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Volumn 15, Issue 10, 1996, Pages 2593-2603

Mutational analysis of mammalian poly(A) polymerase identifies a region for primer binding and a catalytic domain, homologous to the family X polymerases, and to other nucleotidyltransferases

Author keywords

Antibiotic resistance; mRNA 3' end processing; Polymerase; Polymerase module; RNA binding domain

Indexed keywords

DNA DIRECTED DNA POLYMERASE BETA; DNA NUCLEOTIDYLEXOTRANSFERASE; NUCLEOTIDYLTRANSFERASE; POLYNUCLEOTIDE ADENYLYLTRANSFERASE; PRIMER RNA; SIGNAL PEPTIDE;

EID: 0029962371     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1996.tb00617.x     Document Type: Article
Times cited : (169)

References (78)
  • 1
    • 0025130559 scopus 로고
    • Isolation of a temperature-sensitive mutant with an altered tRNA nucleotidyltransferase and cloning of the gene encoding tRNA nucleotidyltransferase in the yeast Saccharomyces cerevisiae
    • Aebi,M., Kirchner,G., Chen,J.-Y., Vijayraghavan,U., Jacobson,A., Martin,N.C. and Abelson,J. (1990) Isolation of a temperature-sensitive mutant with an altered tRNA nucleotidyltransferase and cloning of the gene encoding tRNA nucleotidyltransferase in the yeast Saccharomyces cerevisiae. J. Biol. Chem., 265, 16216-16220.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16216-16220
    • Aebi, M.1    Kirchner, G.2    Chen, J.-Y.3    Vijayraghavan, U.4    Jacobson, A.5    Martin, N.C.6    Abelson, J.7
  • 3
    • 0023756753 scopus 로고
    • A sequence motif in many polymerases
    • Argos,P. (1988) A sequence motif in many polymerases. Nucleic Acids Res., 16, 9909-9916.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 9909-9916
    • Argos, P.1
  • 4
    • 0028947982 scopus 로고
    • Deoxynucleotide triphosphate and pyrophosphate binding sites in the analytically competent ternary complex for the polymerase reaction catalyzed by DNA polymerase I (Klenow fragment)
    • Astatke,M., Grindley,N.D.F. and Joyce,C.M. (1995) Deoxynucleotide triphosphate and pyrophosphate binding sites in the analytically competent ternary complex for the polymerase reaction catalyzed by DNA polymerase I (Klenow fragment). J. Biol. Chem., 270, 1945-1954.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1945-1954
    • Astatke, M.1    Grindley, N.D.F.2    Joyce, C.M.3
  • 5
    • 0027177451 scopus 로고
    • The SWISS-PROT protein sequence databank
    • Bairoch,A. and Boeckmann,B. (1993) The SWISS-PROT protein sequence databank. Nucleic Acids Res., 21, 3093-3096.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 3093-3096
    • Bairoch, A.1    Boeckmann, B.2
  • 6
    • 0029258674 scopus 로고
    • Poly(A) polymerases in the nucleus and cytoplasm of frog oocytes: Dynamic changes during oocyte maturation and early development
    • Ballantyne,S., Bilger,A., Åström,J., Virtanen,A. and Wickens,M. (1995) Poly(A) polymerases in the nucleus and cytoplasm of frog oocytes: dynamic changes during oocyte maturation and early development. RNA, 1, 64-78.
    • (1995) RNA , vol.1 , pp. 64-78
    • Ballantyne, S.1    Bilger, A.2    Åström, J.3    Virtanen, A.4    Wickens, M.5
  • 7
    • 0027730441 scopus 로고
    • Crystal structures of the Klenow fragment of DNA polymerase I complexed with deoxynucleotide triphosphate and pyrophosphate
    • Beese,L.S., Friedmann,J.M. and Steitz,T.A. (1993) Crystal structures of the Klenow fragment of DNA polymerase I complexed with deoxynucleotide triphosphate and pyrophosphate. Biochemistry, 32, 14095-14101.
