메뉴 건너뛰기




Volumn 24, Issue 10, 2004, Pages 4196-4206

Identification of factors regulating poly(A) tail synthesis and maturation

Author keywords

[No Author keywords available]

Indexed keywords

HYBRID PROTEIN; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE; PBP 4 PROTEIN; POLYADENYLIC ACID BINDING PROTEIN; PROTEIN SUBUNIT; UNCLASSIFIED DRUG; CARRIER PROTEIN; EXORIBONUCLEASE; FIR1 PROTEIN, S CEREVISIAE; FUNGAL DNA; FUNGAL RNA; PBP1 PROTEIN, S CEREVISIAE; POLY(A)-SPECIFIC RIBONUCLEASE; POLYADENYLATE SPECIFIC RIBONUCLEASE; POLYNUCLEOTIDE ADENYLYLTRANSFERASE; REF2 PROTEIN, S CEREVISIAE; RNA BINDING PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 2942536740     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.24.10.4196-4206.2004     Document Type: Article
Times cited : (49)

References (49)
  • 1
    • 0029989867 scopus 로고    scopus 로고
    • Mutations in STS1 suppress the defect in 3′ mRNA processing caused by the ma15-2 mutation in Saccharomyces cerevisiae
    • Amrani, N., M. E. Dufour, N. Bonneaud, and F. Lacroute. 1996. Mutations in STS1 suppress the defect in 3′ mRNA processing caused by the ma15-2 mutation in Saccharomyces cerevisiae. Mol. Gen. Genet. 252:552-562.
    • (1996) Mol. Gen. Genet. , vol.252 , pp. 552-562
    • Amrani, N.1    Dufour, M.E.2    Bonneaud, N.3    Lacroute, F.4
  • 2
    • 0031011852 scopus 로고    scopus 로고
    • Yeast Pab1 interacts with Rna15 and participates in the control of the poly(A) tail length in vitro
    • Amrani, N., M. Minet, M. Le Gouar, F. Lacroute, and F. Wyers. 1997. Yeast Pab1 interacts with Rna15 and participates in the control of the poly(A) tail length in vitro. Mol. Cell. Biol. 17:3694-3701.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3694-3701
    • Amrani, N.1    Minet, M.2    Le Gouar, M.3    Lacroute, F.4    Wyers, F.5
  • 3
    • 0034679803 scopus 로고    scopus 로고
    • Distinct roles of two Yth1p domains in 3′-end cleavage and polyadenylation of yeast pre-mRNAs
    • Barabino, S. M., M. Ohnacker, and W. Keller. 2000. Distinct roles of two Yth1p domains in 3′-end cleavage and polyadenylation of yeast pre-mRNAs. EMBO J. 19:3778-3787.
    • (2000) EMBO J. , vol.19 , pp. 3778-3787
    • Barabino, S.M.1    Ohnacker, M.2    Keller, W.3
  • 4
    • 0027255909 scopus 로고
    • Elimination of false positives that arise in using the two-hybrid system
    • Bartel, P., C. T. Chien, R. Sternglanz, and S. Fields. 1993. Elimination of false positives that arise in using the two-hybrid system. BioTechniques 14:920-924.
    • (1993) BioTechniques , vol.14 , pp. 920-924
    • Bartel, P.1    Chien, C.T.2    Sternglanz, R.3    Fields, S.4
  • 7
    • 0030070804 scopus 로고    scopus 로고
    • The yeast Pan2 protein is required for poly(A)-binding protein-stimulated poly(A)-nuclease activity
    • Boeck, R., S. Tarun, Jr., M. Rieger, J. A. Deardorff, S. Muller-Auer, and A. B. Sachs. 1996. The yeast Pan2 protein is required for poly(A)-binding protein-stimulated poly(A)-nuclease activity. J. Biol. Chem. 271:432-438.
