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Volumn 66, Issue , 2000, Pages 67-105

Exoribonucleases and their multiple roles in RNA metabolism

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; EXORIBONUCLEASE; FUNGAL PROTEIN; MESSENGER RNA;

EID: 0035193362     PISSN: 00796603     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0079-6603(00)66027-0     Document Type: Review
Times cited : (121)

References (194)
  • 1
    • 0032932638 scopus 로고    scopus 로고
    • Function, mechanism and regulation of bacterial ribonucleases
    • A.W Nicholson Function, mechanism and regulation of bacterial ribonucleases FEMS Microbiol. Rev. 23 1999 371 390
    • (1999) FEMS Microbiol. Rev. , vol.23 , pp. 371-390
    • Nicholson, A.W1
  • 2
    • 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. Nucleic Acid Res. Mot. Biol. 62 1999 55 108
    • (1999) Prog. Nucleic Acid Res. Mot. Biol. , vol.62 , pp. 55-108
    • Coburn, G.A1    Mackie, G.A2
  • 3
    • 0032916509 scopus 로고    scopus 로고
    • mRNA degradation. A tale of poly(A) and multiprotein machines
    • A.J Carpousis N.F Vanzo L.C Raynal mRNA degradation. A tale of poly(A) and multiprotein machines Trends Genet. 15 1999 24 28
    • (1999) Trends Genet. , vol.15 , pp. 24-28
    • Carpousis, A.J1    Vanzo, N.F2    Raynal, L.C3
  • 4
    • 0032568335 scopus 로고    scopus 로고
    • The exosome: a versatile RNA processing machine
    • C.J Decker The exosome: a versatile RNA processing machine Curr. Biol. 8 1998 R238 R240
    • (1998) Curr. Biol. , vol.8 , pp. R238-R240
    • Decker, C.J1
  • 5
    • 0027220698 scopus 로고
    • Promiscuous exoribonucleases of Escherichia coli
    • M.P Deutscher Promiscuous exoribonucleases of Escherichia coli J. Bacteriol. 175 1993 4577 4583
    • (1993) J. Bacteriol. , vol.175 , pp. 4577-4583
    • Deutscher, M.P1
  • 6
    • 0033570183 scopus 로고    scopus 로고
    • Exonuclease X of Escherichia coli. A novel 3′–5′ DNase and dnaQ superfamily member involved in DNA repair
    • M Viswanathan S.T Lovett Exonuclease X of Escherichia coli . A novel 3′–5′ DNase and dnaQ superfamily member involved in DNA repair J. Biol. Chem. 274 1999 30094 30100
    • (1999) J. Biol. Chem. , vol.274 , pp. 30094-30100
    • Viswanathan, M1    Lovett, S.T2
  • 7
    • 0003395950 scopus 로고
    • Polynucleotide phosphorylase and ribonuclease 11 are required for cell viability and mRNA turnover in Escherichia coli K-12
    • W.P Donovan S.R Kushner Polynucleotide phosphorylase and ribonuclease 11 are required for cell viability and mRNA turnover in Escherichia coli K-12 6th ed. Proc. Natl. Acad. Sci. USA 83 1986 120 124
    • (1986) , pp. 120-124
    • Donovan, W.P1    Kushner, S.R2
  • 8
    • 0033551137 scopus 로고    scopus 로고
    • Oligoribonuclease is an essential component of the mRNA decay pathway
    • S Ghosh M.P Deutscher Oligoribonuclease is an essential component of the mRNA decay pathway 6th ed. Proc. Natl. Acad. Sci. USA 96 1999 4372 4377
    • (1999) , pp. 4372-4377
    • Ghosh, S1    Deutscher, M.P2
  • 9
    • 0030576503 scopus 로고    scopus 로고
    • Maturation pathways for E. coli tRNA precursors: a random multienzyme process in vivo
    • Z Li M.P Deutscher Maturation pathways for E. coli tRNA precursors: a random multienzyme process in vivo Cell 86 1996 503 512
    • (1996) Cell , vol.86 , pp. 503-512
    • Li, Z1    Deutscher, M.P2
  • 10
    • 0032539857 scopus 로고    scopus 로고
    • 3′ exoribonucleolytic trimming is a common feature of the maturation of small, stable RNAs in Escherichia coli
    • Z Li S Pandit M.P Deutscher 3′ exoribonucleolytic trimming is a common feature of the maturation of small, stable RNAs in Escherichia coli 6th ed. Proc. Natl. Acad. Sci. USA 95 1998 2856 2861
    • (1998) , pp. 2856-2861
    • Li, Z1    Pandit, S2    Deutscher, M.P3
  • 11
    • 0029151159 scopus 로고
    • The tRNA processing enzyme RNase T is essential for maturation of 5S RNA
    • Z Li M.P Deutscher The tRNA processing enzyme RNase T is essential for maturation of 5S RNA Proc. Natl. Acad. Sci. USA 92 1995 6883 6886
