메뉴 건너뛰기




Volumn 32, Issue 2, 2003, Pages 202-209

Overexpression and purification of untagged polynucleotide phosphorylases

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; STREPTOMYCES; STREPTOMYCES ANTIBIOTICUS; STREPTOMYCES COELICOLOR;

EID: 0346305936     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2003.08.005     Document Type: Article
Times cited : (16)

References (37)
  • 1
    • 0001719080 scopus 로고
    • Enzymatic synthesis and breakdown of polynucleotides: Polynucleotide phosphorylase
    • M. Grunberg-Manago, S. Ochoa, Enzymatic synthesis and breakdown of polynucleotides: polynucleotide phosphorylase, J. Am. Chem. Soc. 77 (1955) 3165-3166.
    • (1955) J. Am. Chem. Soc. , vol.77 , pp. 3165-3166
    • Grunberg-Manago, M.1    Ochoa, S.2
  • 3
    • 77956896894 scopus 로고
    • Polynucleotide phosphorylase
    • U.Z. Littauer, H. Soreq, Polynucleotide phosphorylase, The Enzymes 15 (1982) 517-553.
    • (1982) The Enzymes , vol.15 , pp. 517-553
    • Littauer, U.Z.1    Soreq, H.2
  • 4
    • 0032617132 scopus 로고    scopus 로고
    • Degradation of mRNA in Escherichia coli: An old problem with some new twists
    • G.A. Coburn, G.A. Mackie, Degradation of mRNA in Escherichia coli: an old problem with some new twists, Prog. Nucl. Acids Res. Mol. Biol. 62 (1999) 55-105.
    • (1999) Prog. Nucl. Acids Res. Mol. Biol. , vol.62 , pp. 55-105
    • Coburn, G.A.1    Mackie, G.A.2
  • 5
    • 0032939521 scopus 로고    scopus 로고
    • mRNA degradation in bacteria
    • R. Rauhut, G. Klug, mRNA degradation in bacteria, FEMS Microbiol. Rev. 23 (1999) 353-370.
    • (1999) FEMS Microbiol. Rev. , vol.23 , pp. 353-370
    • Rauhut, R.1    Klug, G.2
  • 6
    • 0242400018 scopus 로고    scopus 로고
    • Degradation of mRNA in bacteria: Emergence of ubiquitous features
    • P. Régnier, C.M. Arraiano, Degradation of mRNA in bacteria: emergence of ubiquitous features, Bioessays 22 (2000) 235-244.
    • (2000) Bioessays , vol.22 , pp. 235-244
    • Régnier, P.1    Arraiano, C.M.2
  • 7
    • 0035283033 scopus 로고    scopus 로고
    • Exoribonuclease superfamilies: Structural analysis and phylogenetic distribution
    • Y. Zuo, M. Deutscher, Exoribonuclease superfamilies: structural analysis and phylogenetic distribution, Nucl. Acids Res. 29 (2001) 1017-1026.
    • (2001) Nucl. Acids Res. , vol.29 , pp. 1017-1026
    • Zuo, Y.1    Deutscher, M.2
  • 8
    • 0029828944 scopus 로고    scopus 로고
    • Addition of destabilizing poly(A) rich sequences to endonuclease cleavage sites during the degradation of chloroplast RNA
    • I. Lisitsky, P. Klaff, G. Schuster, Addition of destabilizing poly(A) rich sequences to endonuclease cleavage sites during the degradation of chloroplast RNA, Proc. Natl. Acad. Sci. USA 93 (1996) 13398-13403.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13398-13403
    • Lisitsky, I.1    Klaff, P.2    Schuster, G.3
  • 9
    • 0034934778 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase functions as both an exonuclease and a poly(A) polymerase in spinach chloroplasts
    • S. Yehudai-Resheff, M. Hirsh, G. Schuster, Polynucleotide phosphorylase functions as both an exonuclease and a poly(A) polymerase in spinach chloroplasts, Mol. Cell. Biol. 21 (2001) 5408-5416.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5408-5416
    • Yehudai-Resheff, S.1    Hirsh, M.2    Schuster, G.3
  • 10
    • 0027945686 scopus 로고
    • A protein complex that mediates mRNA degradation in Escherichia coli
    • B. Py, C.F. Causton, E.A. Mudd, C.F. Higgins, A protein complex that mediates mRNA degradation in Escherichia coli, Mol. Microbiol. 14 (1994) 717-729.
