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Volumn 321, Issue 3, 2002, Pages 397-409

Mutational analysis of polynucleotide phosphorylase from Escherichia coli

Author keywords

KH domain; PNPase; RNA binding; Translational autocontrol

Indexed keywords

BACTERIAL RNA; PHOSPHATE; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE;

EID: 0036382938     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00645-9     Document Type: Article
Times cited : (75)

References (36)
  • 1
    • 0000875229 scopus 로고
    • Degradation of transfer ribonucleic acid by polynucleotide phosphorylase
    • Thang, M.-N., Guschlbauer, W., Zachau, H. G. & Grunberg-Manago, M. (1967). Degradation of transfer ribonucleic acid by polynucleotide phosphoryl-ase. J. Mol. Biol. 26, 403-421.
    • (1967) J. Mol. Biol. , vol.26 , pp. 403-421
    • Thang, M.-N.1    Guschlbauer, W.2    Zachau, H.G.3    Grunberg-Manago, M.4
  • 2
    • 0014806605 scopus 로고
    • Kinetics of polymerization and phosphorolysis reactions of E. coli polynucleotide phosphorylase. II. Evidence for multiple binding of polynucleotide in the phosphorolysis reaction
    • Godefroy, T. (1970). Kinetics of polymerization and phosphorolysis reactions of E. coli polynucleotide phosphorylase. II. Evidence for multiple binding of polynucleotide in the phosphorolysis reaction. Eur. J. Biochem. 14, 222-230.
    • (1970) Eur. J. Biochem. , vol.14 , pp. 222-230
    • Godefroy, T.1
  • 3
    • 0014742908 scopus 로고
    • Kinetics of polymerization and phosphorolysis reactions of E. coli polynucleotide phosphorylase. Role of oligonucleotides in polymerization
    • Godefroy, T., Cohn, M. & Grunberg-Manago, M. (1970). Kinetics of polymerization and phosphoroly-sis reactions of E. coli polynucleotide phosphorylase. Role of oligonucleotides in polymerization. Eur. J. Biochem. 12, 236-249.
    • (1970) Eur. J. Biochem. , vol.12 , pp. 236-249
    • Godefroy, T.1    Cohn, M.2    Grunberg-Manago, M.3
  • 4
    • 0015240553 scopus 로고
    • Deoxyadenosine diphosphate as a substrate and inhibitor of polynucleotide phosphorylase of Micrococcus luteus. I. Deoxyadenosine diphosphate as a substrate for polymerization and exchange reaction with inorganic 32P
    • Chou, J. Y. & Singer, M. F. (1971). Deoxyadenosine diphosphate as a substrate and inhibitor of polynu-cleotide phosphorylase of Micrococcus luteus. I. Deoxyadenosine diphosphate as a substrate for polymerization and exchange reaction with inorganic 32P. J. Biol. Chem. 246, 7486-7496.
    • (1971) J. Biol. Chem. , vol.246 , pp. 7486-7496
    • Chou, J.Y.1    Singer, M.F.2
  • 5
    • 0034934778 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase functions as both an exonuclease and a poly(A) polymerase in spinach chloroplasts
    • Yehudai-Resheff, S., Hirsch, M. & Schuster, G. (2001). Polynucleotide phosphorylase functions as both an exonuclease and a poly(A) polymerase in spinach chloroplasts. Mol. Cell. Biol. 21, 5408-5416.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5408-5416
    • Yehudai-Resheff, S.1    Hirsch, M.2    Schuster, G.3
  • 6
    • 0034710943 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase functions both as a 3′ → 5′ exonuclease and a poly(A) polymerase in Escherichia coli
    • Mohanty, B. K. & Kushner, S. R. (2000). Polynucleo-tide phosphorylase functions both as a 3′ → 5′ exonuclease and a poly(A) polymerase in Escherichia coli. Proc. Natl Acad. Sci. USA, 97, 11966-11971.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 11966-11971
    • Mohanty, B.K.1    Kushner, S.R.2
  • 7
    • 0035793043 scopus 로고    scopus 로고
    • RNA degradosomes exist in vivo in Escherichia coli as multicomponent complexes associated with the cytoplasmic membrane via the N-terminal region of ribonuclease E.
    • Liou, G. G., Jane, W. N., Cohen, S. N., Lin, N. S. & Lin-Chao, S. (2001). RNA degradosomes exist in vivo in Escherichia coli as multicomponent complexes associated with the cytoplasmic membrane via the N-terminal region of ribonuclease E. Proc. Natl Acad. Sci. USA, 98, 63-68.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 63-68
