    scopus 로고
    • Genetic and biochemical chracterization of Drosophila snipper: A promiscuous member of the metazoan 3′hExo/ERI-1 family of 3′ to 5′ exonucleases
    • Kupsco, J.M., Wu, M.-J., Marzluff, W.F., Thapar, R., and Duronio, R.J. 2006. Genetic and biochemical chracterization of Drosophila snipper: A promiscuous member of the metazoan 3′hExo/ERI-1 family of 3′ to 5′ exonucleases. RNA 12: 2103-2117.
    • (2006) RNA , vol.12 , pp. 2103-2117
    • Kupsco, J.M.1    Wu, M.-J.2    Marzluff, W.F.3    Thapar, R.4    Duronio, R.J.5
  • 23
    • 15244343863 scopus 로고    scopus 로고
    • mRNA decay in prokaryotes and eukaryotes: Different approaches to a similar problem
    • Kushner, S.R. 2004. mRNA decay in prokaryotes and eukaryotes: Different approaches to a similar problem. IUBMB Life 56: 585-594.
    • (2004) IUBMB Life , vol.56 , pp. 585-594
    • Kushner, S.R.1
  • 24
    • 34249026025 scopus 로고    scopus 로고
    • A family of poly(U) polymerases
    • Kwak, J.E. and Wickens, M. 2007. A family of poly(U) polymerases. RNA 13: 860-867.
    • (2007) RNA , vol.13 , pp. 860-867
    • Kwak, J.E.1    Wickens, M.2
  • 27
    • 3543111496 scopus 로고    scopus 로고
    • A protein interaction framework for human mRNA degradation
    • Lehner, B. and Sanderson, C.M. 2004. A protein interaction framework for human mRNA degradation. Genome Res. 14: 1315-1323.
    • (2004) Genome Res , vol.14 , pp. 1315-1323
    • Lehner, B.1    Sanderson, C.M.2
  • 28
    • 0141819096 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities
    • Lejeune, F., Li, X., and Maquat, L.E. 2003. Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities. Mol. Cell 12: 675-687.
    • (2003) Mol. Cell , vol.12 , pp. 675-687
    • Lejeune, F.1    Li, X.2    Maquat, L.E.3
  • 29
    • 33845407784 scopus 로고    scopus 로고
    • Reconstitution, activities, and structure of the eukaryotic RNA exosome
    • Liu, Q., Greimann, J.C., and Lima, C.D. 2006. Reconstitution, activities, and structure of the eukaryotic RNA exosome. Cell 127: 1223-1237.
    • (2006) Cell , vol.127 , pp. 1223-1237
    • Liu, Q.1    Greimann, J.C.2    Lima, C.D.3
  • 30
    • 0038730985 scopus 로고    scopus 로고
    • mRNA decay: X (XRN1) marks the spot
    • Long, R.M. and McNally, M.T. 2003. mRNA decay: X (XRN1) marks the spot. Mol. Cell 11: 1126-1128.
    • (2003) Mol. Cell , vol.11 , pp. 1126-1128
    • Long, R.M.1    McNally, M.T.2
  • 31
    • 0031039529 scopus 로고    scopus 로고
    • The gene for histone RNA hairpin binding protein is located on human chromosome 4 and encodes a novel type of RNA binding protein
    • Martin, F., Schaller, A., Eglite, S., Schümperli, D., and Müller, B. 1997. The gene for histone RNA hairpin binding protein is located on human chromosome 4 and encodes a novel type of RNA binding protein. EMBO J. 16: 769-778.
    • (1997) EMBO J , vol.16 , pp. 769-778
    • Martin, F.1    Schaller, A.2    Eglite, S.3    Schümperli, D.4    Müller, B.5
  • 32
    • 19344366158 scopus 로고    scopus 로고
    • Metazoan replication dependent histone mRNAs: A unique class of RNA polymerase II transcripts
    • Marzluff, W.F. 2005. Metazoan replication dependent histone mRNAs: A unique class of RNA polymerase II transcripts. Curr. Opin. Cell Biol. 17: 274-280.