    • (1994) Mol. Microbiol. , vol.14 , pp. 717-729
    • Py, B.1    Causton, C.F.2    Mudd, E.A.3    Higgins, C.F.4
  • 11
    • 0029922992 scopus 로고    scopus 로고
    • A DEAD-box RNA helicase in the Escherichia coli RNA degradosome
    • B. Py, C.F. Higgins, H.M. Krisch, A.J. Carpousis, A DEAD-box RNA helicase in the Escherichia coli RNA degradosome, Nature 381 (1996) 169-172.
    • (1996) Nature , vol.381 , pp. 169-172
    • Py, B.1    Higgins, C.F.2    Krisch, H.M.3    Carpousis, A.J.4
  • 12
    • 0014429037 scopus 로고
    • Purification and properties of polynucleotide phosphorylase from Escherichia coli
    • Y. Kimhi, U.Z. Littauer, Purification and properties of polynucleotide phosphorylase from Escherichia coli, J. Biol. Chem. 243 (1968) 231-240.
    • (1968) J. Biol. Chem. , vol.243 , pp. 231-240
    • Kimhi, Y.1    Littauer, U.Z.2
  • 14
    • 0032531768 scopus 로고    scopus 로고
    • Ribonuclease E is a 5′-end-dependent endonuclease
    • G.A. Mackie, Ribonuclease E is a 5′-end-dependent endonuclease, Nature 295 (1998) 720-723.
    • (1998) Nature , vol.295 , pp. 720-723
    • Mackie, G.A.1
  • 15
    • 0028272880 scopus 로고
    • Purification and properties of ATP:GTP 3′-pyrophosphotransferase (guanosine pentaphosphate synthetase) from Streptomyces antibioticus
    • G.H. Jones, Purification and properties of ATP:GTP 3′- pyrophosphotransferase (guanosine pentaphosphate synthetase) from Streptomyces antibioticus, J. Bacteriol. 176 (1994) 1475-1481.
    • (1994) J. Bacteriol. , vol.176 , pp. 1475-1481
    • Jones, G.H.1
  • 16
    • 0028324042 scopus 로고
    • Activation of ATP-GTP 3′-pyrophosphotransferase (guanosine pentaphosphate synthetase) in Streptomyces antibioticus
    • G.H. Jones, Activation of ATP-GTP 3′-pyrophosphotransferase (guanosine pentaphosphate synthetase) in Streptomyces antibioticus, J. Bacteriol. 176 (1994) 1482-1487.
    • (1994) J. Bacteriol. , vol.176 , pp. 1482-1487
    • Jones, G.H.1
  • 17
    • 0003174053 scopus 로고    scopus 로고
    • The stringent response
    • F.C. Neidhardt, R. Curtiss III, J.L. Ingraham, E.C.C. Lin, K.B. Low, B. Magasanik, W.S. Reznikoff, M. Riley. M. Schaechter, H.E. Umbarger (Eds.), ASM Press, Washington, DC
    • M. Cashel, D.R. Gentry, V.J. Hernandez, D. Vinella, The stringent response. In: F.C. Neidhardt, R. Curtiss III, J.L. Ingraham, E.C.C. Lin, K.B. Low, B. Magasanik, W.S. Reznikoff, M. Riley. M. Schaechter, H.E. Umbarger (Eds.), Escherichia coli and Salmonella: Cellular and Molecular Biology. ASM Press, Washington, DC, 1996, pp. 1458-1496.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , pp. 1458-1496
    • Cashel, M.1    Gentry, D.R.2    Hernandez, V.J.3    Vinella, D.4
  • 18
    • 0030922782 scopus 로고    scopus 로고
    • The ppGpp synthetase gene (relA) of Streptomyces coelicolor A3(2) plays a conditional role in antibiotic production and morphological differentiation
    • R. Chakraburtty, M.J. Bibb, The ppGpp synthetase gene (relA) of Streptomyces coelicolor A3(2) plays a conditional role in antibiotic production and morphological differentiation, J. Bacteriol. 179 (1997) 5854-5864.
