메뉴 건너뛰기




Volumn 18, Issue 10, 1998, Pages 5942-5951

Processivity of the Saccharomyces cerevisiae poly(A) polymerase requires interactions at the carboxyl-terminal RNA binding domain

Author keywords

[No Author keywords available]

Indexed keywords

POLYNUCLEOTIDE ADENYLYLTRANSFERASE;

EID: 0031658778     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.18.10.5942     Document Type: Article
Times cited : (44)

References (36)
  • 1
    • 0031011852 scopus 로고    scopus 로고
    • Yeast Pabl interacts with Rna15 and participates in the control of the poly(A) tail length in vitro
    • Amrani, N., M. Minet, M. Le Gouar, F. Lacrouite, and F. Wyers. 1997. Yeast Pabl 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    Lacrouite, F.4    Wyers, F.5
  • 2
    • 1842329727 scopus 로고    scopus 로고
    • The 30-kD subunit of mammalian cleavage and polyadenylation specificity factor and its yeast homolog are RNA-binding zinc finger proteins
    • Barabino, S., W. Hubner, A. Jenny, L. Minvielle-Sebastia, and W. Keller, 1997. The 30-kD subunit of mammalian cleavage and polyadenylation specificity factor and its yeast homolog are RNA-binding zinc finger proteins. Genes Dev. 11:1703-1716.
    • (1997) Genes Dev. , vol.11 , pp. 1703-1716
    • Barabino, S.1    Hubner, W.2    Jenny, A.3    Minvielle-Sebastia, L.4    Keller, W.5
  • 3
    • 0029126514 scopus 로고
    • Analyzing protein-protein interactions using two-hybrid system
    • Bartel, P., and S. Fields. 1995. Analyzing protein-protein interactions using two-hybrid system. Methods Enzymol. 254:241-263.
    • (1995) Methods Enzymol. , vol.254 , pp. 241-263
    • Bartel, P.1    Fields, S.2
  • 4
    • 0026656539 scopus 로고
    • Separation of factors required for cleavage and polyadenylation of yeast pre-mRNA
    • Chen, J., and C. Moore. 1992. Separation of factors required for cleavage and polyadenylation of yeast pre-mRNA. Mol. Cell. Biol. 12:3470-3481.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3470-3481
    • Chen, J.1    Moore, C.2
  • 5
    • 0029857320 scopus 로고    scopus 로고
    • Cell-cycle related regulation of poly(A) polymerase by phosphorylation
    • Colgan, D., K. Murthy, C. Prives, and J. Manley. 1996. Cell-cycle related regulation of poly(A) polymerase by phosphorylation. Nature 384:282-285.
    • (1996) Nature , vol.384 , pp. 282-285
    • Colgan, D.1    Murthy, K.2    Prives, C.3    Manley, J.4
  • 7
    • 0024266139 scopus 로고
    • New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Gietz, R., and A. Sugino. 1988. New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 74:527-534.
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.1    Sugino, A.2
  • 8
    • 0031610367 scopus 로고    scopus 로고
    • U1 snRNP inhibits pre-mRNA polyadenylation through a direct interaction between U170K and poly(A) polymerase
    • Gunderson, S., M. Polycarpou-Schwarz, and I. Mattaj. 1998. U1 snRNP inhibits pre-mRNA polyadenylation through a direct interaction between U170K and poly(A) polymerase. Mol. Cell 1:255-264.
    • (1998) Mol. Cell , vol.1 , pp. 255-264
    • Gunderson, S.1    Polycarpou-Schwarz, M.2    Mattaj, I.3
  • 9
    • 0031004560 scopus 로고    scopus 로고
    • Involvement of the carboxyl terminus of vertebrate poly(A) polymerase in U1A autoregulation and in the coupling of splicing and polyadenylation
    • Gunderson, S., S. Vagner, M. Poly carpou-Schwarz, and I. Mattaj. 1997. Involvement of the carboxyl terminus of vertebrate poly(A) polymerase in U1A autoregulation and in the coupling of splicing and polyadenylation. Genes Dev. 11:761-773.
    • (1997) Genes Dev. , vol.11 , pp. 761-773
    • Gunderson, S.1    Vagner, S.2    Carpou-Schwarz, M.P.3    Mattaj, I.4
  • 10
    • 0016607411 scopus 로고
    • The polyadenylate polymerases from yeast
    • Haff, L., and E. Keller. 1975. The polyadenylate polymerases from yeast. J. Biol. Chem. 250:1838-1846.
    • (1975) J. Biol. Chem. , vol.250 , pp. 1838-1846
    • Haff, L.1    Keller, E.2
  • 11
    • 0029360327 scopus 로고
    • DNA polymerase β belongs to an ancient nucleotidyltransferase superfamily
    • Holm, L., and C. Sander. 1995. DNA polymerase β belongs to an ancient nucleotidyltransferase superfamily. Trends Biochem. Sci. 20:345-347.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 345-347
    • Holm, L.1    Sander, C.2
  • 12
    • 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
  • 14
    • 0016689711 scopus 로고
    • Poly(A) polymerase of bovine lymphosarcoma