    • (2005) Curr. Opin. Cell Biol , vol.17 , pp. 274-280
    • Marzluff, W.F.1
  • 33
  • 34
    • 0030702085 scopus 로고    scopus 로고
    • The exosome: A conserved eukaryotic RNA processing complex containing multiple 3′ → 5′ exoribonucleases
    • Mitchell, P., Petfalski, E., Shevchenko, A., Mann, M., and Tollervey, D. 1997. The exosome: A conserved eukaryotic RNA processing complex containing multiple 3′ → 5′ exoribonucleases. Cell 91: 457-466.
    • (1997) Cell , vol.91 , pp. 457-466
    • Mitchell, P.1    Petfalski, E.2    Shevchenko, A.3    Mann, M.4    Tollervey, D.5
  • 35
    • 0034710943 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase functions both as a 3′ → 5′ exonuclease and a poly(A) polymerase in Escherichia coli
    • Mohanty, B.K. and Kushner, S.R. 2000. Polynucleotide phosphorylase functions both as a 3′ → 5′ exonuclease and a poly(A) polymerase in Escherichia coli. Proc. Natl. Acad. Sci. 97: 11966-11971.
    • (2000) Proc. Natl. Acad. Sci , vol.97 , pp. 11966-11971
    • Mohanty, B.K.1    Kushner, S.R.2
  • 36
    • 0037080834 scopus 로고    scopus 로고
    • The mammalian exosome mediates the efficient degradation of mRNAs that contain AU-rich elements
    • Mukherjee, D., Gao, M., O'Connor, J.P., Raijmakers, R., Pruijn, G., Lutz, C.S., and Wilusz, J.R. 2002. The mammalian exosome mediates the efficient degradation of mRNAs that contain AU-rich elements. EMBO J. 21: 165-174.
    • (2002) EMBO J , vol.21 , pp. 165-174
    • Mukherjee, D.1    Gao, M.2    O'Connor, J.P.3    Raijmakers, R.4    Pruijn, G.5    Lutz, C.S.6    Wilusz, J.R.7
  • 37
    • 34147223557 scopus 로고    scopus 로고
    • A + U-rich instability elements differentially activate 5′-3′ and 3′-5′ mRNA decay
    • Murray, E.L. and Schoenberg, D.R. 2007. A + U-rich instability elements differentially activate 5′-3′ and 3′-5′ mRNA decay. Mol. Cell. Biol. 27: 2791-2799.
    • (2007) Mol. Cell. Biol , vol.27 , pp. 2791-2799
    • Murray, E.L.1    Schoenberg, D.R.2
  • 38
    • 21244454028 scopus 로고    scopus 로고
    • Human mitochondrial mRNAs are stabilized with polyadenylation regulated by mitochondria-specific poly(A) polymerase and polynucleotide phosphorylase
    • Nagaike, T., Suzuki, T., Katoh, T., and Ueda, T. 2005. Human mitochondrial mRNAs are stabilized with polyadenylation regulated by mitochondria-specific poly(A) polymerase and polynucleotide phosphorylase. J. Biol. Chem. 280: 19721-19727.
    • (2005) J. Biol. Chem , vol.280 , pp. 19721-19727
    • Nagaike, T.1    Suzuki, T.2    Katoh, T.3    Ueda, T.4
  • 39
    • 34247552158 scopus 로고    scopus 로고
    • NELF interacts with CBC and participates in 3′ end processing of replication-dependent histone mRNAs
    • Narita, T., Yung, T.M., Yamamoto, J., Tsuboi, Y., Tanabe, H., Tanaka, K., Yamaguchi, Y., and Handa, H. 2007. NELF interacts with CBC and participates in 3′ end processing of replication-dependent histone mRNAs. Mol. Cell 26: 349-365.
    • (2007) Mol. Cell , vol.26 , pp. 349-365
    • Narita, T.1    Yung, T.M.2    Yamamoto, J.3    Tsuboi, Y.4    Tanabe, H.5    Tanaka, K.6    Yamaguchi, Y.7    Handa, H.8
  • 40
    • 15444368560 scopus 로고    scopus 로고
    • Decay of mRNAs targeted by RISC requires XRN1, the Ski complex, and the exosome
    • Orban, T.I. and Izaurralde, E. 2005. Decay of mRNAs targeted by RISC requires XRN1, the Ski complex, and the exosome. RNA 11: 459-469.