    • (1997) J. Bacteriol. , vol.179 , pp. 5854-5864
    • Chakraburtty, R.1    Bibb, M.J.2
  • 19
    • 0033053011 scopus 로고    scopus 로고
    • relA is required for actinomycin production in Streptomyces antibioticus
    • S. Hoyt, G.H. Jones, relA is required for actinomycin production in Streptomyces antibioticus, J. Bacteriol. 181 (1999) 3824-3829.
    • (1999) J. Bacteriol. , vol.181 , pp. 3824-3829
    • Hoyt, S.1    Jones, G.H.2
  • 20
    • 0034435974 scopus 로고    scopus 로고
    • A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity and regulation
    • M. Symmons, G.H. Jones, B. Luisi, A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity and regulation. Structure 8 (2000) 1215-1226.
    • (2000) Structure , vol.8 , pp. 1215-1226
    • Symmons, M.1    Jones, G.H.2    Luisi, B.3
  • 22
    • 0038687705 scopus 로고    scopus 로고
    • A Streptomyces coelicolor functional orthologue of Escherichia coli RNase E shows evolutionary shuffling of catalytic and PNPase-binding domains
    • K. Lee, S.N. Cohen, A Streptomyces coelicolor functional orthologue of Escherichia coli RNase E shows evolutionary shuffling of catalytic and PNPase-binding domains, Mol. Microbiol. 48 (2003) 349-360.
    • (2003) Mol. Microbiol. , vol.48 , pp. 349-360
    • Lee, K.1    Cohen, S.N.2
  • 23
    • 0029854299 scopus 로고    scopus 로고
    • Polyadenylation of mRNA in bacteria
    • N. Sarkar, Polyadenylation of mRNA in bacteria, Microbiology UK 142 (1996) 3125-3133.
    • (1996) Microbiology UK , vol.142 , pp. 3125-3133
    • Sarkar, N.1
  • 24
    • 0031009317 scopus 로고    scopus 로고
    • Polyadenylation of mRNA in prokaryotes
    • N. Sarkar, Polyadenylation of mRNA in prokaryotes, Ann. Rev. Biochem. 66 (1997) 173-197.
    • (1997) Ann. Rev. Biochem. , vol.66 , pp. 173-197
    • Sarkar, N.1
  • 25
    • 0036267108 scopus 로고    scopus 로고
    • cDNA cloning confirms the polyadenylation of RNA decay intermediates in Streptomyces coelicolor
    • P. Bralley, G.H. Jones, cDNA cloning confirms the polyadenylation of RNA decay intermediates in Streptomyces coelicolor, Microbiology UK 148 (2002) 1421-1425.
    • (2002) Microbiology UK , vol.148 , pp. 1421-1425
    • Bralley, P.1    Jones, G.H.2
  • 26
    • 0038182527 scopus 로고    scopus 로고
    • RNA polyadenylation and degradation in cyanobacteria are similar to the chloroplast but different from E. coli
    • R. Rott, G. Zipor, V. Portnoy, V. Liveanu, G. Schuster, RNA polyadenylation and degradation in cyanobacteria are similar to the chloroplast but different from E. coli, J. Biol. Chem. 278 (2003) 15771-15777.
    • (2003) J. Biol. Chem. , vol.278 , pp. 15771-15777
    • Rott, R.1    Zipor, G.2    Portnoy, V.3    Liveanu, V.4    Schuster, G.5
  • 27
    • 0034710943 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase functions both as a 3′-5′ exonuclease and a poly(A) polymerase in Escherichia coli
    • B.K. Mohanty, S.R. Kushner, Polynucleotide phosphorylase functions both as a 3′-5′ exonuclease and a poly(A) polymerase in Escherichia coli, Proc. Natl. Acad. Sci. USA 97 (2000) 11966-11971.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11966-11971
    • Mohanty, B.K.1    Kushner, S.R.2
  • 28
    • 0034978592 scopus 로고    scopus 로고
    • Poly(A) polymerase activity and RNA polyadenylation in Streptomyces coelicolor A3(2)
    • P. Bralley, G.H. Jones, Poly(A) polymerase activity and RNA polyadenylation in Streptomyces coelicolor A3(2), Mol. Microbiol. 40 (2001) 1155-1164.