    • (1996) J. Biol. Chem. , vol.271 , pp. 432-438
    • Boeck, R.1    Tarun Jr., S.2    Rieger, M.3    Deardorff, J.A.4    Muller-Auer, S.5    Sachs, A.B.6
  • 8
    • 0031740339 scopus 로고    scopus 로고
    • Poly(A) tail length control in Saccharomyces cerevisiae occurs by message-specific deadenylation
    • Brown, C. E., and A. B. Sachs. 1998. Poly(A) tail length control in Saccharomyces cerevisiae occurs by message-specific deadenylation. Mol. Cell. Biol. 18:6548-6559.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6548-6559
    • Brown, C.E.1    Sachs, A.B.2
  • 9
    • 0029811599 scopus 로고    scopus 로고
    • PAN3 encodes a subunit of the Pab1p-dependent poly(A) nuclease in Saccharomyces cerevisiae
    • Brown, C. E., S. Z. Tarun, Jr., R. Boeck, and A. B. Sachs. 1996. PAN3 encodes a subunit of the Pab1p-dependent poly(A) nuclease in Saccharomyces cerevisiae. Mol. Cell. Biol. 16:5744-5753.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5744-5753
    • Brown, C.E.1    Tarun Jr., S.Z.2    Boeck, R.3    Sachs, A.B.4
  • 10
    • 0032213290 scopus 로고    scopus 로고
    • A specific RNA-protein interaction at yeast polyadenylation efficiency elements
    • Chen, S., and L. E. Hyman. 1998. A specific RNA-protein interaction at yeast polyadenylation efficiency elements. Nucleic Acids Res. 26:4965-4974.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4965-4974
    • Chen, S.1    Hyman, L.E.2
  • 11
    • 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
  • 12
    • 0029804618 scopus 로고    scopus 로고
    • Two novel targets of the MAP kinase Kss1 are negative regulators of invasive growth in the yeast Saccharomyces cerevisiae
    • Cook, J. G., L. Bardwell, S. J. Kron, and J. Thorner. 1996. Two novel targets of the MAP kinase Kss1 are negative regulators of invasive growth in the yeast Saccharomyces cerevisiae. Genes Dev. 10:2831-2848.
    • (1996) Genes Dev. , vol.10 , pp. 2831-2848
    • Cook, J.G.1    Bardwell, L.2    Kron, S.J.3    Thorner, J.4
  • 13
    • 0030835542 scopus 로고    scopus 로고
    • The Uba2 and Ufd1 proteins of Saccharomyces cerevisiae interact with poly(A) polymerase and affect the polyadenylation activity of cell extracts
    • del Olmo, M., N. Mizrahi, S. Gross, and C. L. Moore. 1997. The Uba2 and Ufd1 proteins of Saccharomyces cerevisiae interact with poly(A) polymerase and affect the polyadenylation activity of cell extracts. Mol. Gen. Genet. 255:209-218.
    • (1997) Mol. Gen. Genet. , vol.255 , pp. 209-218
    • Del Olmo, M.1    Mizrahi, N.2    Gross, S.3    Moore, C.L.4
  • 14
    • 0036863611 scopus 로고    scopus 로고
    • A role for SSU72 in balancing RNA polymerase II transcription elongation and termination
    • Dichtl, B., D. Blank, M. Ohnacker, A. Friedlein, D. Roeder, H. Langen, and W. Keller. 2002. A role for SSU72 in balancing RNA polymerase II transcription elongation and termination. Mol. Cell 10:1139-1150.
    • (2002) Mol. Cell , vol.10 , pp. 1139-1150
    • Dichtl, B.1    Blank, D.2    Ohnacker, M.3    Friedlein, A.4    Roeder, D.5    Langen, H.6    Keller, W.7
  • 15
    • 0036682601 scopus 로고    scopus 로고
    • Yhh1p/Cft1p directly links poly(A) site recognition and RNA polymerase II transcription termination
    • Dichtl, B., D. Blank, M. Sadowski, W. Hubner, S. Weiser, and W. Keller. 2002. Yhh1p/Cft1p directly links poly(A) site recognition and RNA polymerase II transcription termination. EMBO J. 21:4125-4135.
    • (2002) EMBO J. , vol.21 , pp. 4125-4135
    • Dichtl, B.1    Blank, D.2    Sadowski, M.3    Hubner, W.4    Weiser, S.5    Keller, W.6
  • 16
    • 0035876112 scopus 로고    scopus 로고
    • Recognition of polyadenylation sites in yeast pre-mRNAs by cleavage and polyadenylation factor
    • Dichtl, B., and W. Keller. 2001. Recognition of polyadenylation sites in yeast pre-mRNAs by cleavage and polyadenylation factor. EMBO J. 20:3197-3209.
    • (2001) EMBO J. , vol.20 , pp. 3197-3209
    • Dichtl, B.1    Keller, W.2
  • 18
    • 0028954118 scopus 로고
    • Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure
    • Gietz, R. D., R. H. Schiestl, A. R. Willems, and R. A. Woods. 1995. Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure. Yeast 11:355-360.