    • Liou, G.G.1    Jane, W.N.2    Cohen, S.N.3    Lin, N.S.4    Lin-Chao, S.5
  • 8
    • 0028269435 scopus 로고
    • Copurification of E. coli RNase E and PNPase: Evidence for a specific association between two enzymes important in RNA processing and degradation
    • Carpousis, A. J., van Houwe, G., Ehretsmann, C. & Krisch, H. M. (1994). Copurification of E. coli RNase E and PNPase: evidence for a specific association between two enzymes important in RNA processing and degradation. Cell, 11, 889-900.
    • (1994) Cell , vol.11 , pp. 889-900
    • Carpousis, A.J.1    Van Houwe, G.2    Ehretsmann, C.3    Krisch, H.M.4
  • 9
    • 0014866632 scopus 로고
    • Cinétiques des réactions catalysées par la polynucléotide phosphorylase d' E. coli: III - Le 2′ désoxy ADP comme substrat et inhibiteur
    • Bon, S., Godefroy, T. & Grunberg-Manago, M. (1970). Cinétiques des réactions catalysées par la polynucléotide phosphorylase d' E. coli: III-Le 2′ désoxy ADP comme substrat et inhibiteur. Eur. J. Biochem. 16, 363-372.
    • (1970) Eur. J. Biochem. , vol.16 , pp. 363-372
    • Bon, S.1    Godefroy, T.2    Grunberg-Manago, M.3
  • 10
    • 0010588238 scopus 로고
    • Oligonucleotides as primers for PNPase
    • Singer, M. F., Heppel, L. A. & Hilmoe, R. J. (1960). Oligonucleotides as primers for PNPase. J. Biol. Chem. 235, 738-750.
    • (1960) J. Biol. Chem. , vol.235 , pp. 738-750
    • Singer, M.F.1    Heppel, L.A.2    Hilmoe, R.J.3
  • 11
    • 0027327486 scopus 로고
    • The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein
    • Siomi, H., Siomi, M. C., Nussbaum, R. L. & Dreyfuss, G. (1993). The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein. Cell, 74, 291-298.
    • (1993) Cell , vol.74 , pp. 291-298
    • Siomi, H.1    Siomi, M.C.2    Nussbaum, R.L.3    Dreyfuss, G.4
  • 12
    • 0023088853 scopus 로고
    • Nucleotide sequence of the pnp gene of Escherichia coli encoding polynucleotide phosphorylase
    • Régnier, P., Grunberg-Manago, M. & Portier, C. (1987). Nucleotide sequence of the pnp gene of Escherichia coli encoding polynucleotide phosphorylase. J. Biol. Chem. 262, 63-68.
    • (1987) J. Biol. Chem. , vol.262 , pp. 63-68
    • Régnier, P.1    Grunberg-Manago, M.2    Portier, C.3
  • 13
    • 0029030017 scopus 로고
    • Localized Bicaudal-C RNA encodes a protein containing a KH domain, the RNA binding motif of FMR1
    • Mahone, M., Saffman, E. & Lasko, P. F. (1995). Localized Bicaudal-C RNA encodes a protein containing a KH domain, the RNA binding motif of FMR1. EMBO J. 14, 2043-2055.
    • (1995) EMBO J. , vol.14 , pp. 2043-2055
    • Mahone, M.1    Saffman, E.2    Lasko, P.F.3
  • 14
    • 0031862144 scopus 로고    scopus 로고
    • In vitro genetic analysis of the RNA binding site of vigilin, a multi-KH-domain protein
    • Kanalori, H., Dodson, R. E. & Shapiro, D. J. (1998). In vitro genetic analysis of the RNA binding site of vigilin, a multi-KH-domain protein. Mol. Cell. Biol. 18, 3991-4003.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3991-4003
    • Kanalori, H.1    Dodson, R.E.2    Shapiro, D.J.3
  • 15
    • 0031471204 scopus 로고    scopus 로고
    • The solution structure of the S1 RNA binding domain: A member of an ancient nucleic acid-binding fold
    • Bycroft, M., Hubbard, T. J. P., Proctor, M., Freund, S. M. V. & Murzin, A. G. (1997). The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold. Cell, 88, 235-242.
    • (1997) Cell , vol.88 , pp. 235-242
    • Bycroft, M.1    Hubbard, T.J.P.2    Proctor, M.3    Freund, S.M.V.4    Murzin, A.G.5
  • 16
    • 0034435974 scopus 로고    scopus 로고
    • A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation
    • Symmons, M. F., Jones, G. H. & Luisi, B. F. (2000). A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation. Struct. Fold. Des. 8, 1215-1226.
    • (2000) Struct. Fold. Des. , vol.8 , pp. 1215-1226
    • Symmons, M.F.1    Jones, G.H.2    Luisi, B.F.3