    • (2001) Mol. Microbiol. , vol.40 , pp. 1155-1164
    • Bralley, P.1    Jones, G.H.2
  • 29
    • 0029974966 scopus 로고    scopus 로고
    • Guanosine pentaphosphate synthetase from Streptomyces antibioticus is also a polynucleotide phosphorylase
    • G.H. Jones, M.J. Bibb, Guanosine pentaphosphate synthetase from Streptomyces antibioticus is also a polynucleotide phosphorylase, J. Bacteriol. 178 (1996) 4281-4288.
    • (1996) J. Bacteriol. , vol.178 , pp. 4281-4288
    • Jones, G.H.1    Bibb, M.J.2
  • 30
    • 0030035418 scopus 로고    scopus 로고
    • A set of ordered cosmids and a detailed genetic and physical map for the 8 MB Streptomyces coelicolor A3(2) chromosome
    • M. Redenbach, H.M. Kieser, D. Denapaite, A. Eichner, J. Cullum, H. Kinashi, D.A. Hopwood, A set of ordered cosmids and a detailed genetic and physical map for the 8 MB Streptomyces coelicolor A3(2) chromosome, Mol. Microbiol. 21 (1996) 77-96.
    • (1996) Mol. Microbiol. , vol.21 , pp. 77-96
    • Redenbach, M.1    Kieser, H.M.2    Denapaite, D.3    Eichner, A.4    Cullum, J.5    Kinashi, H.6    Hopwood, D.A.7
  • 31
    • 0032569032 scopus 로고    scopus 로고
    • Reconstitution of the degradation of the mRNA for ribosomal protein S20 with purified enzymes
    • G.A. Coburn, G.A. Mackie, Reconstitution of the degradation of the mRNA for ribosomal protein S20 with purified enzymes, J. Mol. Biol. 279 (1998) 1061-1074.
    • (1998) J. Mol. Biol. , vol.279 , pp. 1061-1074
    • Coburn, G.A.1    Mackie, G.A.2
  • 32
    • 0017701040 scopus 로고
    • Initiation of mammalian protein synthesis. I. Purification and characterization of seven initiation factors
    • M.H. Schreier, B. Erni, T. Staehlin, Initiation of mammalian protein synthesis. I. Purification and characterization of seven initiation factors, J. Mol. Biol. 116 (1977) 727-753.
    • (1977) J. Mol. Biol. , vol.116 , pp. 727-753
    • Schreier, M.H.1    Erni, B.2    Staehlin, T.3
  • 33
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding
    • M.M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding, Anal. Biochem. 72 (1976) 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural protein during the assembly of the head of bacteriophage T4
    • U. Laemmli, Cleavage of structural protein during the assembly of the head of bacteriophage T4, Nature 227 (1970) 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.1
  • 35
    • 0017648969 scopus 로고
    • Purification and characterization of polynucleotide phosphorylase from Escherichia coli - Probe for the analysis of 3′-sequences of RNA
    • H. Soreq, U.Z. Littauer, Purification and characterization of polynucleotide phosphorylase from Escherichia coli - probe for the analysis of 3′-sequences of RNA, J. Biol. Chem. 252 (1977) 6885-6888.
    • (1977) J. Biol. Chem. , vol.252 , pp. 6885-6888
    • Soreq, H.1    Littauer, U.Z.2
  • 36
    • 0002021047 scopus 로고
    • Protein concentration determination
    • Wiley-Liss, Inc, New York
    • D.M. Bollag, S.J. Edelstein, Protein concentration determination, in: Protein Methods, Wiley-Liss, Inc, New York, 1992, pp. 46-49.
    • (1992) Protein Methods , pp. 46-49
    • Bollag, D.M.1    Edelstein, S.J.2
  • 37
    • 0014742908 scopus 로고
    • Kinetics of polymerization and phosphorolysis reactions of E. coli polynucleotide phosphorylase-role of oligonucleotides in polymerization
    • T. Godefroy, M. Cohn, M. Grunberg-Manago, Kinetics of polymerization and phosphorolysis reactions of E. coli polynucleotide phosphorylase-role of oligonucleotides in polymerization, Eur. J. Biochem. 12 (1970) 236-249.
    • (1970) Eur. J. Biochem. , vol.12 , pp. 236-249
    • Godefroy, T.1    Cohn, M.2    Grunberg-Manago, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.