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Volumn 170, Issue 1, 2005, Pages 33-46

Mutations in the Saccharomyces cerevisiae LSM1 gene that affect mRNA decapping and 3′ end protection

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; CARBOXY TERMINAL SEQUENCE; EUKARYOTE; FUNGAL GENE; GENE DELETION; GENE MUTATION; LSM1 GENE; NONHUMAN; PHENOTYPE; POINT MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN; RNA CAPPING; RNA DEGRADATION; SACCHAROMYCES CEREVISIAE;

EID: 20444429430     PISSN: 00166731     EISSN: None     Source Type: Journal    
DOI: 10.1534/genetics.104.034322     Document Type: Article
Times cited : (53)

References (86)
  • 1
    • 0030267492 scopus 로고    scopus 로고
    • Control of mRNA stability in higher plants
    • ABLER, M. L., and P. J. GREEN, 1996 Control of mRNA stability in higher plants. Plant Mol. Biol. 32: 63-78.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 63-78
    • Abler, M.L.1    Green, P.J.2
  • 2
    • 0033569743 scopus 로고    scopus 로고
    • A doughnut-shaped heteromer of human Sm-like proteins binds to the 3′-end of U6 snRNA, thereby facilitating U4/U6 duplex formation in vitro
    • ACHSEL, T., H. BRAHMS, B. KASTNER, A. BACHI, M. WILM et al., 1999 A doughnut-shaped heteromer of human Sm-like proteins binds to the 3′-end of U6 snRNA, thereby facilitating U4/U6 duplex formation in vitro. EMBO J. 18: 5789-5802.
    • (1999) EMBO J. , vol.18 , pp. 5789-5802
    • Achsel, T.1    Brahms, H.2    Kastner, B.3    Bachi, A.4    Wilm, M.5
  • 3
    • 0035957394 scopus 로고    scopus 로고
    • The Sm domain is an ancient RNA-binding motif with oligo(U) specificity
    • ACHSEL, T., H. STARK and R. LUHRMANN, 2001 The Sm domain is an ancient RNA-binding motif with oligo(U) specificity. Proc. Natl. Acad. Sci. USA 98: 3685-3689.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3685-3689
    • Achsel, T.1    Stark, H.2    Luhrmann, R.3
  • 4
    • 0033567131 scopus 로고    scopus 로고
    • The yeast exosome and human PM-Scl are related complexes of 3′ → 5′ exonucleases
    • ALLMANG, C., E. PETFALSKI, A. PODTELEJNIKOV, M. MANN, D. TOLLERVEY et al., 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
  • 5
    • 0000577868 scopus 로고    scopus 로고
    • The 3′ to 5′ degradation of yeast mRNAs is a general mechanism for mRNA turnover that requires the SKI2 DEVH box protein and 3′ to 5′ exonucleases of the exosome complex
    • ANDERSON, J. S. J., and R. P. PARKER, 1998 The 3′ to 5′ degradation of yeast mRNAs is a general mechanism for mRNA turnover that requires the SKI2 DEVH box protein and 3′ to 5′ exonucleases of the exosome complex. EMBO J. 17: 1497-1506.
    • (1998) EMBO J. , vol.17 , pp. 1497-1506
    • Anderson, J.S.J.1    Parker, R.P.2
  • 6
    • 0032606088 scopus 로고    scopus 로고
    • Model building by comparison at CASP3: Using expert knowledge and computer automation
    • BATES, P. A., and M. J. STERNBERG, 1999 Model building by comparison at CASP3: using expert knowledge and computer automation. Proteins (Suppl 3): 47-54.
    • (1999) Proteins , Issue.SUPPL. 3 , pp. 47-54
    • Bates, P.A.1    Sternberg, M.J.2
  • 7
    • 0035747672 scopus 로고    scopus 로고
    • Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM
    • BATES, P. A., L. A. KELLEY, R. M. MACCALLUM and M. J. STERNBERG, 2001 Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM. Proteins (Suppl 5): 39-46.
    • (2001) Proteins , Issue.SUPPL. 5 , pp. 39-46
    • Bates, P.A.1    Kelley, L.A.2    Maccallum, R.M.3    Sternberg, M.J.4
  • 8
    • 0029758321 scopus 로고    scopus 로고
    • An essential component of the decapping enzyme required for normal rates of mRNA turnover
    • BEELMAN, C. A., A. STEVENS, G. CAPONIGRO, T. E. LAGRANDEUR, L. HATFIELD et al., 1996 An essential component of the decapping enzyme required for normal rates of mRNA turnover. Nature 382: 642-646.