    • (1993) Biochemistry , vol.32 , pp. 14095-14101
    • Beese, L.S.1    Friedmann, J.M.2    Steitz, T.A.3
  • 8
    • 0026009674 scopus 로고
    • Purification of the cleavage and polyadenylation factor involved in the 3′ processing of messenger RNA precursors
    • Bienroth,S., Wahle,E., Suter-Crazzolara,C. and Keller, W. (1991) Purification of the cleavage and polyadenylation factor involved in the 3′ processing of messenger RNA precursors. J. Biol. Chem., 266, 19768-19776.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19768-19776
    • Bienroth, S.1    Wahle, E.2    Suter-Crazzolara, C.3    Keller, W.4
  • 9
    • 0027439688 scopus 로고
    • Assembly of a processive messenger RNA polyadenylation complex
    • Bienroth,S., Keller,W. and Wahle,E. (1993) Assembly of a processive messenger RNA polyadenylation complex. EMBO J., 12, 585-594.
    • (1993) EMBO J. , vol.12 , pp. 585-594
    • Bienroth, S.1    Keller, W.2    Wahle, E.3
  • 10
    • 0027753933 scopus 로고
    • Analysis of the RNA-recognition motif and RS and RGG domains: Conservation in metazoan pre-mRNA splicing factors
    • Birney,E., Kumar,S. and Krainer,A.R. (1993) Analysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factors. Nucleic Acids Res., 21, 5803-5816.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 5803-5816
    • Birney, E.1    Kumar, S.2    Krainer, A.R.3
  • 11
    • 0026733634 scopus 로고
    • Mutations in T7 RNA polymerase that support the proposal for a common polymerase active site structure
    • Bonner,G., Patra,D., Lafer,E.M. and Sousa,R. (1992) Mutations in T7 RNA polymerase that support the proposal for a common polymerase active site structure. EMBO J., 11, 3767-3775.
    • (1992) EMBO J. , vol.11 , pp. 3767-3775
    • Bonner, G.1    Patra, D.2    Lafer, E.M.3    Sousa, R.4
  • 12
    • 0028129989 scopus 로고
    • Conserved structures and diversity of functions of RNA-binding proteins
    • Burd,C.G. and Dreyfuss,G. (1994) Conserved structures and diversity of functions of RNA-binding proteins. Science, 265, 615-621.
    • (1994) Science , vol.265 , pp. 615-621
    • Burd, C.G.1    Dreyfuss, G.2
  • 13
    • 0026346185 scopus 로고
    • Gel retardation
    • Carey,J. (1991) Gel retardation. Methods Enzymol, 208, 103-117.
    • (1991) Methods Enzymol , vol.208 , pp. 103-117
    • Carey, J.1
  • 14
    • 0024282810 scopus 로고
    • 3′ cleavage and polyadenylation of mRNA precursors in vitro requires a poly(A) polymerase, a cleavage factor, and a snRNP
    • Christofori,G. and Keller,W. (1988) 3′ cleavage and polyadenylation of mRNA precursors in vitro requires a poly(A) polymerase, a cleavage factor, and a snRNP. Cell. 54, 875-889.
    • (1988) Cell , vol.54 , pp. 875-889
    • Christofori, G.1    Keller, W.2
  • 15
    • 0025606431 scopus 로고
    • Molecular cloning and expression of a hexameric Drosaphila heat shock factor subject to negative regulation
    • Clos,J., Westwood,J.T., Becker,B.P., Wilson,S., Lambert,K. and Wu,C. (1990) Molecular cloning and expression of a hexameric Drosaphila heat shock factor subject to negative regulation. Cell. 63, 1085-1097.