    • (2005) RNA , vol.11 , pp. 459-469
    • Orban, T.I.1    Izaurralde, E.2
  • 41
    • 0023462745 scopus 로고
    • The stem-loop structure at the 3′ end of histone mRNA is necessary and sufficient for regulation of histone mRNA stability
    • Pandey, N.B. and Marzluff, W.F. 1987. The stem-loop structure at the 3′ end of histone mRNA is necessary and sufficient for regulation of histone mRNA stability. Mol. Cell. Biol. 7: 4557-4559.
    • (1987) Mol. Cell. Biol , vol.7 , pp. 4557-4559
    • Pandey, N.B.1    Marzluff, W.F.2
  • 42
    • 0742288008 scopus 로고    scopus 로고
    • The enzymes and control of eukaryotic mRNA turnover
    • Parker, R. and Song, H. 2004. The enzymes and control of eukaryotic mRNA turnover. Nat. Struct. Mol. Biol. 11: 121-127.
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 121-127
    • Parker, R.1    Song, H.2
  • 43
    • 34248225381 scopus 로고    scopus 로고
    • Efficient RNA polyuridylation by non-canonical poly(A) polymerases
    • Rissland, O.S., Mikulaslova, A., and Norbury, C.J. 2007. Efficient RNA polyuridylation by non-canonical poly(A) polymerases. Mol. Cell. Biol. 27: 3612-3624.
    • (2007) Mol. Cell. Biol , vol.27 , pp. 3612-3624
    • Rissland, O.S.1    Mikulaslova, A.2    Norbury, C.J.3
  • 44
    • 0023053281 scopus 로고
    • H4 histone messenger RNA decay in cell-free extracts initiates at or near the 3′ terminus and proceeds 3′ to 5′
    • Ross, J. and Kobs, G. 1986. H4 histone messenger RNA decay in cell-free extracts initiates at or near the 3′ terminus and proceeds 3′ to 5′. J. Mol. Biol. 188: 579-593.
    • (1986) J. Mol. Biol , vol.188 , pp. 579-593
    • Ross, J.1    Kobs, G.2
  • 45
    • 0022979324 scopus 로고
    • Histone mRNA degradation in vivo: The first detectable step occurs at or near the 3′ terminus
    • Ross, J., Peltz, S.W., Kobs, G., and Brewer, G. 1986. Histone mRNA degradation in vivo: The first detectable step occurs at or near the 3′ terminus. Mol. Cell. Biol. 6: 4362-4371.
    • (1986) Mol. Cell. Biol , vol.6 , pp. 4362-4371
    • Ross, J.1    Peltz, S.W.2    Kobs, G.3    Brewer, G.4
  • 46
    • 0023236379 scopus 로고
    • Properties of the exonuclease activity that degrades H4 histone mRNA
    • Ross, J., Kobs, G., Brewer, G., and Peltz, S.W. 1987. Properties of the exonuclease activity that degrades H4 histone mRNA. J. Biol. Chem. 262: 9374-9381.
    • (1987) J. Biol. Chem , vol.262 , pp. 9374-9381
    • Ross, J.1    Kobs, G.2    Brewer, G.3    Peltz, S.W.4
  • 47
    • 0036786956 scopus 로고    scopus 로고
    • The stem-loop binding protein is required for efficient translation of histone mRNA in vivo and in vitro
    • Sanchez, R. and Marzluff, W.F. 2002. The stem-loop binding protein is required for efficient translation of histone mRNA in vivo and in vitro. Mol. Cell. Biol. 22: 7093-7104.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 7093-7104
    • Sanchez, R.1    Marzluff, W.F.2
  • 48
    • 0028321764 scopus 로고
    • The site of 3′ end formation of histone messenger RNA is a fixed distance from the downstream element recognized by the U7 snRNP
    • Scharl, E.C. and Steitz, J.A. 1994. The site of 3′ end formation of histone messenger RNA is a fixed distance from the downstream element recognized by the U7 snRNP. EMBO J. 13: 2432-2440.
    • (1994) EMBO J , vol.13 , pp. 2432-2440
    • Scharl, E.C.1    Steitz, J.A.2
  • 49
    • 19644400971 scopus 로고    scopus 로고
    • Uridine addition after microRNA-directed cleavage
    • Shen, B. and Goodman, H.M. 2004. Uridine addition after microRNA-directed cleavage. Science 306: 997.