    • (1996) Nature , vol.382 , pp. 642-646
    • Beelman, C.A.1    Stevens, A.2    Caponigro, G.3    Lagrandeur, T.E.4    Hatfield, L.5
  • 9
    • 0031841817 scopus 로고    scopus 로고
    • Capped mRNA degradation intermediates accumulate in the yeast spb8-2 mutant
    • BOECK, R., B. LAPEYRE, C. E. BROWN and A. B. SACHS, 1998 Capped mRNA degradation intermediates accumulate in the yeast spb8-2 mutant. Mol. Cell. Biol. 18: 5062-5072.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5062-5072
    • Boeck, R.1    Lapeyre, B.2    Brown, C.E.3    Sachs, A.B.4
  • 10
    • 0033866402 scopus 로고    scopus 로고
    • The two proteins Pat1p (Mrt1p) and Spb8p interact in vivo, are required for mRNA decay, and are functionally linked to Pab1p
    • BONNEROT, C., R. BOECK and B. LAPEYRE, 2000 The two proteins Pat1p (Mrt1p) and Spb8p interact in vivo, are required for mRNA decay, and are functionally linked to Pab1p. Mol. Cell. Biol. 20: 5939-5946.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5939-5946
    • Bonnerot, C.1    Boeck, R.2    Lapeyre, B.3
  • 11
    • 0034599976 scopus 로고    scopus 로고
    • A Sm-like protein complex that participates in mRNA degradation
    • BOUVERET, E., G. RIGAUT, A. SHEVCHENKO, M. WILM and B. SERAPHIN, 2000 A Sm-like protein complex that participates in mRNA degradation. EMBO J. 19: 1661-1671.
    • (2000) EMBO J. , vol.19 , pp. 1661-1671
    • Bouveret, E.1    Rigaut, G.2    Shevchenko, A.3    Wilm, M.4    Seraphin, B.5
  • 12
    • 0034839596 scopus 로고    scopus 로고
    • Computational modeling of eukaryotic mRNA turnover
    • CAO, D., and R. PARKER, 2001 Computational modeling of eukaryotic mRNA turnover. RNA 7: 1192-1212.
    • (2001) RNA , vol.7 , pp. 1192-1212
    • Cao, D.1    Parker, R.2
  • 13
    • 0028809873 scopus 로고
    • Multiple functions for the poly(A)-binding protein in mRNA decapping and deadenylation in yeast
    • CAPONIGRO, G., and R. PARKER, 1995 Multiple functions for the poly(A)-binding protein in mRNA decapping and deadenylation in yeast. Genes Dev. 9: 2421-2432.
    • (1995) Genes Dev. , vol.9 , pp. 2421-2432
    • Caponigro, G.1    Parker, R.2
  • 14
    • 3943051423 scopus 로고    scopus 로고
    • Eukaryotic mRNA decapping
    • COLLER, J., and R. PARKER, 2004 Eukaryotic mRNA decapping. Annu. Rev. Biochem. 73: 861-890.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 861-890
    • Coller, J.1    Parker, R.2
  • 15
    • 0032532439 scopus 로고    scopus 로고
    • mRNA stabilization by poly(A)-binding protein is independent of poly(A) and requires translation
    • COLLER, J. M., N. K. GRAY and M. P. WICKENS, 1998 mRNA stabilization by poly(A)-binding protein is independent of poly(A) and requires translation. Genes Dev. 12: 3226-3235.
    • (1998) Genes Dev. , vol.12 , pp. 3226-3235
    • Coller, J.M.1    Gray, N.K.2    Wickens, M.P.3
  • 16
    • 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., M. TUCKER, U. SHETH, M. A. VALENCIA-SANCHEZ and R. PARKER, 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
  • 17
    • 0035876146 scopus 로고    scopus 로고
    • Crystal structure of a heptameric Sm-like protein complex from archaea: Implications for the structure and evolution of snRNPs
    • COLLINS, B. M., S. J. HARROP, G. D. KORNFELD, I. W. DAWES, P. M. CURMI et al., 2001 Crystal structure of a heptameric Sm-like protein complex from archaea: implications for the structure and evolution of snRNPs. J. Mol. Biol. 309: 915-923.
    • (2001) J. Mol. Biol. , vol.309 , pp. 915-923
    • Collins, B.M.1    Harrop, S.J.2    Kornfeld, G.D.3    Dawes, I.W.4    Curmi, P.M.5
  • 18
    • 0036678447 scopus 로고    scopus 로고
    • Domain fishing: A first step in protein comparative modelling
    • CONTRERAS-MOREIRA, B., and P. A. BATES, 2002 Domain fishing: a first step in protein comparative modelling. Bioinformatics 18: 1141-1142.
    • (2002) Bioinformatics , vol.18 , pp. 1141-1142
    • Contreras-Moreira, B.1    Bates, P.A.2
  • 19
    • 0029054375 scopus 로고
    • Identification and characterization of Uss1p (Sdb23p): A novel U6 snRNA-associated protein with significant similarity to core proteins of small nuclear ribonucleoproteins
    • COOPER, M., L. H. JOHNSTON and J. D. BEGGS, 1995 Identification and characterization of Uss1p (Sdb23p): a novel U6 snRNA-associated protein with significant similarity to core proteins of small nuclear ribonucleoproteins. EMBO J. 14: 2066-2075.
    • (1995) EMBO J. , vol.14 , pp. 2066-2075
    • Cooper, M.1    Johnston, L.H.2    Beggs, J.D.3
  • 20
    • 2442566370 scopus 로고    scopus 로고
    • Cytoplasmic foci are sites of mRNA decay in human cells
    • COUGOT, N., S. BABAJKO and B. SERAPHIN, 2004 Cytoplasmic foci are sites of mRNA decay in human cells. J. Cell Biol. 165: 31-40.
    • (2004) J. Cell Biol. , vol.165 , pp. 31-40
    • Cougot, N.1    Babajko, S.2    Seraphin, B.3
  • 22
    • 0027320701 scopus 로고
    • A turnover pathway for both stable and unstable mRNAs in yeast: Evidence for a requirement for deadenylation
    • DECKER, C. J., and R. PARKER, 1993 A turnover pathway for both stable and unstable mRNAs in yeast: evidence for a requirement for deadenylation. Genes Dev. 7: 1632-1643.