    • (1990) Cell , vol.63 , pp. 1085-1097
    • Clos, J.1    Westwood, J.T.2    Becker, B.P.3    Wilson, S.4    Lambert, K.5    Wu, C.6
  • 16
    • 15844377147 scopus 로고    scopus 로고
    • Contreras,A., Drummond,M., Bali,A., Blanco,G., Garcia,E., Bush,G., Kennedy,C. and Merrick,M. (1991) SWISS-PROT accession number: P36223
    • Contreras,A., Drummond,M., Bali,A., Blanco,G., Garcia,E., Bush,G., Kennedy,C. and Merrick,M. (1991) SWISS-PROT accession number: P36223.
  • 17
    • 0023019585 scopus 로고
    • Cloning, sequencing, and species relatedness of the Escherichia coli cca gene encoding the enzyme tRNA nucleotidyltransferase
    • Cudny,H., Lupski,J.R., Godson,G.N. and Deutscher,M.P. (1986) Cloning, sequencing, and species relatedness of the Escherichia coli cca gene encoding the enzyme tRNA nucleotidyltransferase. J. Biol. Chem., 261, 6444-6449.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6444-6449
    • Cudny, H.1    Lupski, J.R.2    Godson, G.N.3    Deutscher, M.P.4
  • 18
    • 0025836159 scopus 로고
    • Aspartic acid residues at positions 190 and 192 of rat DNA polymerase β are involved in primer binding
    • Date,T., Yamamoto,S., Tanihara,K., Nishimoto,Y. and Matsukage,A. (1991) Aspartic acid residues at positions 190 and 192 of rat DNA polymerase β are involved in primer binding. Biochemistry, 30, 5286-5292.
    • (1991) Biochemistry , vol.30 , pp. 5286-5292
    • Date, T.1    Yamamoto, S.2    Tanihara, K.3    Nishimoto, Y.4    Matsukage, A.5
  • 19
    • 0027974928 scopus 로고
    • 2.3 Å crystal structure of the catalytic domain of DNA polymerase β
    • Davies,J.F., Almassy,R.J., Hostomska,Z., Ferre,R.A. and Hostomsky,Z. (1994) 2.3 Å crystal structure of the catalytic domain of DNA polymerase β. Cell. 76, 1123-1133.
    • (1994) Cell , vol.76 , pp. 1123-1133
    • Davies, J.F.1    Almassy, R.J.2    Hostomska, Z.3    Ferre, R.A.4    Hostomsky, Z.5
  • 21
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux,J., Haeberli,P. and Smithies,O. (1984) A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res., 12, 387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 22
    • 0025949412 scopus 로고
    • Nuclear targeting sequences - A consensus?
    • Dingwall,C. and Laskey,R.A. (1991) Nuclear targeting sequences - a consensus? Trends Biochem. Sci., 16, 478-481.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 478-481
    • Dingwall, C.1    Laskey, R.A.2
  • 24
    • 0029112798 scopus 로고
    • Mutational studies of human DNA polymerase α
    • Dong,Q. and Wang,T.S.F. (1995) Mutational studies of human DNA polymerase α. J. Biol. Chem., 270, 21563-21570.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21563-21570
    • Dong, Q.1    Wang, T.S.F.2
  • 25
    • 15844418690 scopus 로고    scopus 로고
    • Ghosh,S.K., Kusari,J., Bandyopadhyay,S.K., Samanta,H., Kumar,R. and Sen,G.C. (1991) SWISS-PROT accession number: P29081
    • Ghosh,S.K., Kusari,J., Bandyopadhyay,S.K., Samanta,H., Kumar,R. and Sen,G.C. (1991) SWISS-PROT accession number: P29081.
  • 26
    • 0027258576 scopus 로고
    • The KH domain occurs in a diverse set of RNA-binding proteins that include the antiterminator NusA and is probably involved in binding to nucleic acid
    • Gibson,T., Thompson,J.D. and Heringa,J. (1993a) The KH domain occurs in a diverse set of RNA-binding proteins that include the antiterminator NusA and is probably involved in binding to nucleic acid. FEBS Lett., 324, 361-366.