    • (2004) Science , vol.306 , pp. 997
    • Shen, B.1    Goodman, H.M.2
  • 50
    • 0037968357 scopus 로고    scopus 로고
    • Decapping and decay of messenger RNA occur in cytoplasmic processing bodies
    • Sheth, U. and Parker, R. 2003. Decapping and decay of messenger RNA occur in cytoplasmic processing bodies. Science 300: 805-808.
    • (2003) Science , vol.300 , pp. 805-808
    • Sheth, U.1    Parker, R.2
  • 51
    • 36248947229 scopus 로고    scopus 로고
    • 3′ Terminal oligo U-tract-mediated stimulation of decapping
    • Song, M.G. and Kiledjian, M. 2007. 3′ Terminal oligo U-tract-mediated stimulation of decapping. RNA 13: 2356-2365.
    • (2007) RNA , vol.13 , pp. 2356-2365
    • Song, M.G.1    Kiledjian, M.2
  • 52
    • 33751297741 scopus 로고    scopus 로고
    • The Cid1 family of non-canonical poly(A) polymerases
    • Stevenson, A.L. and Norbury, C.J. 2006. The Cid1 family of non-canonical poly(A) polymerases. Yeast 23: 991-1000.
    • (2006) Yeast , vol.23 , pp. 991-1000
    • Stevenson, A.L.1    Norbury, C.J.2
  • 53
    • 33646200678 scopus 로고    scopus 로고
    • ARE-mRNA degradation requires the 5′-3′ decay pathway
    • Stoecklin, G., Mayo, T., and Anderson, P. 2006. ARE-mRNA degradation requires the 5′-3′ decay pathway. EMBO Rep. 7: 72-77.
    • (2006) EMBO Rep , vol.7 , pp. 72-77
    • Stoecklin, G.1    Mayo, T.2    Anderson, P.3
  • 54
    • 0033984159 scopus 로고    scopus 로고
    • Complex protein interactions within the human polyadenylation machinery identify a novel component
    • Takagaki, Y. and Manley, J.L. 2000. Complex protein interactions within the human polyadenylation machinery identify a novel component. Mol. Cell. Biol. 20: 1515-1525.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 1515-1525
    • Takagaki, Y.1    Manley, J.L.2
  • 55
    • 0035930337 scopus 로고    scopus 로고
    • Targeting an mRNA for decapping: Displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs
    • Tharun, S. and Parker, R. 2001. Targeting an mRNA for decapping: Displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs. Mol. Cell 8: 1075-1083.
    • (2001) Mol. Cell , vol.8 , pp. 1075-1083
    • Tharun, S.1    Parker, R.2
  • 56
    • 0034732089 scopus 로고    scopus 로고
    • Yeast Sm-like proteins function in mRNA decapping and decay
    • Tharun, S., He, W.H., Mayes, A.E., Lennertz, P., Beggs, J.D., and Parker, R. 2000. Yeast Sm-like proteins function in mRNA decapping and decay. Nature 404: 515-518.
    • (2000) Nature , vol.404 , pp. 515-518
    • Tharun, S.1    He, W.H.2    Mayes, A.E.3    Lennertz, P.4    Beggs, J.D.5    Parker, R.6
  • 57
    • 20444429430 scopus 로고    scopus 로고
    • Mutations in the Saccharomyces cerevisiae LSM1 gene that affect mRNA decapping and 3′ end protection
    • Tharun, S., Muhlrad, D., Chowdhury, A., and Parker, R. 2005. Mutations in the Saccharomyces cerevisiae LSM1 gene that affect mRNA decapping and 3′ end protection. Genetics 170: 33-46.
    • (2005) Genetics , vol.170 , pp. 33-46
    • Tharun, S.1    Muhlrad, D.2    Chowdhury, A.3    Parker, R.4
  • 58
    • 33746489955 scopus 로고    scopus 로고
    • Identification, cloning, and functional analysis of the human U6 snRNA-specific terminal uridylyl transferase
    • Trippe, R., Guschina, E., Hossbach, M., Urlaub, H., Luhrmann, R., and Benecke, B.J. 2006. Identification, cloning, and functional analysis of the human U6 snRNA-specific terminal uridylyl transferase. RNA 12: 1494-1504.