    • (1993) Genes Dev. , vol.7 , pp. 1632-1643
    • Decker, C.J.1    Parker, R.2
  • 23
    • 0036792048 scopus 로고    scopus 로고
    • mRNA decay enzymes: Decappers conserved between yeast and mammals
    • DECKER, C. J., and R. PARKER, 2002 mRNA decay enzymes: decappers conserved between yeast and mammals. Proc. Natl. Acad. Sci. USA 99: 12512-12514.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12512-12514
    • Decker, C.J.1    Parker, R.2
  • 24
    • 0033214061 scopus 로고    scopus 로고
    • The DCP2 protein is required for mRNA decapping in Saccharomyces cerevisiae and contains a functional MutT motif
    • DUNCKLEY, T., and R. PARKER, 1999 The DCP2 protein is required for mRNA decapping in Saccharomyces cerevisiae and contains a functional MutT motif. EMBO J. 18: 5411-5422.
    • (1999) EMBO J. , vol.18 , pp. 5411-5422
    • Dunckley, T.1    Parker, R.2
  • 25
    • 0035148534 scopus 로고    scopus 로고
    • Two related proteins, Edc1p and Edc2p, stimulate mRNA decapping in Saccharomyces cerevisiae
    • DUNCKLEY, T., M. TUCKER and R. PARKER, 2001 Two related proteins, Edc1p and Edc2p, stimulate mRNA decapping in Saccharomyces cerevisiae. Genetics 157: 27-37.
    • (2001) Genetics , vol.157 , pp. 27-37
    • Dunckley, T.1    Tucker, M.2    Parker, R.3
  • 26
    • 2542459281 scopus 로고    scopus 로고
    • An Lsm2-Lsm7 complex in Saccharomyces cerevisiae associates with the small nucleolar RNA snR5
    • FERNANDEZ, C. F., B. K. PANNONE, X. CHEN, G. FUCHS and S. L. WOLIN, 2004 An Lsm2-Lsm7 Complex in Saccharomyces cerevisiae Associates with the Small Nucleolar RNA snR5. Mol. Biol. Cell 15: 2842-2852.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2842-2852
    • Fernandez, C.F.1    Pannone, B.K.2    Chen, X.3    Fuchs, G.4    Wolin, S.L.5
  • 27
    • 0037013898 scopus 로고    scopus 로고
    • The DEAD box protein Dhh1 stimulates the decapping enzyme Dcp1
    • FISCHER, N., and K. WEIS, 2002 The DEAD box protein Dhh1 stimulates the decapping enzyme Dcp1. EMBOJ. 21: 2788-2797.
    • (2002) EMBOJ. , vol.21 , pp. 2788-2797
    • Fischer, N.1    Weis, K.2
  • 28
    • 0035282971 scopus 로고    scopus 로고
    • A novel mRNA-decapping activity in HeLa cytoplasmic extracts is regulated by AU-rich elements
    • GAO, M., C. J. WILUSZ, S. W. PELTZ and J. WILUSZ, 2001 A novel mRNA-decapping activity in HeLa cytoplasmic extracts is regulated by AU-rich elements. EMBO J. 20: 1134-1143.
    • (2001) EMBO J. , vol.20 , pp. 1134-1143
    • Gao, M.1    Wilusz, C.J.2    Peltz, S.W.3    Wilusz, J.4
  • 29
    • 0033598805 scopus 로고    scopus 로고
    • In silico detection of control signals: mRNA 3′-end -processing sequences in diverse species
    • GRABER, J. H., C. R. CANTOR, S. C. MOHR and T. F. SMITH, 1999 In silico detection of control signals: mRNA 3′-end -processing sequences in diverse species. Proc. Natl. Acad. Sci. USA 96: 14055-14060.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14055-14060
    • Graber, J.H.1    Cantor, C.R.2    Mohr, S.C.3    Smith, T.F.4
  • 30
    • 0035819859 scopus 로고    scopus 로고
    • Regulation of mRNA stability in mammalian cells
    • GUHANIYOGI, J., and G. BREWER, 2001 Regulation of mRNA stability in mammalian cells. Gene 265: 11-23.
    • (2001) Gene , vol.265 , pp. 11-23
    • Guhaniyogi, J.1    Brewer, G.2
  • 31
    • 0036635441 scopus 로고    scopus 로고
    • Overexpression of the Sm-like proto-oncogene in primary and metastatic pancreatic endocrine tumors
    • GUMBS, A. A., C. BASSI, P. S. MOORE, M. FALCONI, I. FRIGERIO et al., 2002 Overexpression of the Sm-like proto-oncogene in primary and metastatic pancreatic endocrine tumors. JOP 3: 109-115.