  • 17
    • 0016438636 scopus 로고
    • Quaternary structure of Escherichia coli polynucleotide phosphorylase: New evidence for a trimeric structure
    • Portier, C. (1975). Quaternary structure of Escherichia coli polynucleotide phosphorylase: new evidence for a trimeric structure. FEBS Letters, 50, 79-81.
    • (1975) FEBS Letters , vol.50 , pp. 79-81
    • Portier, C.1
  • 18
    • 0016705035 scopus 로고
    • Quaternary structure of polynucleotide phosphorylase from Escherichia coli: Evidence of a complex between two type of polypeptide chains
    • Portier, C. (1975). Quaternary structure of polynucleotide phosphorylase from Escherichia coli: evidence of a complex between two type of polypeptide chains. Eur. J. Biochem. 55, 573-582.
    • (1975) Eur. J. Biochem. , vol.55 , pp. 573-582
    • Portier, C.1
  • 19
    • 0014442167 scopus 로고
    • Electron microscopy of Escherichia coli polynucleotide phosphorylase molecules and polyribonucleotide formation
    • Valentine, R. C., Thang, M.-N. & Grunberg-Manago, M. (1969). Electron microscopy of Escherichia coli polynucleotide phosphorylase molecules and polyribonucleotide formation. J. Mol. Biol. 39, 389-391.
    • (1969) J. Mol. Biol. , vol.39 , pp. 389-391
    • Valentine, R.C.1    Thang, M.-N.2    Grunberg-Manago, M.3
  • 20
    • 0029974966 scopus 로고    scopus 로고
    • Guanosine pentaphosphate synthetase from Streptomyces antibioticus is also a polynucleotide phosphorylase
    • Jones, G. H. & Bibb, M. J. (1996). Guanosine pentaphosphate synthetase from Streptomyces antibioticus is also a polynucleotide phosphorylase. J. Bacteriol. 178, 4281-4288.
    • (1996) J. Bacteriol. , vol.178 , pp. 4281-4288
    • Jones, G.H.1    Bibb, M.J.2
  • 21
    • 0026654962 scopus 로고
    • E. coli polynucleotide phosphorylase expression is autoregulated through an RNase III-dependent mechanism
    • Robert-LeMeur, M. & Portier, C. (1992). E. coli polynucleotide phosphorylase expression is autoregulated through an RNase III-dependent mechanism. EMBO J. 11, 2633-2641.
    • (1992) EMBO J. , vol.11 , pp. 2633-2641
    • Robert-LeMeur, M.1    Portier, C.2
  • 22
    • 0035803559 scopus 로고    scopus 로고
    • PNPase autocontrols its expression by degrading a double-stranded structure in the pnp mRNA leader
    • Jarrige, A.-C., Mathy, N. & Portier, C. (2001). PNPase autocontrols its expression by degrading a double-stranded structure in the pnp mRNA leader. EMBO J. 20, 1-10.
    • (2001) EMBO J. , vol.20 , pp. 1-10
    • Jarrige, A.-C.1    Mathy, N.2    Portier, C.3
  • 23
    • 0028358101 scopus 로고
    • Polynucleotide phosphorylase of Escherichia coli induces the degradation of its RNase III processed messenger by preventing its translation
    • Robert-LeMeur, M. & Portier, C. (1994). Polynucleotide phosphorylase of Escherichia coli induces the degradation of its RNase III processed messenger by preventing its translation. Nucl. Acids Res. 22, 397-403.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 397-403
    • Robert-LeMeur, M.1    Portier, C.2
  • 24
    • 0025088052 scopus 로고
    • Low copy number plasmids for regulated low-level expression of cloned genes in Escherichia coli with blue/white insert screening capability
    • Lerner, C. G. & Inouye, M. (1990). Low copy number plasmids for regulated low-level expression of cloned genes in Escherichia coli with blue/white insert screening capability. Nucl. Acids Res. 18, 4631-4633.
    • (1990) Nucl. Acids Res. , vol.18 , pp. 4631-4633
    • Lerner, C.G.1    Inouye, M.2
  • 25
    • 85031452384 scopus 로고
    • Séparation et identification de polynucléotide phosphorylase par électrophorèse sur gel de polyacrylamide
    • Thang, M.-N., Thang, D.-C. & Léautey, J. (1967). Séparation et identification de polynucléotide phosphorylase par électrophorèse sur gel de polyacrylamide. C. R. Acad. Sci. Paris, 165, 1823-1826.
    • (1967) C. R. Acad. Sci. Paris , vol.165 , pp. 1823-1826
    • Thang, M.-N.1    Thang, D.-C.2    Léautey, J.3