    • (2006) RNA , vol.12 , pp. 1494-1504
    • Trippe, R.1    Guschina, E.2    Hossbach, M.3    Urlaub, H.4    Luhrmann, R.5    Benecke, B.J.6
  • 59
    • 1642565815 scopus 로고    scopus 로고
    • The bacterial Sm-like protein Hfq: A key player in RNA transactions
    • Valentin-Hansen, P., Eriksen, M., and Udesen, C. 2004. The bacterial Sm-like protein Hfq: A key player in RNA transactions. Mol. Microbiol. 51: 1525-1533.
    • (2004) Mol. Microbiol , vol.51 , pp. 1525-1533
    • Valentin-Hansen, P.1    Eriksen, M.2    Udesen, C.3
  • 61
    • 0036810248 scopus 로고    scopus 로고
    • RNAi-mediated PTB depletion leads to enhanced exon definition
    • Wagner, E.J. and Garcia-Blanco, M.A. 2002. RNAi-mediated PTB depletion leads to enhanced exon definition. Mol. Cell 10: 943-949.
    • (2002) Mol. Cell , vol.10 , pp. 943-949
    • Wagner, E.J.1    Garcia-Blanco, M.A.2
  • 62
    • 33747779675 scopus 로고    scopus 로고
    • ZFP100, a component of the active U7 snRNP limiting for histone pre-mRNA processing, is required for entry into S-phase
    • Wagner, E.J. and Marzluff, W.F. 2006. ZFP100, a component of the active U7 snRNP limiting for histone pre-mRNA processing, is required for entry into S-phase. Mol. Cell. Biol. 26: 6702-6712.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 6702-6712
    • Wagner, E.J.1    Marzluff, W.F.2
  • 63
    • 0029839610 scopus 로고    scopus 로고
    • The protein which binds the 3′ end of histone mRNA: A novel RNA-binding protein required for histone pre-mRNA processing
    • Wang, Z.-F., Whitfield, M.L., Ingledue, T.I., Dominski, Z., and Marzluff, W.F. 1996. The protein which binds the 3′ end of histone mRNA: A novel RNA-binding protein required for histone pre-mRNA processing. Genes & Dev. 10: 3028-3040.
    • (1996) Genes & Dev , vol.10 , pp. 3028-3040
    • Wang, Z.-F.1    Whitfield, M.L.2    Ingledue, T.I.3    Dominski, Z.4    Marzluff, W.F.5
  • 64
  • 65
    • 0034128749 scopus 로고    scopus 로고
    • Stem-loop binding protein, the protein that binds the 3′ end of histone mRNA, is cell cycle regulated by both translational and posttranslational mechanisms
    • Whitfield, M.L., Zheng, L.-X., Baldwin, A., Ohta, T., Hurt, M.M., and Marzluff, W.F. 2000. Stem-loop binding protein, the protein that binds the 3′ end of histone mRNA, is cell cycle regulated by both translational and posttranslational mechanisms. Mol. Cell. Biol. 20: 4188-4198.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 4188-4198
    • Whitfield, M.L.1    Zheng, L.-X.2    Baldwin, A.3    Ohta, T.4    Hurt, M.M.5    Marzluff, W.F.6
  • 66
    • 2442419461 scopus 로고    scopus 로고
    • Endonuclease-mediated mRNA decay involves the selective targeting of PMR1 to polyribosome-bound substrate mRNA
    • Yang, F. and Schoenberg, D.R. 2004. Endonuclease-mediated mRNA decay involves the selective targeting of PMR1 to polyribosome-bound substrate mRNA. Mol. Cell 14: 435-445.
    • (2004) Mol. Cell , vol.14 , pp. 435-445
    • Yang, F.1    Schoenberg, D.R.2
  • 67
    • 33750044572 scopus 로고    scopus 로고
    • Characterization of 3′hExo, a 3′ exonuclease specifically interacting with the 3′ end of histone mRNA
    • Yang, X.C., Purdy, M., Marzluff, W.F., and Dominski, Z. 2006. Characterization of 3′hExo, a 3′ exonuclease specifically interacting with the 3′ end of histone mRNA. J. Biol. Chem. 281: 30447-30454.
    • (2006) J. Biol. Chem , vol.281 , pp. 30447-30454
    • Yang, X.C.1    Purdy, M.2    Marzluff, W.F.3    Dominski, Z.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.