    • (2002) JOP , vol.3 , pp. 109-115
    • Gumbs, A.A.1    Bassi, C.2    Moore, P.S.3    Falconi, M.4    Frigerio, I.5
  • 32
    • 0029791555 scopus 로고    scopus 로고
    • Mutations in trans-acting factors affecting mRNA decapping in Saccharomyces cerevisiae
    • HATFIELD, L., C. A. BEELMAN, A. STEVENS and R. PARKER, 1996 Mutations in trans-acting factors affecting mRNA decapping in Saccharomyces cerevisiae. Mol. Cell. Biol. 16: 5830-5838.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5830-5838
    • Hatfield, L.1    Beelman, C.A.2    Stevens, A.3    Parker, R.4
  • 33
    • 0034741815 scopus 로고    scopus 로고
    • The yeast cytoplasmic Lsm1/Pat1p complex protects mRNA 3′ termini from partial degradation
    • HE, W., and R. PARKER, 2001 The yeast cytoplasmic Lsm1/Pat1p complex protects mRNA 3′ termini from partial degradation. Genetics 158: 1445-1455.
    • (2001) Genetics , vol.158 , pp. 1445-1455
    • He, W.1    Parker, R.2
  • 34
    • 0025938440 scopus 로고
    • Determinants and regulation of cytoplasmic mRNA stability in eukaryotic cells
    • HENTZE, M. W., 1991 Determinants and regulation of cytoplasmic mRNA stability in eukaryotic cells. Biochim. Biophys. Acta 1090: 281-292.
    • (1991) Biochim. Biophys. Acta , vol.1090 , pp. 281-292
    • Hentze, M.W.1
  • 35
    • 0029054377 scopus 로고
    • snRNP Sm proteins share two evolutionarily conserved sequence motifs which are involved in Sm protein-protein interactions
    • HERMANN, H., P. FABRIZIO, V. A. RAKER, K. FOULAKI, H. HORNIG et al., 1995 snRNP Sm proteins share two evolutionarily conserved sequence motifs which are involved in Sm protein-protein interactions. EMBO J. 14: 2076-2088.
    • (1995) EMBO J. , vol.14 , pp. 2076-2088
    • Hermann, H.1    Fabrizio, P.2    Raker, V.A.3    Foulaki, K.4    Hornig, H.5
  • 36
    • 0027214097 scopus 로고
    • Yeast cells lacking 5′→3′ exoribonuclease 1 contain mRNA species that are poly(A) deficient and partially lack the 5′ cap structure
    • HSU, C. L., and A. STEVENS, 1993 Yeast cells lacking 5′→ 3′ exoribonuclease 1 contain mRNA species that are poly(A) deficient and partially lack the 5′ cap structure. Mol. Cell. Biol. 13: 4826-4835.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4826-4835
    • Hsu, C.L.1    Stevens, A.2
  • 37
    • 0036909093 scopus 로고    scopus 로고
    • The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci
    • INGELFINGER, D., D. J. ARNDT-JOVIN, R. LUHRMANN and T. ACHSEL, 2002 The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci. RNA 8: 1489-1501.
    • (2002) RNA , vol.8 , pp. 1489-1501
    • Ingelfinger, D.1    Arndt-Jovin, D.J.2    Luhrmann, R.3    Achsel, T.4
  • 38
    • 0033524941 scopus 로고    scopus 로고
    • Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs
    • KAMBACH, C., S. WALKE, R. YOUNG, J. M. AVIS, E. DE LA FORTELLE et al., 1999 Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs. Cell 96: 375-387.
    • (1999) Cell , vol.96 , pp. 375-387
    • Kambach, C.1    Walke, S.2    Young, R.3    Avis, J.M.4    De La Fortelle, E.5
  • 39
    • 3142515957 scopus 로고    scopus 로고
    • Poly(A)-binding-protein-mediated regulation of hDcp2 decapping in vitro
    • KHANNA, R., and M. KILEDJIAN, 2004 Poly(A)-binding-protein-mediated regulation of hDcp2 decapping in vitro. EMBO J. 23: 1968-1976.
    • (2004) EMBO J. , vol.23 , pp. 1968-1976
    • Khanna, R.1    Kiledjian, M.2
  • 40
    • 1642343366 scopus 로고    scopus 로고
    • Identification of Edc3p as an enhancer of mRNA decapping in Saccharomyces cerevisiae
    • KSHIRSAGAR, M., and R. PARKER, 2004 Identification of Edc3p as an enhancer of mRNA decapping in Saccharomyces cerevisiae. Genetics 166: 729-739.
    • (2004) Genetics , vol.166 , pp. 729-739
    • Kshirsagar, M.1    Parker, R.2
  • 41
    • 0019829528 scopus 로고
    • Snurps and scyrps
    • LERNER, M. R., and J. A. STEITZ, 1981 Snurps and scyrps. Cell 25: 298-300.
    • (1981) Cell , vol.25 , pp. 298-300
    • Lerner, M.R.1    Steitz, J.A.2
  • 42
    • 0037009517 scopus 로고    scopus 로고
    • The scavenger mRNA decapping enzyme DcpS is a member of the HIT family of pyrophosphatases
    • LIU, H., N. D. RODGERS, X. JIAO and M. KILEDJIAN, 2002 The scavenger mRNA decapping enzyme DcpS is a member of the HIT family of pyrophosphatases. EMBO J. 21: 4699-4708.
    • (2002) EMBO J. , vol.21 , pp. 4699-4708
    • Liu, H.1    Rodgers, N.D.2    Jiao, X.3    Kiledjian, M.4
  • 43
    • 0025173604 scopus 로고
    • Structure of spliceosomal snRNPs and their role in pre-mRNA splicing
    • LUHRMANN, R., B. KASTNER and M. BACH, 1990 Structure of spliceosomal snRNPs and their role in pre-mRNA splicing. Biochim. Biophys. Acta 1087: 265-292.