    • Keshgegian, A. A., S. M. Meltzer, and J. J. Furth. 1975. Poly(A) polymerase of bovine lymphosarcoma. Cancer Res. 35:1141-1146.
    • (1975) Cancer Res. , vol.35 , pp. 1141-1146
    • Keshgegian, A.A.1    Meltzer, S.M.2    Furth, J.J.3
  • 15
    • 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. Henry, S. Gross, E. Shen, J. Zhao, P. Silver, and C. 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.1    Henry, M.2    Gross, S.3    Shen, E.4    Zhao, J.5    Silver, P.6    Moore, C.7
  • 16
    • 0029910068 scopus 로고    scopus 로고
    • Purification of the Saccharomyces cerevisiae cleavage/polyadenylation factor I
    • Kessler, M. M., J. Zhao, and C. L. Moore. 1996. Purification of the Saccharomyces cerevisiae cleavage/polyadenylation factor I. J. Biol. Chem. 271:27167-27175.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27167-27175
    • Kessler, M.M.1    Zhao, J.2    Moore, C.L.3
  • 17
    • 0027250384 scopus 로고
    • 3′-end labeling of RNA with recombinant yeast poly(A) polymerase
    • Lingner, J., and W. Keller. 1993. 3′-end labeling of RNA with recombinant yeast poly(A) polymerase. Nucleic Acids Res. 21:2917-2920.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 2917-2920
    • Lingner, J.1    Keller, W.2
  • 18
    • 0025787944 scopus 로고
    • Cloning and expression of the essential gene for poly(A) polymerase from S. cerevisiae
    • Lingner, J., J. Kellermann, and W. Keller. 1991. Cloning and expression of the essential gene for poly(A) polymerase from S. cerevisiae. Nature 354:496-498.
    • (1991) Nature , vol.354 , pp. 496-498
    • Lingner, J.1    Kellermann, J.2    Keller, W.3
  • 19
    • 0025912305 scopus 로고
    • Purification and characterization of poly(A) polymerase from Saccharomyces cerevisiae
    • Lingner, J., I. Radtke, E. Wahle, and W. Keller. 1991. Purification and characterization of poly(A) polymerase from Saccharomyces cerevisiae. J. Biol. Chem. 266:8741-8746.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8741-8746
    • Lingner, J.1    Radtke, I.2    Wahle, E.3    Keller, W.4
  • 20
    • 0028867277 scopus 로고
    • Effects of mutations in the Saccharomyces cerevisiae RNA14, RNA15, and PAP1 genes on polyadenylation in vivo
    • Mandart, E., and R. Parker. 1995. Effects of mutations in the Saccharomyces cerevisiae RNA14, RNA15, and PAP1 genes on polyadenylation in vivo. Mol Cell. Biol. 15:6979-6986.
    • (1995) Mol Cell. Biol. , vol.15 , pp. 6979-6986
    • Mandart, E.1    Parker, R.2
  • 21
    • 0029962371 scopus 로고    scopus 로고
    • Mutational analysis of mammalian poly(A) polymerase identifies a region for primer binding and a catalytic domain, homologous to the family χ polymerases and to other nucleotidyltrans-ferases
    • Martin, G., and W. Keller. 1996. Mutational analysis of mammalian poly(A) polymerase identifies a region for primer binding and a catalytic domain, homologous to the family χ polymerases and to other nucleotidyltrans-ferases. EMBO J. 15:2593-2603.
    • (1996) EMBO J. , vol.15 , pp. 2593-2603
    • Martin, G.1    Keller, W.2
  • 22
    • 0031915525 scopus 로고    scopus 로고
    • Tailing and 3′-end labeling of RNA with yeast poly(A) polymerase and various nucleotides
    • Martin, G., and W. Keller. 1998. Tailing and 3′-end labeling of RNA with yeast poly(A) polymerase and various nucleotides. RNA 4:226-230.
    • (1998) RNA , vol.4 , pp. 226-230
    • Martin, G.1    Keller, W.2
  • 23
    • 0030800231 scopus 로고    scopus 로고
    • The major yeast poly(A)-binding protein is associated with cleavage factor IA and functions in premessenger RNA 3′-end formation
    • Minvielle-Sebastia, L., P. Preker, T. Wiederkehr, Y. Strahm, and W. Keller. 1997. The major yeast poly(A)-binding protein is associated with cleavage factor IA and functions in premessenger RNA 3′-end formation. Proc. Natl. Acad. Sci. USA 94:7897-7902.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7897-7902
    • Minvielle-Sebastia, L.1    Preker, P.2    Wiederkehr, T.3    Strahm, Y.4    Keller, W.5
  • 24
    • 0028789410 scopus 로고
    • The 160 kD subunit of human cleavage-polyadenylation specificity factor coordinates pre-mRNA 3′ end formation
    • Murthy, K. G. K., and J. L. Manley. 1995. The 160 kD subunit of human cleavage-polyadenylation specificity factor coordinates pre-mRNA 3′ end formation. Genes Dev. 9:2672-2683.
    • (1995) Genes Dev. , vol.9 , pp. 2672-2683
    • Murthy, K.G.K.1    Manley, J.L.2
  • 25