    • (1995) Yeast , vol.11 , pp. 355-360
    • Gietz, R.D.1    Schiestl, R.H.2    Willems, A.R.3    Woods, R.A.4
  • 19
    • 0034282752 scopus 로고    scopus 로고
    • Multiple portions of poly(A)-binding protein stimulate translation in vivo
    • Gray, N. K., J. M. Coller, K. S. Dickson, and M. Wickens. 2000. Multiple portions of poly(A)-binding protein stimulate translation in vivo. EMBO J. 19:4723-4733.
    • (2000) EMBO J. , vol.19 , pp. 4723-4733
    • Gray, N.K.1    Coller, J.M.2    Dickson, K.S.3    Wickens, M.4
  • 20
    • 0035162071 scopus 로고    scopus 로고
    • Rna15 interaction with the A-rich yeast polyadenylation signal is an essential step in mRNA 3′-end formation
    • Gross, S., and C. L. Moore. 2001. Rna15 interaction with the A-rich yeast polyadenylation signal is an essential step in mRNA 3′-end formation. Mol. Cell. Biol. 21:8045-8055.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 8045-8055
    • Gross, S.1    Moore, C.L.2
  • 22
    • 0035000153 scopus 로고    scopus 로고
    • Fip1 regulates the activity of poly(A) polymerase through multiple interactions
    • Helmling, S., A. Zhelkovsky, and C. L. Moore. 2001. Fip1 regulates the activity of poly(A) polymerase through multiple interactions. Mol. Cell. Biol. 21:2026-2037.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2026-2037
    • Helmling, S.1    Zhelkovsky, A.2    Moore, C.L.3
  • 23
    • 0029018708 scopus 로고
    • Identification of a new family of tissue-specific basic helix-loop-helix proteins with a two-hybrid system
    • Hollenberg, S. M., R. Sternglanz, P. F. Cheng, and H. Weintraub. 1995. Identification of a new family of tissue-specific basic helix-loop-helix proteins with a two-hybrid system. Mol. Cell. Biol. 15:3813-3822.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3813-3822
    • Hollenberg, S.M.1    Sternglanz, R.2    Cheng, P.F.3    Weintraub, H.4
  • 24
    • 0002799007 scopus 로고    scopus 로고
    • Poly(A) metabolism and translation: The closed loop model
    • J. W. Hershey, M. B. Mathews, and N. Sonenberg (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Jacobson, A. 1996. Poly(A) metabolism and translation: the closed loop model, p. 451-480. In J. W. Hershey, M. B. Mathews, and N. Sonenberg (ed.), Translational control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1996) Translational Control , pp. 451-480
    • Jacobson, A.1
  • 25
    • 0030455820 scopus 로고    scopus 로고
    • Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast
    • James, P., J. Halladay, and E. A. Craig. 1996. Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast. Genetics 144:1425-1436.
    • (1996) Genetics , vol.144 , pp. 1425-1436
    • James, P.1    Halladay, J.2    Craig, E.A.3
  • 26
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson, E. S., P. C. Ma, I. M. Ota, and A. Varshavsky. 1995. A proteolytic pathway that recognizes ubiquitin as a degradation signal. J. Biol. Chem. 270:17442-17456.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17442-17456
    • Johnson, E.S.1    Ma, P.C.2    Ota, I.M.3    Varshavsky, A.4
  • 27
    • 0025483120 scopus 로고
    • Yeast Saccharomyces cerevisiae selectable markers in pUC18 polylinkers
    • Jones, J. S., and L. Prakash. 1990. Yeast Saccharomyces cerevisiae selectable markers in pUC18 polylinkers. Yeast 6:363-366.
    • (1990) Yeast , vol.6 , pp. 363-366
    • Jones, J.S.1    Prakash, L.2
  • 28
    • 0030913309 scopus 로고    scopus 로고
    • A comparison of mammalian and yeast pre-mRNA 3′-end processing
    • Keller, W., and L. Minvielle-Sebastia. 1997. A comparison of mammalian and yeast pre-mRNA 3′-end processing. Curr. Opin. Cell Biol. 9:329-336.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 329-336
    • Keller, W.1    Minvielle-Sebastia, L.2
  • 29
    • 0030803670 scopus 로고    scopus 로고
    • Hrpl, a sequence-specific RNA-binding protein that shuttles between the nucleus and the cytoplasm, is required for mRNA 3′-end formation in yeast
    • Kessler, M. M., M. F. Henry, E. Shen, J. Zhao, S. Gross, P. A. Silver, and C. L. Moore. 1997. Hrpl, a sequence-specific RNA-binding protein that shuttles between the nucleus and the cytoplasm, is required for mRNA 3′-end formation in yeast. Genes Dev. 11:2545-2556.