    • (1990) Biochim. Biophys. Acta , vol.1087 , pp. 265-292
    • Luhrmann, R.1    Kastner, B.2    Bach, M.3
  • 44
    • 0036888905 scopus 로고    scopus 로고
    • Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay
    • LYKKE-ANDERSEN, J., 2002 Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay. Mol. Cell. Biol. 22: 8114-8121.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8114-8121
    • Lykke-Andersen, J.1
  • 45
    • 0033517098 scopus 로고    scopus 로고
    • Characterization of Sm-like proteins in yeast and their association with U6 snRNA
    • MAYES, A. E., L. VERDONE, P. LEGRAIN and J. D. BEGGS, 1999 Characterization of Sm-like proteins in yeast and their association with U6 snRNA. EMBO J. 18: 4321-4331.
    • (1999) EMBO J. , vol.18 , pp. 4321-4331
    • Mayes, A.E.1    Verdone, L.2    Legrain, P.3    Beggs, J.D.4
  • 46
    • 0002782867 scopus 로고    scopus 로고
    • Hfq: A bacterial Sm-like protein that mediates RNA-RNA interaction
    • MOLLER, T., T. FRANCH, P. HOJRUP, D. R. KEENE, H. P. BACHINGER et al., 2002 Hfq: a bacterial Sm-like protein that mediates RNA-RNA interaction. Mol. Cell 9: 23-30.
    • (2002) Mol. Cell , vol.9 , pp. 23-30
    • Moller, T.1    Franch, T.2    Hojrup, P.3    Keene, D.R.4    Bachinger, H.P.5
  • 47
    • 0026441426 scopus 로고
    • Mutations affecting stability and deadenylation of the yeast MFA2 transcript
    • MUHLRAD, D., and R. PARKER, 1992 Mutations affecting stability and deadenylation of the yeast MFA2 transcript. Genes Dev. 6: 2100-2111.
    • (1992) Genes Dev. , vol.6 , pp. 2100-2111
    • Muhlrad, D.1    Parker, R.2
  • 48
    • 0028202495 scopus 로고
    • Deadenylation of the unstable mRNA encoded by the yeast MFA2 gene leads to decapping followed by 5′→3′ digestion of the transcript
    • MUHLRAD, D., C. J. DECKER and R. PARKER, 1994 Deadenylation of the unstable mRNA encoded by the yeast MFA2 gene leads to decapping followed by 5′→3′ digestion of the transcript. Genes Dev. 8: 855-866.
    • (1994) Genes Dev. , vol.8 , pp. 855-866
    • Muhlrad, D.1    Decker, C.J.2    Parker, R.3
  • 49
    • 0028961870 scopus 로고
    • Turnover mechanisms of the stable yeast PGK1 mRNA
    • MUHLRAD, D., C. J. DECKER and R. PARKER, 1995 Turnover mechanisms of the stable yeast PGK1 mRNA. Mol. Cell. Biol. 15: 2145-2156.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2145-2156
    • Muhlrad, D.1    Decker, C.J.2    Parker, R.3
  • 50
    • 0035826794 scopus 로고    scopus 로고
    • The crystal structure of a heptameric archaeal Sm protein: Implications for the eukaryotic snRNP core
    • MURA, C., D. CASCIO, M. R. SAWAYA and D. S. EISENBERG, 2001 The crystal structure of a heptameric archaeal Sm protein: Implications for the eukaryotic snRNP core. Proc. Natl. Acad. Sci. USA 98: 5532-5537.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5532-5537
    • Mura, C.1    Cascio, D.2    Sawaya, M.R.3    Eisenberg, D.S.4
  • 51
    • 0037378351 scopus 로고    scopus 로고
    • The oligomerization and ligand-binding properties of Sm-like archaeal proteins (SmAPs)
    • MURA, C., A. KOZHUKHOVSKY, M. GINGERY, M. PHILLIPS and D. EISENBERG, 2003 The oligomerization and ligand-binding properties of Sm-like archaeal proteins (SmAPs). Protein Sci. 12: 832-847.
    • (2003) Protein Sci. , vol.12 , pp. 832-847
    • Mura, C.1    Kozhukhovsky, A.2    Gingery, M.3    Phillips, M.4    Eisenberg, D.5
  • 52
    • 0032535451 scopus 로고    scopus 로고
    • A role for the yeast La protein in U6 snRNP assembly: Evidence that the La protein is a molecular chaperone for RNA polymerase III transcripts
    • PANNONE, B. K., D. XUE and S. L. WOLIN, 1998 A role for the yeast La protein in U6 snRNP assembly: evidence that the La protein is a molecular chaperone for RNA polymerase III transcripts. EMBO J. 17: 7442-7453.
    • (1998) EMBO J. , vol.17 , pp. 7442-7453
    • Pannone, B.K.1    Xue, D.2    Wolin, S.L.3
  • 53
    • 0035022015 scopus 로고    scopus 로고
    • Multiple functional interactions between components of the Lsm2-Lsm8 complex, U6 snRNA, and the yeast La protein
    • PANNONE, B. K., S. D. KIM, D. A. NOE and S. L. WOLIN, 2001 Multiple functional interactions between components of the Lsm2-Lsm8 complex, U6 snRNA, and the yeast La protein. Genetics 158: 187-196.