  • 26
    • 0033066929 scopus 로고    scopus 로고
    • A novel mutation in the KH domain of polynucleotide phosphorylase affects autoregulation and mRNA decay in Escherichia coli
    • Garcia-Mena, J., Das, A., Sanchez-Trujillo, A., Portier, C. & Montanez, C. (1999). A novel mutation in the KH domain of polynucleotide phosphorylase affects autoregulation and mRNA decay in Escherichia coli. Mol. Microbiol. 33, 235-248.
    • (1999) Mol. Microbiol. , vol.33 , pp. 235-248
    • Garcia-Mena, J.1    Das, A.2    Sanchez-Trujillo, A.3    Portier, C.4    Montanez, C.5
  • 27
    • 0035253621 scopus 로고    scopus 로고
    • KH domain: One motif, two folds
    • Grishin, N. V. (2001). KH domain: one motif, two folds. Nucl. Acids Res. 29, 638-643.
    • (2001) Nucl. Acids Res. , vol.29 , pp. 638-643
    • Grishin, N.V.1
  • 29
    • 0028236525 scopus 로고
    • Essential role for KH domains in RNA binding: Impaired RNA binding by a mutation in the KH domain of FMR1 that causes fragile X syndrome
    • Siomi, H., Choi, M., Siomi, M. C., Nussbaum, R. L. & Dreyfuss, G. (1994). Essential role for KH domains in RNA binding: impaired RNA binding by a mutation in the KH domain of FMR1 that causes fragile X syndrome. Cell, 77, 33-39.
    • (1994) Cell , vol.77 , pp. 33-39
    • Siomi, H.1    Choi, M.2    Siomi, M.C.3    Nussbaum, R.L.4    Dreyfuss, G.5
  • 30
    • 0034977180 scopus 로고    scopus 로고
    • Increased expression of E. coli polynucleotide phosphorylase at low temperature is linked to a decrease in the efficiency of autocontrol
    • Mathy, N., Jarrige, A.-C., Robert-Le Meur, M. & Por-tier, C. (2001). Increased expression of E. coli polynucleotide phosphorylase at low temperature is linked to a decrease in the efficiency of autocontrol. J. Bacteriol. 183, 3848-3854.
    • (2001) J. Bacteriol. , vol.183 , pp. 3848-3854
    • Mathy, N.1    Jarrige, A.-C.2    Robert-Le Meur, M.3    Portier, C.4
  • 31
    • 0023370347 scopus 로고
    • The first step in the functional inactivation of the E. coli polynucleotide phosphorylase messenger is a ribonuclease III processing at the 5′ end
    • Portier, C., Dondon, L., Grunberg-Manago, M. & Régnier, P. (1987). The first step in the functional inactivation of the E. coli polynucleotide phosphorylase messenger is a ribonuclease III processing at the 5′ end. EMBO J. 6, 2165-2170.
    • (1987) EMBO J. , vol.6 , pp. 2165-2170
    • Portier, C.1    Dondon, L.2    Grunberg-Manago, M.3    Régnier, P.4
  • 32
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A. (1985). Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl Acad. Sci. USA, 82, 488-492.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 33
    • 0002972659 scopus 로고
    • Assay of β-galactosidase
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • Miller, J. H. (1972). Assay of β-galactosidase. In Experiments in Molecular Genetics, pp. 352-355, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
    • (1972) Experiments in Molecular Genetics , pp. 352-355
    • Miller, J.H.1
  • 34
    • 0018956067 scopus 로고
    • Isolation of a polynucleotide phosphorylase mutant using a kanamycin resistant determinant
    • Portier, C. (1980). Isolation of a polynucleotide phosphorylase mutant using a kanamycin resistant determinant. Mol. Gen. Genet. 178, 343-349.
    • (1980) Mol. Gen. Genet. , vol.178 , pp. 343-349
    • Portier, C.1
  • 35
    • 4244120872 scopus 로고
    • Microdetermination of phosphorus
    • Chen, P. S., Toribara, T. Y. & Warner, H. (1956). Microdetermination of phosphorus. Anal. Chem. 28, 1756-1758.
    • (1956) Anal. Chem. , vol.28 , pp. 1756-1758
    • Chen, P.S.1    Toribara, T.Y.2    Warner, H.3
  • 36
    • 0014690791 scopus 로고
    • The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis
    • Weber, K. Osborn, M. (1969). The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem. 244, 4406-4412.
    • (1969) J. Biol. Chem. , vol.244 , pp. 4406-4412
    • Weber, K.1    Osborn, M.2


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