    • 0030789421 scopus 로고    scopus 로고
    • A multisubunit 3′ end processing factor from yeast containing poly(A) poly-merase and homologues of the subunits of mammalian cleavage and poly-adenylation specificity factor
    • Preker, P., M. Ohnacker, L. Minvielle-Sebastia, and W. Keller. 1997. A multisubunit 3′ end processing factor from yeast containing poly(A) poly-merase and homologues of the subunits of mammalian cleavage and poly-adenylation specificity factor. EMBO J. 16:4727-4737.
    • (1997) EMBO J. , vol.16 , pp. 4727-4737
    • Preker, P.1    Ohnacker, M.2    Minvielle-Sebastia, L.3    Keller, W.4
  • 26
    • 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
  • 27
    • 0028209980 scopus 로고
    • Poly(A) polymerase contains multiple functional domains
    • Raabe, T., K. G. K. Murthy, and J. L. Manley. 1994. Poly(A) polymerase contains multiple functional domains. Mol. Cell. Biol. 14:2946-2957.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2946-2957
    • Raabe, T.1    Murthy, K.G.K.2    Manley, J.L.3
  • 28
    • 0015223458 scopus 로고
    • Enzymic synthesis of ribonucleotide terminated oligodeoxynucleotides and their use as primers for the enzymic synthesis of polydeoxynucleotides
    • Roychoudhury, R., and H. Kossel. 1971. Enzymic synthesis of ribonucleotide terminated oligodeoxynucleotides and their use as primers for the enzymic synthesis of polydeoxynucleotides. Eur. J. Biochem. 22:310-320.
    • (1971) Eur. J. Biochem. , vol.22 , pp. 310-320
    • Roychoudhury, R.1    Kossel, H.2
  • 29
    • 0023053585 scopus 로고
    • A single gene from yeast for both nuclear and cytoplasmic polyadenylate-binding proteins: Domain structure and expression
    • Sachs, A., M. Bond, and R. Kornberg. 1986. A single gene from yeast for both nuclear and cytoplasmic polyadenylate-binding proteins: domain structure and expression. Cell 45:827-835.
    • (1986) Cell , vol.45 , pp. 827-835
    • Sachs, A.1    Bond, M.2    Kornberg, R.3
  • 30
    • 0029881023 scopus 로고    scopus 로고
    • Structural and mechanistic relationships between nucleic acid polymerases
    • Sousa, R. 1996. Structural and mechanistic relationships between nucleic acid polymerases. Trends Biochem. Sci. 21:186-191.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 186-191
    • Sousa, R.1
  • 31
    • 0028869677 scopus 로고
    • Use of vaccinia virus poly(A) polymerase for RNA 3′-end labeling with a chain-terminating nucleotide or a short 3′ homopolymer tract
    • Thomson, J., and P. Gershon. 1995. Use of vaccinia virus poly(A) polymerase for RNA 3′-end labeling with a chain-terminating nucleotide or a short 3′ homopolymer tract. BioTechniques 19:416-425.
    • (1995) BioTechniques , vol.19 , pp. 416-425
    • Thomson, J.1    Gershon, P.2
  • 32
  • 33
    • 0025907963 scopus 로고
    • Purification and characterization of a mammalian polyade- Nylate polymerase involved in the 3′ end processing of messenger RNA precursors
    • Wahle, E. 1991. Purification and characterization of a mammalian polyade- nylate polymerase involved in the 3′ end processing of messenger RNA precursors. J. Biol. Chem. 266:3131-3139.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3131-3139
    • Wahle, E.1
  • 34
    • 0030635047 scopus 로고    scopus 로고
    • The mechanism of 3′ cleavage and polyadenylation of eukaryotic pre-mRNA
    • Wahle, E., and U. Kuhn. 1997. The mechanism of 3′ cleavage and polyadenylation of eukaryotic pre-mRNA. Prog. Nucleic Acid Res. Mol. Biol. 57:41-70.
    • (1997) Prog. Nucleic Acid Res. Mol. Biol. , vol.57 , pp. 41-70
    • Wahle, E.1    Kuhn, U.2
  • 35
    • 0031588978 scopus 로고    scopus 로고
    • Purification and characterization of full-length mammalian poly(A) polymerase
    • Wittmann, T., and E. Wahle. 1997. Purification and characterization of full-length mammalian poly(A) polymerase. Biochim. Biophys. Acta 1350:293-305.
    • (1997) Biochim. Biophys. Acta , vol.1350 , pp. 293-305
    • Wittmann, T.1    Wahle, E.2
  • 36
    • 0028881786 scopus 로고
    • Structure-function relationships in the Saccharomyces cerevisiae poly(A) polymerase
    • Zhelkovsky, A. M., M. M. Kessler, and C. L. Moore. 1995. Structure-function relationships in the Saccharomyces cerevisiae poly(A) polymerase. J. Biol. Chem. 270:26715-26720.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26715-26720
    • Zhelkovsky, A.M.1    Kessler, M.M.2    Moore, C.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.