    • (2001) Genetics , vol.158 , pp. 187-196
    • Pannone, B.K.1    Kim, S.D.2    Noe, D.A.3    Wolin, S.L.4
  • 55
    • 0041832085 scopus 로고    scopus 로고
    • Functional characterization of the mammalian mRNA decapping enzyme hDcp2
    • PICCIRILLO, C., R. KHANNA and M. KILEDJIAN, 2003 Functional characterization of the mammalian mRNA decapping enzyme hDcp2. RNA 9: 1138-1147.
    • (2003) RNA , vol.9 , pp. 1138-1147
    • Piccirillo, C.1    Khanna, R.2    Kiledjian, M.3
  • 56
    • 0032862988 scopus 로고    scopus 로고
    • Spliceosomal U snRNP core assembly: Sm proteins assemble onto an Sm site RNA nonanucleotide in a specific and thermodynamically stable manner
    • RAKER, V. A., K. HARTMUTH, B. KASTNER and R. LUHRMANN, 1999 Spliceosomal U snRNP core assembly: Sm proteins assemble onto an Sm site RNA nonanucleotide in a specific and thermodynamically stable manner. Mol. Cell. Biol. 19: 6554-6565.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6554-6565
    • Raker, V.A.1    Hartmuth, K.2    Kastner, B.3    Luhrmann, R.4
  • 57
    • 0037053430 scopus 로고    scopus 로고
    • Modulation of eukaryotic mRNA stability via the cap-binding translation complex eIF4F
    • RAMIREZ, C. V., C. VILELA, K. BERTHELOT and J. E. MCCARTHY, 2002 Modulation of eukaryotic mRNA stability via the cap-binding translation complex eIF4F. J. Mol. Biol. 318: 951-962.
    • (2002) J. Mol. Biol. , vol.318 , pp. 951-962
    • Ramirez, C.V.1    Vilela, C.2    Berthelot, K.3    Mccarthy, J.E.4
  • 58
    • 0033564627 scopus 로고    scopus 로고
    • Sm and Sm-like proteins assemble in two related complexes of deep evolutionary origin
    • SALGADO-GARRIDO, J., E. BRAGADO-NILSSON, S. KANDELS-LEAVIS and B. SERAPHIN, 1999 Sm and Sm-like proteins assemble in two related complexes of deep evolutionary origin. EMBO J. 18:3451-3462.
    • (1999) EMBO J. , vol.18 , pp. 3451-3462
    • Salgado-Garrido, J.1    Bragado-Nilsson, E.2    Kandels-Leavis, S.3    Seraphin, B.4
  • 59
    • 0036645689 scopus 로고    scopus 로고
    • Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: A bacterial Sm-like protein
    • SCHUMACHER, M. A., R. F. PEARSON, T. MOLLER, P. VALENTIN-HANSEN and R. G. BRENNAN, 2002 Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: a bacterial Sm-like protein. EMBO J. 21: 3546-3556.
    • (2002) EMBO J. , vol.21 , pp. 3546-3556
    • Schumacher, M.A.1    Pearson, R.F.2    Moller, T.3    Valentin-Hansen, P.4    Brennan, R.G.5
  • 60
    • 0032778953 scopus 로고    scopus 로고
    • Mutations in translation initiation factors lead to increased rates of deadenylation and decapping of mRNAs in Saccharomyces cerevisiae
    • SCHWARTZ, D. C., and R. PARKER, 1999 Mutations in translation initiation factors lead to increased rates of deadenylation and decapping of mRNAs in Saccharomyces cerevisiae. Mol. Cell. Biol. 19: 5247-5256.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5247-5256
    • Schwartz, D.C.1    Parker, R.2
  • 61
    • 0033773044 scopus 로고    scopus 로고
    • mRNA decapping in yeast requires dissociation of the cap binding protein, eukaryotic translation initiation factor 4E
    • SCHWARTZ, D. C., and R. PARKER, 2000 mRNA decapping in yeast requires dissociation of the cap binding protein, eukaryotic translation initiation factor 4E. Mol. Cell. Biol. 20: 7933-7942.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7933-7942
    • Schwartz, D.C.1    Parker, R.2
  • 62
    • 0037322952 scopus 로고    scopus 로고
    • The enhancer of decapping proteins, Edc1p and Edc2p, bind RNA and stimulate the activity of the decapping enzyme
    • SCHWARTZ, D., C. J. DECKER and R. PARKER, 2003 The enhancer of decapping proteins, Edc1p and Edc2p, bind RNA and stimulate the activity of the decapping enzyme. RNA 9: 239-251.
    • (2003) RNA , vol.9 , pp. 239-251
    • Schwartz, D.1    Decker, C.J.2    Parker, R.3
  • 63
    • 0030745970 scopus 로고    scopus 로고
    • CaSm: An Sm-like protein that contributes to the transformed state in cancer cells
    • SCHWEINFEST, C. W., M. W. GRABER, J. M. CHAPMAN, T. S. PAPAS, P. L. BARON et al., 1997 CaSm: an Sm-like protein that contributes to the transformed state in cancer cells. Cancer Res. 57: 2961-2965.
    • (1997) Cancer Res. , vol.57 , pp. 2961-2965
    • Schweinfest, C.W.1    Graber, M.W.2    Chapman, J.M.3    Papas, T.S.4    Baron, P.L.5
  • 64
    • 0027012508 scopus 로고
    • The HIT protein family: A new family of proteins present in prokaryotes, yeast and mammals
    • SERAPHIN, B., 1992 The HIT protein family: a new family of proteins present in prokaryotes, yeast and mammals. DNA Seq. 3: 177-179.