    • (1997) Genes Dev. , vol.11 , pp. 2545-2556
    • Kessler, M.M.1    Henry, M.F.2    Shen, E.3    Zhao, J.4    Gross, S.5    Silver, P.A.6    Moore, C.L.7
  • 30
    • 0242380645 scopus 로고    scopus 로고
    • The role of the yeast cleavage and polyadenylation factor subunit Ydh1p/Cft2p in pre-mRNA 3′-end formation
    • Kyburz, A., M. Sadowski, B. Dichtl, and W. Keller. 2003. The role of the yeast cleavage and polyadenylation factor subunit Ydh1p/Cft2p in pre-mRNA 3′-end formation. Nucleic Acids Res. 31:3936-3945.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3936-3945
    • Kyburz, A.1    Sadowski, M.2    Dichtl, B.3    Keller, W.4
  • 31
    • 0026446398 scopus 로고
    • 3′-UTR-dependent deadenylation by the yeast poly(A) nuclease
    • Lowell, J. E., D. Z. Rudner, and A. B. Sachs. 1992. 3′-UTR- dependent deadenylation by the yeast poly(A) nuclease. Genes Dev. 6:2088-2099.
    • (1992) Genes Dev. , vol.6 , pp. 2088-2099
    • Lowell, J.E.1    Rudner, D.Z.2    Sachs, A.B.3
  • 32
    • 0031724595 scopus 로고    scopus 로고
    • Pbp1p, a factor interacting with Saccharomyces cerevisiae poly(A)-binding protein, regulates polyadenylation
    • Mangus, D. A., N. Amrani, and A. Jacobson. 1998. Pbp1p, a factor interacting with Saccharomyces cerevisiae poly(A)-binding protein, regulates polyadenylation. Mol. Cell. Biol. 18:7383-7396.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7383-7396
    • Mangus, D.A.1    Amrani, N.2    Jacobson, A.3
  • 34
    • 0038487811 scopus 로고    scopus 로고
    • Poly(A)-binding proteins: Multifunctional scaffolds for the post-transcriptional control of gene expression
    • Mangus, D. A., M. C. Evans, and A. Jacobson. 2003. Poly(A)-binding proteins: multifunctional scaffolds for the post-transcriptional control of gene expression. Genome Biol. 4:223.1-223.14.
    • (2003) Genome Biol. , vol.4
    • Mangus, D.A.1    Evans, M.C.2    Jacobson, A.3
  • 35
    • 0034602833 scopus 로고    scopus 로고
    • The WD-repeat protein Pfs2p bridges two essential factors within the yeast pre-mRNA 3′-end-processing complex
    • Ohnacker, M., S. M. L. Barabino, P. J. Preker, and W. Keller. 2000. The WD-repeat protein Pfs2p bridges two essential factors within the yeast pre-mRNA 3′-end-processing complex. EMBO J. 19:37-47.
    • (2000) EMBO J. , vol.19 , pp. 37-47
    • Ohnacker, M.1    Barabino, S.M.L.2    Preker, P.J.3    Keller, W.4
  • 36
    • 0028999657 scopus 로고
    • The FIP1 gene encodes a component of a yeast pre-mRNA polyadenylation factor that directly interacts with poly(A) polymerase
    • Preker, P. J., J. Lingner, L. Minvielle-Sebastia, and W. Keller. 1995. The FIP1 gene encodes a component of a yeast pre-mRNA polyadenylation factor that directly interacts with poly(A) polymerase. Cell 81:379-389.
    • (1995) Cell , vol.81 , pp. 379-389
    • Preker, P.J.1    Lingner, J.2    Minvielle-Sebastia, L.3    Keller, W.4
  • 38
    • 0028799704 scopus 로고
    • REF2 encodes an RNA-binding protein directly involved in yeast mRNA 3′-end formation
    • Russnak, R., K. W. Nehrke, and T. Platt. 1995. REF2 encodes an RNA-binding protein directly involved in yeast mRNA 3′-end formation. Mol. Cell. Biol. 15:1689-1697.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1689-1697
    • Russnak, R.1    Nehrke, K.W.2    Platt, T.3
  • 39
    • 0030325199 scopus 로고    scopus 로고
    • RNA binding analysis of yeast REF2 and its two-hybrid interaction with a new gene product, FIR1
    • Russnak, R., S. Pereira, and T. Platt. 1996. RNA binding analysis of yeast REF2 and its two-hybrid interaction with a new gene product, FIR1. Gene Expr. 6:241-258.