    • (1993) FEBS Lett. , vol.324 , pp. 361-366
    • Gibson, T.1    Thompson, J.D.2    Heringa, J.3
  • 27
    • 0027260844 scopus 로고
    • KH domains within the FMR1 sequence suggest that fragile X syndrome stems from a defect in RNA metabolism
    • Gibson,T.J., Rice,P.M., Thompson,J.D. and Heringa,J. (1993b) KH domains within the FMR1 sequence suggest that fragile X syndrome stems from a defect in RNA metabolism. Trends Biochem. Sci., 18, 331-333.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 331-333
    • Gibson, T.J.1    Rice, P.M.2    Thompson, J.D.3    Heringa, J.4
  • 28
  • 29
    • 0028173689 scopus 로고
    • The human U1A snRNP protein regulates polyadenylation via a direct interaction with poly(A) polymerase
    • Gunderson,S.I., Beyer,K., Martin,G., Keller,W., Boelens,W.C. and Mattaj,I.W. (1994) The human U1A snRNP protein regulates polyadenylation via a direct interaction with poly(A) polymerase. Cell, 76, 531-541.
    • (1994) Cell , vol.76 , pp. 531-541
    • Gunderson, S.I.1    Beyer, K.2    Martin, G.3    Keller, W.4    Boelens, W.C.5    Mattaj, I.W.6
  • 30
    • 0019258624 scopus 로고
    • Elution of proteins from sodium dodecyl sulfate-polyacrylamide gels
    • Hager,D.A. and Burgess,R.R. (1980) Elution of proteins from sodium dodecyl sulfate-polyacrylamide gels. Anal. Biochem., 109, 76-86.
    • (1980) Anal. Biochem. , vol.109 , pp. 76-86
    • Hager, D.A.1    Burgess, R.R.2
  • 31
    • 0026861506 scopus 로고
    • The RNP motif protein family
    • Haynes,S.R. (1992) The RNP motif protein family. New Biol., 4, 421-429.
    • (1992) New Biol. , vol.4 , pp. 421-429
    • Haynes, S.R.1
  • 33
    • 0029360327 scopus 로고
    • DNA polymerase β belongs to an ancient nucleotidyltransferase superfamily
    • Holm,L. and Sander,C. (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
  • 34
    • 0025766848 scopus 로고
    • Compilation and alignment of DNA polymerase sequences
    • Ito,J. and Braithwaite,D.K. (1991) Compilation and alignment of DNA polymerase sequences. Nucleic Acids Res., 19, 4045-4057.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4045-4057
    • Ito, J.1    Braithwaite, D.K.2
  • 35
    • 0028206048 scopus 로고
    • Function and structure relationships in DNA polymerases
    • Joyce,C.M. and Steitz,T.A. (1994) Function and structure relationships in DNA polymerases. Annu. Rev. Biochem., 63, 777-822.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 777-822
    • Joyce, C.M.1    Steitz, T.A.2
  • 36
    • 0029069868 scopus 로고
    • No end yet to messenger RNA 3′ processing!
    • Keller,W. (1995) No end yet to messenger RNA 3′ processing! Cell, 81, 829-832.
    • (1995) Cell , vol.81 , pp. 829-832
    • Keller, W.1
  • 37
    • 0026041206 scopus 로고
    • Cleavage and polyadenylation factor CPF specifically interacts with the premRNA 3′ processing signal AAUAAA
    • Keller,W., Bienroth,S., Lang,K.M. and Christofori,G. (1991) Cleavage and polyadenylation factor CPF specifically interacts with the premRNA 3′ processing signal AAUAAA. EMBO J., 10, 4241-4249.
    • (1991) EMBO J. , vol.10 , pp. 4241-4249
    • Keller, W.1    Bienroth, S.2    Lang, K.M.3    Christofori, G.4
  • 38
    • 0025761656 scopus 로고
    • RNA recognition: Towards identifying determinants of specificity
    • Kenan,D.J., Query,C.C. and Keene,J.D. (1991) RNA recognition: towards identifying determinants of specificity. Trends Biochem. Sci., 16, 214-220.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 214-220
    • Kenan, D.J.1    Query, C.C.2    Keene, J.D.3
  • 39
    • 0028983795 scopus 로고
    • Crystal structure of Thermus aquaticus DNA polymerase
    • Kim,Y., Eom,S.H., Wang,J., Lee,D.-S., Suh,S.W. and Steitz,T.A. (1995) Crystal structure of Thermus aquaticus DNA polymerase. Nature, 376, 612-616.