    • (1992) DNA Seq. , vol.3 , pp. 177-179
    • Seraphin, B.1
  • 65
    • 0028997105 scopus 로고
    • Sm and Sm-like proteins belong to a large family: Identification of proteins of the U6 as well as the U1, U2, U4 and U5 snRNPs
    • SERAPHIN, B., 1995 Sm and Sm-like proteins belong to a large family: identification of proteins of the U6 as well as the U1, U2, U4 and U5 snRNPs. EMBO J. 14: 2089-2098.
    • (1995) EMBO J. , vol.14 , pp. 2089-2098
    • Seraphin, B.1
  • 66
    • 0037968357 scopus 로고    scopus 로고
    • Decapping and decay of messenger RNA occur in cytoplasmic processing bodies
    • SHETH, U., and R. PARKER, 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
  • 67
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • SIKORSKI, R. S., and P. HIETER, 1989 A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122: 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 68
    • 15444379718 scopus 로고    scopus 로고
    • Processing bodies require RNA for assembly and contain non-translating mRNAs
    • TEIXEIRA, D., U. SHETH, M. A. VALENCIA-SANCHEZ, M. BRENGUES and R. PARKER, 2005 Processing bodies require RNA for assembly and contain non-translating mRNAs. RNA 11: 371-382.
    • (2005) RNA , vol.11 , pp. 371-382
    • Teixeira, D.1    Sheth, U.2    Valencia-Sanchez, M.A.3    Brengues, M.4    Parker, R.5
  • 69
    • 0032940545 scopus 로고    scopus 로고
    • Analysis of mutations in the yeast mRNA decapping enzyme
    • THARUN, S., and R. PARKER, 1999 Analysis of mutations in the yeast mRNA decapping enzyme. Genetics 151: 1273-1285.
    • (1999) Genetics , vol.151 , pp. 1273-1285
    • Tharun, S.1    Parker, R.2
  • 70
    • 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 R. PARKER, 2001a 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
  • 71
    • 20444385353 scopus 로고    scopus 로고
    • Turnover of mRNA in eukaryotic cells
    • edited by D. Soll, S. Nishimura and P. Moore. Pergamon, New York/Oxford
    • THARUN, S., and R. PARKER, 2001b Turnover of mRNA in eukaryotic cells, pp. 245-257 in RNA, edited by D. SOLL, S. NISHIMURA and P. MOORE. Pergamon, New York/Oxford.
    • (2001) RNA , pp. 245-257
    • Tharun, S.1    Parker, R.2
  • 72
    • 0034732089 scopus 로고    scopus 로고
    • Yeast Sm-like proteins function in mRNA decapping and decay
    • THARUN, S., W. HE, A. E. MAYES, P. LENNERTZ, J. D. BEGGS et al., 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.2    Mayes, A.E.3    Lennertz, P.4    Beggs, J.D.5
  • 73
    • 0035341325 scopus 로고    scopus 로고
    • RNA binding in an Sm core domain: X-ray structure and functional analysis of an archaeal Sm protein complex
    • TORO, I., S. THORE, C. MAYER, J. BASQUIN, B. SERAPHIN et al., 2001 RNA binding in an Sm core domain: X-ray structure and functional analysis of an archaeal Sm protein complex. EMBO J. 20: 2293-2303.
    • (2001) EMBO J. , vol.20 , pp. 2293-2303
    • Toro, I.1    Thore, S.2    Mayer, C.3    Basquin, J.4    Seraphin, B.5
  • 74
    • 0344875482 scopus 로고    scopus 로고
    • Functional conservation of Dhh1p, a cytoplasmic DExD/H-box protein present in large complexes
    • TSENG-ROGENSKI, S. S., J. L. CHONG, C. B. THOMAS, S. ENOMOTO, J. BERMAN et al., 2003 Functional conservation of Dhh1p, a cytoplasmic DExD/H-box protein present in large complexes. Nucleic Acids Res. 31: 4995-5002.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 4995-5002
    • Tseng-Rogenski, S.S.1    Chong, J.L.2    Thomas, C.B.3    Enomoto, S.4    Berman, J.5
  • 75
    • 0035830508 scopus 로고    scopus 로고
    • The transcription factor associated Ccr4 and Caf1 proteins are components of the major cytoplasmic mRNA deadenylase in Saccharomyces cerevisiae
    • TUCKER, M., M. A. VALENCIA-SANCHEZ, R. R. STAPEES, J. CHEN, C. L. DENIS et al., 2001 The transcription factor associated Ccr4 and Caf1 proteins are components of the major cytoplasmic mRNA deadenylase in Saccharomyces cerevisiae. Cell 104: 377-386.
    • (2001) Cell , vol.104 , pp. 377-386
    • Tucker, M.1    Valencia-Sanchez, M.A.2    Stapees, R.R.3    Chen, J.4    Denis, C.L.5
  • 76
    • 0035863194 scopus 로고    scopus 로고
    • Sm protein-Sm site RNA interactions within the inner ring of the spliceosomal snRNP core structure
    • URLAUB, H., V. A. RAKER, S. KOSTKA and R. LUHRMANN, 2001 Sm protein-Sm site RNA interactions within the inner ring of the spliceosomal snRNP core structure. EMBO J. 20: 187-196.