    • (1996) Gene Expr. , vol.6 , pp. 241-258
    • Russnak, R.1    Pereira, S.2    Platt, T.3
  • 40
    • 0024416021 scopus 로고
    • The poly(A) binding protein is required for poly(A) shortening and 60S ribosomal subunit-dependent translation initiation
    • Sachs, A. B., and R. W. Davis. 1989. The poly(A) binding protein is required for poly(A) shortening and 60S ribosomal subunit-dependent translation initiation. Cell 58:857-867.
    • (1989) Cell , vol.58 , pp. 857-867
    • Sachs, A.B.1    Davis, R.W.2
  • 43
    • 0027432273 scopus 로고
    • Parameters affecting lithium acetate-mediated transformation of Saccharomyces cerevisiae and development of a rapid and simplified procedure
    • Soni, R., J. P. Carmichael, and J. A. Murray. 1993. Parameters affecting lithium acetate-mediated transformation of Saccharomyces cerevisiae and development of a rapid and simplified procedure. Curr. Genet. 24:455-459.
    • (1993) Curr. Genet. , vol.24 , pp. 455-459
    • Soni, R.1    Carmichael, J.P.2    Murray, J.A.3
  • 44
    • 0037443968 scopus 로고    scopus 로고
    • Functional dissection of the zinc finger and flanking domains of the Yth1 cleavage/polyadenylation factor
    • Tacahashi, Y., S. Helmling, and C. L. Moore. 2003. Functional dissection of the zinc finger and flanking domains of the Yth1 cleavage/polyadenylation factor. Nucleic Acids Res. 31:1744-1752.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 1744-1752
    • Tacahashi, Y.1    Helmling, S.2    Moore, C.L.3
  • 45
    • 0031128205 scopus 로고    scopus 로고
    • Regulation of the mating pheromone and invasive growth responses in yeast by two MAP kinase substrates
    • Tedford, K., S. Kim, D. Sa, K. Stevens, and M. Tyers. 1997. Regulation of the mating pheromone and invasive growth responses in yeast by two MAP kinase substrates. Curr. Biol. 7:228-238.
    • (1997) Curr. Biol. , vol.7 , pp. 228-238
    • Tedford, K.1    Kim, S.2    Sa, D.3    Stevens, K.4    Tyers, M.5
  • 46
    • 0030635047 scopus 로고    scopus 로고
    • The mechanism of 3′ cleavage and polyadenylation of eukaryotic pre-mRNA
    • Wahle, E., and U. Kudie;hn. 1997. The mechanism of 3′ cleavage and polyadenylation of eukaryotic pre-mRNA. Prog. Nucleic Acid Res. Mol. Biol. 57:41-71.
    • (1997) Prog. Nucleic Acid Res. Mol. Biol. , vol.57 , pp. 41-71
    • Wahle, E.1    Kudie2    hn, U.3
  • 48
    • 0033059981 scopus 로고    scopus 로고
    • Formation of mRNA 3′ ends in eukaryotes: Mechanism, regulation, and interrelationships with other steps in mRNA synthesis
    • Zhao, J., L. Hyman, and C. Moore. 1999. Formation of mRNA 3′ ends in eukaryotes: mechanism, regulation, and interrelationships with other steps in mRNA synthesis. Microbiol. Mol. Biol. Rev. 63:405-445.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 405-445
    • Zhao, J.1    Hyman, L.2    Moore, C.3
  • 49
    • 0031658778 scopus 로고    scopus 로고
    • Processivity of the Saccharomyces cerevisiae poly(A) polymerase requires interactions at the carboxyl-terminal RNA binding domain
    • Zhelkovsky, A., S. Helmling, and C. Moore. 1998. Processivity of the Saccharomyces cerevisiae poly(A) polymerase requires interactions at the carboxyl-terminal RNA binding domain. Mol. Cell. Biol. 18:5942-5951.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5942-5951
    • Zhelkovsky, A.1    Helmling, S.2    Moore, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.