    • (1995) Nature , vol.376 , pp. 612-616
    • Kim, Y.1    Eom, S.H.2    Wang, J.3    Lee, D.-S.4    Suh, S.W.5    Steitz, T.A.6
  • 40
    • 0026693137 scopus 로고
    • Crystal structure at 3.5Å resolution of HIV-1 reverse transcriptase complexed with an inhibitor
    • Kohlstaedt,L.A., Wang,J., Friedmann,J.M., Rice,P.A. and Steitz,T.A. (1992) Crystal structure at 3.5Å resolution of HIV-1 reverse transcriptase complexed with an inhibitor. Science, 256, 1783-1790.
    • (1992) Science , vol.256 , pp. 1783-1790
    • Kohlstaedt, L.A.1    Wang, J.2    Friedmann, J.M.3    Rice, P.A.4    Steitz, T.A.5
  • 41
    • 0029056926 scopus 로고
    • Crystal structure of the large fragment of Thermus aquaticus DNA polymerase I at 2.5-Å resolution: Structural basis for thermostability
    • Korolev,S., Nayal,M., Barnes,W.M., Di Cera,E. and Waksman,G. (1995) Crystal structure of the large fragment of Thermus aquaticus DNA polymerase I at 2.5-Å resolution: Structural basis for thermostability. Proc. Natl Acad. Sci. USA. 92, 9264-9268.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 9264-9268
    • Korolev, S.1    Nayal, M.2    Barnes, W.M.3    Di Cera, E.4    Waksman, G.5
  • 42
    • 0029029232 scopus 로고
    • Nuclear localisation signals overlap DNA- Or RNA-binding domains in nucleic acid-binding proteins
    • LaCasse,E.C. and Lefebvre,Y.A. (1995) Nuclear localisation signals overlap DNA-or RNA-binding domains in nucleic acid-binding proteins. Nucleic Acids Res., 23, 1647-1656.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 1647-1656
    • LaCasse, E.C.1    Lefebvre, Y.A.2
  • 43
    • 15844400578 scopus 로고    scopus 로고
    • Leblanc,D.J., Lee,L.N. and Inamine,J.M. (1991) SWISS-PROT accession number: Q07448
    • Leblanc,D.J., Lee,L.N. and Inamine,J.M. (1991) SWISS-PROT accession number: Q07448.
  • 44
    • 0025787944 scopus 로고
    • Cloning and expression of the essential gene for poly(A) polymerase from S.cerevisiae
    • Lingner,J., Kellerrnann,J. and Keller,W. (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    Kellerrnann, J.2    Keller, W.3
  • 45
    • 0028927051 scopus 로고
    • A complex protein assembly catalyzes polyadenylation of mRNA precursors
    • Manley,J.L. (1995) A complex protein assembly catalyzes polyadenylation of mRNA precursors. Curr. Opin. Genet. Dev., 5, 222-228.
    • (1995) Curr. Opin. Genet. Dev. , vol.5 , pp. 222-228
    • Manley, J.L.1
  • 46
    • 15844412341 scopus 로고
    • UV cross-linking of protein to bromouridine-substituted RNA
    • Jost,J.P. and Saluz,H.P. (eds), Birkhäuser, Basel, Switzerland
    • McEwan,I. (1991) UV cross-linking of protein to bromouridine-substituted RNA In Jost,J.P. and Saluz,H.P. (eds), BioMethods. Birkhäuser, Basel, Switzerland, Vol. 5. pp. 71-80.