    • (2001) EMBO J. , vol.20 , pp. 187-196
    • Urlaub, H.1    Raker, V.A.2    Kostka, S.3    Luhrmann, R.4
  • 77
    • 0037121926 scopus 로고    scopus 로고
    • Human Dcp2: A catalytically active mRNA decapping enzyme located in specific cytoplasmic structures
    • VAN DIJK, E., N. COUGOT, S. MEYER, S. BABAJKO, E. WAHLE et al., 2002 Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures. EMBO J. 21: 6915-6924.
    • (2002) EMBO J. , vol.21 , pp. 6915-6924
    • Van Dijk, E.1    Cougot, N.2    Meyer, S.3    Babajko, S.4    Wahle, E.5
  • 78
    • 0142027794 scopus 로고    scopus 로고
    • DcpS can act in the 5′-3′ mRNA decay pathway in addition to the 3′-5′ pathway
    • VAN DIJK, E., H. LE HIR and B. SERAPHIN, 2003 DcpS can act in the 5′-3′ mRNA decay pathway in addition to the 3′-5′ pathway. Proc. Natl. Acad. Sci. USA 100: 12081-12086.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12081-12086
    • Van Dijk, E.1    Le Hir, H.2    Seraphin, B.3
  • 79
    • 0033777266 scopus 로고    scopus 로고
    • Function of the ski4p (Csl4p) and Ski7p proteins in 3′-to-5′ degradation of mRNA
    • VAN HOOF, A., R. R. STAPLES, R. E. BAKER and R. PARKER, 2000 Function of the ski4p (Csl4p) and Ski7p proteins in 3′-to-5′ degradation of mRNA. Mol. Cell. Biol. 20: 8230-8243.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8230-8243
    • Van Hoof, A.1    Staples, R.R.2    Baker, R.E.3    Parker, R.4
  • 80
    • 0034663782 scopus 로고    scopus 로고
    • The eukaryotic mRNA decapping protein Dcp1 interacts physically and functionally with the eIF4F translation initiation complex
    • VILELA, C., C. VELASCO, M. PTUSHKINA and J. E. MCCARTHY, 2000 The eukaryotic mRNA decapping protein Dcp1 interacts physically and functionally with the eIF4F translation initiation complex. EMBO J. 19: 4372-4382.
    • (2000) EMBO J. , vol.19 , pp. 4372-4382
    • Vilela, C.1    Velasco, C.2    Ptushkina, M.3    Mccarthy, J.E.4
  • 81
    • 0035861864 scopus 로고    scopus 로고
    • Functional link between the mammalian exosome and mRNA decapping
    • WANG, Z., and M. KILEDJIAN, 2001 Functional link between the mammalian exosome and mRNA decapping. Cell 107: 751-762.
    • (2001) Cell , vol.107 , pp. 751-762
    • Wang, Z.1    Kiledjian, M.2
  • 83
    • 0034761729 scopus 로고    scopus 로고
    • Poly(A)-binding proteins regulate both mRNA deadenylation and decapping in yeast cytoplasmic extracts
    • WILUSZ, C. J., M. GAO, C. L. JONES, J. WILUSZ and S. W. PELTZ, 2001 Poly(A)-binding proteins regulate both mRNA deadenylation and decapping in yeast cytoplasmic extracts. RNA 7: 1416-1424.
    • (2001) RNA , vol.7 , pp. 1416-1424
    • Wilusz, C.J.1    Gao, M.2    Jones, C.L.3    Wilusz, J.4    Peltz, S.W.5
  • 84
    • 0034012159 scopus 로고    scopus 로고
    • Deletion of the PAT1 gene affects translation initiation and suppresses a PAB1 gene deletion in yeast
    • WYERS, F., M. MINET, M. E. DUFOUR, L. T. VO and F. LACROUTE, 2000 Deletion of the PAT1 gene affects translation initiation and suppresses a PAB1 gene deletion in yeast. Mol. Cell. Biol. 20: 3538-3549.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3538-3549
    • Wyers, F.1    Minet, M.2    Dufour, M.E.3    Vo, L.T.4    Lacroute, F.5
  • 85
    • 0032938118 scopus 로고    scopus 로고
    • Nip7p interacts with Nop8p, an essential nucleolar protein required for 60S ribosome biogenesis, and the exosome subunit Rrp43p
    • ZANCHIN, N. I., and D. S. GOLDFARB, 1999 Nip7p interacts with Nop8p, an essential nucleolar protein required for 60S ribosome biogenesis, and the exosome subunit Rrp43p. Mol. Cell. Biol. 19: 1518-1525.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1518-1525
    • Zanchin, N.I.1    Goldfarb, D.S.2
  • 86
    • 18144402771 scopus 로고    scopus 로고
    • Reconstitution of two recombinant Lsm protein complexes reveals aspects of their architecture, assembly and function
    • in press
    • ZARIC, B., M. CHAMI, H. REMIGY, A. ENGEL, K. BALLMER-HOFER et al., 2005 Reconstitution of two recombinant Lsm protein complexes reveals aspects of their architecture, assembly and function. J. Biol. Chem. (in press).
    • (2005) J. Biol. Chem.
    • Zaric, B.1    Chami, M.2    Remigy, H.3    Engel, A.4    Ballmer-Hofer, K.5


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