    • (1991) BioMethods , vol.5 , pp. 71-80
    • McEwan, I.1
  • 47
    • 0026573580 scopus 로고
    • A general and fast method to generate multiple site directed mutations
    • Mikaelian,I. and Sergeant,A. (1992) A general and fast method to generate multiple site directed mutations. Nucleic Acids Res., 20, 376.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 376
    • Mikaelian, I.1    Sergeant, A.2
  • 48
    • 0028990057 scopus 로고
    • The RNP domain: A sequence-specific RNA-binding domain involved in processing and transport of RNA
    • Nagai,K., Oubridge,C, Ito,N., Avis,J. and Evans,P. (1995) The RNP domain: a sequence-specific RNA-binding domain involved in processing and transport of RNA. Trends Biochem. Sci., 20, 235-240.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 235-240
    • Nagai, K.1    Oubridge, C.2    Ito, N.3    Avis, J.4    Evans, P.5
  • 49
    • 0021992794 scopus 로고
    • Domain of E. coli DNA polymerase I showing sequence homology to T7 DNA polymerase
    • Ollis,D.L., Kline,C. and Steitz,T.A. (1985) Domain of E. coli DNA polymerase I showing sequence homology to T7 DNA polymerase. Nature, 313, 818-819.
    • (1985) Nature , vol.313 , pp. 818-819
    • Ollis, D.L.1    Kline, C.2    Steitz, T.A.3
  • 50
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson,W.R. and Lipman,D.J. (1988) Improved tools for biological sequence comparison. Proc. Natl Acad. Sci. USA, 85, 2444-2448.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 51
    • 0028865333 scopus 로고
    • Structural investigation of the antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase
    • Pedersen,L.C., Benning,M.M. and Holden,H.M. (1995) Structural investigation of the antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase. Biochemistry, 34, 13305-13311.
    • (1995) Biochemistry , vol.34 , pp. 13305-13311
    • Pedersen, L.C.1    Benning, M.M.2    Holden, H.M.3
  • 52
    • 0028049441 scopus 로고
    • Structures of ternary complexes of rat DNA polymerase β, a DNA template-primer and ddCTP
    • Pelletier,H., Sawaya,M.R., Kumar,A., Wilson,S.H. and Kraut,J. (1994) Structures of ternary complexes of rat DNA polymerase β, a DNA template-primer and ddCTP. Science, 264, 1891-1903.
    • (1994) Science , vol.264 , pp. 1891-1903
    • Pelletier, H.1    Sawaya, M.R.2    Kumar, A.3    Wilson, S.H.4    Kraut, J.5
  • 53
    • 0024784519 scopus 로고
    • Identification of four conserved motifs among the RNA-dependent polymerase encoding elements
    • Poch,O., Sauvaget,I., Delarue,M. and Tordo,N. (1989) Identification of four conserved motifs among the RNA-dependent polymerase encoding elements. EMBO J., 8, 3867-3874.
    • (1989) EMBO J. , vol.8 , pp. 3867-3874
    • Poch, O.1    Sauvaget, I.2    Delarue, M.3    Tordo, N.4
  • 54
    • 0025121103 scopus 로고
    • Identificalion of residues critical for the polymerase activity of the Klenow fragment of DNA polymerase I from Escherichia coli
    • Polesky,A.H., Steitz,T.A., Grindley,N.D.F. and Joyce,C.M. (1990) Identificalion of residues critical for the polymerase activity of the Klenow fragment of DNA polymerase I from Escherichia coli. J. Biol. Chem., 265, 14579-14591.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14579-14591
    • Polesky, A.H.1    Steitz, T.A.2    Grindley, N.D.F.3    Joyce, C.M.4
  • 56
    • 0025871846 scopus 로고
    • Primary structure and expression of bovine poly(A) polymerase
    • Raabe,T., Bollum,F.J. and Manley,J.L. (1991) Primary structure and expression of bovine poly(A) polymerase. Nature, 353, 229-234.
    • (1991) Nature , vol.353 , pp. 229-234
    • Raabe, T.1    Bollum, F.J.2    Manley, J.L.3
  • 57
    • 0028209980 scopus 로고
    • Poly(A) polymerase contains multiple functional domains
    • Raabe,T., Murthy,K.G.K. and Manley,J.L. (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
  • 58
    • 0026078249 scopus 로고
    • Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: Identification of a class of bipartite nuclear targeting sequences
    • Robbins,J., Dilworth,S.M., Laskey,R.A. and Dingwall,C. (1991) Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: Identification of a class of bipartite nuclear targeting sequences. Cell, 64, 615-623.
    • (1991) Cell , vol.64 , pp. 615-623
    • Robbins, J.1    Dilworth, S.M.2    Laskey, R.A.3    Dingwall, C.4
  • 59
    • 0027291015 scopus 로고
    • Prediction of protein structure at better than 70% accuracy
    • Rost,B. and Sander,C. (1993) Prediction of protein structure at better than 70% accuracy. J. Mol. Biol., 232, 584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 60
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost,B. and Sander,C. (1994) Combining evolutionary information and neural networks to predict protein secondary structure. Proteins, 19, 55-72.
    • (1994) Proteins , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 61
    • 0027496278 scopus 로고
    • Molecular structure of kanamycin nucleotidyl-transferase determined to 3.0-Å resolution
    • Sakon,J., Liao,H.H., Kanikula,A.M., Benning,M.M., Rayment,I. and Holden,H.M. (1993) Molecular structure of kanamycin nucleotidyl-transferase determined to 3.0-Å resolution. Biochemistry, 32, 11977-11984.
    • (1993) Biochemistry , vol.32 , pp. 11977-11984
    • Sakon, J.1    Liao, H.H.2    Kanikula, A.M.3    Benning, M.M.4    Rayment, I.5    Holden, H.M.6
  • 62
    • 0028136070 scopus 로고
    • Crystal structure of rat DNA polymerase β: Evidence for a common polymerase mechanism
    • Sawaya,M.R., Pelletier,H., Kumar,A., Wilson,S.H. and Kraut,J. (1994) Crystal structure of rat DNA polymerase β: evidence for a common polymerase mechanism. Science, 264, 1930-1935.
    • (1994) Science , vol.264 , pp. 1930-1935
    • Sawaya, M.R.1    Pelletier, H.2    Kumar, A.3    Wilson, S.H.4    Kraut, J.5
  • 63
    • 0027478123 scopus 로고
    • Molecular genetics of aminoglycoside resistance genes and familial relationships of the aminoglycoside-modifying enzymes
    • Shaw,K.J., Rather,P.N., Hare,R.S. and Miller,G.H. (1993) Molecular genetics of aminoglycoside resistance genes and familial relationships of the aminoglycoside-modifying enzymes. Microbiol. Rev., 57, 138-163.
    • (1993) Microbiol. Rev. , vol.57 , pp. 138-163
    • Shaw, K.J.1    Rather, P.N.2    Hare, R.S.3    Miller, G.H.4
  • 64
    • 0027163526 scopus 로고
    • Crystal structure of bacteriophage T7 RNA polymerase at 3.3 Å resolution
    • Sousa,R., Chung,Y.J., Rose,J.P. and Wang,B. (1993) Crystal structure of bacteriophage T7 RNA polymerase at 3.3 Å resolution. Nature, 364, 593-599.
    • (1993) Nature , vol.364 , pp. 593-599
    • Sousa, R.1    Chung, Y.J.2    Rose, J.P.3    Wang, B.4
  • 65
    • 15844424588 scopus 로고    scopus 로고
    • Steglitz-Moersdorf,U., Moersdorf,G. and Kaltwasser,H. (1993) SWISS-PROT accession number: P28786
    • Steglitz-Moersdorf,U., Moersdorf,G. and Kaltwasser,H. (1993) SWISS-PROT accession number: P28786.
  • 66
    • 0004876612 scopus 로고
    • Qualitative and quantitative studies of protein-DNA interactions by gel mobility-shift assay
    • Jost,J.-P. and Saluz,H.P. (eds), Birkhäuser, Basel, Switzerland
    • Stone,S.R., Hughes,M.J. and Jost,J.-P. (1991) Qualitative and quantitative studies of protein-DNA interactions by gel mobility-shift assay In Jost,J.-P. and Saluz,H.P. (eds), BioMethods. Birkhäuser, Basel, Switzerland, Vol. 5, pp. 163-194.
    • (1991) BioMethods , vol.5 , pp. 163-194
    • Stone, S.R.1    Hughes, M.J.2    Jost, J.-P.3
  • 69
    • 0025817865 scopus 로고
    • A novel poly(A)-binding protein acts as a specificity factor in the second phase of messenger RNA polyadenylation
    • Wahle,E. (1991a) A novel poly(A)-binding protein acts as a specificity factor in the second phase of messenger RNA polyadenylation. Cell, 66, 759-768.
    • (1991) Cell , vol.66 , pp. 759-768
    • Wahle, E.1
  • 70
    • 0025907963 scopus 로고
    • Purification and characterization of a mammalian polyadenylate polymerase involved in the 3′ end processing of messenger RNA precursors
    • Wahle,E. (1991b) Purification and characterization of a mammalian polyadenylate 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
  • 71
    • 0028988016 scopus 로고
    • 3′-end cleavage and polyadenylation of mRNA precursors
    • Wahle,E. (1995) 3′-end cleavage and polyadenylation of mRNA precursors. Biochim. Biophys. Acta, 1261, 183-194.
    • (1995) Biochim. Biophys. Acta , vol.1261 , pp. 183-194
    • Wahle, E.1
  • 72
    • 0025987814 scopus 로고
    • Isolation and expression of cDNA clones encoding mammalian poly(A) polymerase
    • Wahle,E., Martin,G., Schiltz,E. and Keller,W. (1991) Isolation and expression of cDNA clones encoding mammalian poly(A) polymerase. EMBO J., 10, 4251-4257.
    • (1991) EMBO J. , vol.10 , pp. 4251-4257
    • Wahle, E.1    Martin, G.2    Schiltz, E.3    Keller, W.4
  • 74
    • 0002889930 scopus 로고
    • 'Resistance transfer factor' an episome in enterobacteriaceae
    • Watanabe,T. and Fukasawa,T. (1960) 'Resistance transfer factor' an episome in enterobacteriaceae. Biochem. Biophys. Res. Commun., 3, 660-665.
    • (1960) Biochem. Biophys. Res. Commun. , vol.3 , pp. 660-665
    • Watanabe, T.1    Fukasawa, T.2
  • 75
    • 0028295681 scopus 로고
    • The C.elegans genome project: Contiguous nucleotide sequence of over two megabases from chromosome III
    • Wilson,R. et al. (1994) The C.elegans genome project: Contiguous nucleotide sequence of over two megabases from chromosome III. Nature, 368, 32-38.
    • (1994) Nature , vol.368 , pp. 32-38
    • Wilson, R.1
  • 76
    • 0029643952 scopus 로고
    • Recombining the structures of HIV integrase, RuvC and RNase H
    • Yang,W. and Steitz,T.A. (1995) Recombining the structures of HIV integrase, RuvC and RNase H. Structure, 3, 131-134.
    • (1995) Structure , vol.3 , pp. 131-134
    • Yang, W.1    Steitz, T.A.2
  • 77
    • 15844380660 scopus 로고    scopus 로고
    • Zhao,W.W. and Manley,J.J. (1993) EMBL data library accession number: L22658
    • Zhao,W.W. and Manley,J.J. (1993) EMBL data library accession number: L22658.
  • 78
    • 0028881786 scopus 로고
    • Structure-function relationships in the Saccharomyces cerevisiae poly(A) polymerase
    • Zhelkovsky,A.M., Kessler,M.M. and Moore,C.L. (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


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