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6883-6886
    • Li, Z1    Deutscher, M.P2
  • 12
    • 0032951885 scopus 로고    scopus 로고
    • Maturation of 23S ribosomal RNA requires the exoribonuclease RNase T
    • Z Li S Pandit M.P Deutscher Maturation of 23S ribosomal RNA requires the exoribonuclease RNase T RNA 5 1999 139 146
    • (1999) RNA , vol.5 , pp. 139-146
    • Li, Z1    Pandit, S2    Deutscher, M.P3
  • 13
    • 0026666335 scopus 로고
    • The presence of only one of five exoribonucleases is sufficient to support the growth of Escherichia coli
    • K.O Kelly M.P Deutscher The presence of only one of five exoribonucleases is sufficient to support the growth of Escherichia coli J Bacteriol. 174 1992 6682 6684
    • (1992) J Bacteriol. , vol.174 , pp. 6682-6684
    • Kelly, K.O1    Deutscher, M.P2
  • 14
    • 0030836805 scopus 로고    scopus 로고
    • Comparative sequence analysis of ribonucleases HII, III, II, PH, and D
    • I.S Mian Comparative sequence analysis of ribonucleases HII, III, II, PH, and D Nucleic Acids Res. 25 1997 3187 3195
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3187-3195
    • Mian, I.S1
  • 15
    • 77956939091 scopus 로고
    • RNase I, II and IV of Escherichia coli
    • V Shen D Schlessinger RNase I, II and IV of Escherichia coli 6th ed. P.D Boyer The Enzymes Vol. XV 1982 Academic Press New York 501 515 part B
    • (1982) , pp. 501-515
    • Shen, V1    Schlessinger, D2
  • 16
    • 0026334860 scopus 로고
    • Enzymatic basis for hydrolytic versus phosphorolytic mRNA degradation in Escherichia coli and Bacillus subtilis
    • M.P Deutscher N.B Reuven Enzymatic basis for hydrolytic versus phosphorolytic mRNA degradation in Escherichia coli and Bacillus subtilis 6th ed. Proc. Natl. Acad. Sci. USA 88 1991 3277 3280
    • (1991) , pp. 3277-3280
    • Deutscher, M.P1    Reuven, N.B2
  • 17
    • 0032486392 scopus 로고    scopus 로고
    • The vacB gene required for virulence in Shigella flexneri and Escherichia coli encodes the exoribonuclease RNase R
    • Z.F Cheng Y Zuo Z Li K.E Rudd M.P Deutscher The vacB gene required for virulence in Shigella flexneri and Escherichia coli encodes the exoribonuclease RNase R J. Biol. Chem. 273 1998 14077 14080
    • (1998) J. Biol. Chem. , vol.273 , pp. 14077-14080
    • Cheng, Z.F1    Zuo, Y2    Li, Z3    Rudd, K.E4    Deutscher, M.P5
  • 18
    • 0030041546 scopus 로고    scopus 로고
    • Overexpression, purification, and properties of Escherichia coli ribonuclease II
    • G.A Coburn G.A Mackie Overexpression, purification, and properties of Escherichia coli ribonuclease II J. Biol. Chem. 271 1996 1048 1053
    • (1996) J. Biol. Chem. , vol.271 , pp. 1048-1053
    • Coburn, G.A1    Mackie, G.A2
  • 19
    • 0025636164 scopus 로고
    • Different specificities of ribonuclease II and polynucleotide phosphorylase in TmRNA decay
    • G Guarneros C Portier Different specificities of ribonuclease II and polynucleotide phosphorylase in TmRNA decay Biochimie 72 1990 771 777
    • (1990) Biochimie , vol.72 , pp. 771-777
    • Guarneros, G1    Portier, C2
  • 20
    • 0028007315 scopus 로고
    • The processive reaction mechanism of ribonuclease II
    • V.J Cannistraro D Kennell The processive reaction mechanism of ribonuclease II J. Mol. Biol. 243 1994 930 943
    • (1994) J. Mol. Biol. , vol.243 , pp. 930-943
    • Cannistraro, V.J1    Kennell, D2
  • 21
    • 0032803786 scopus 로고    scopus 로고
    • The reaction mechanism of ribonuclease II and its interaction with nucleic acid secondary structures
    • V.J Cannistraro D Kennell The reaction mechanism of ribonuclease II and its interaction with nucleic acid secondary structures Biochim. Biophys. Acta 1433 1999 170 187
    • (1999) Biochim. Biophys. Acta , vol.1433 , pp. 170-187
    • Cannistraro, V.J1    Kennell, D2
  • 22
    • 0029945427 scopus 로고    scopus 로고
    • Differential sensitivities of portions of the mRNA for ribosomal protein S20 to 3′-exonucleases dependent on oligoadenylation and RNA secondary structure
    • G.A Coburn G.A Mackie Differential sensitivities of portions of the mRNA for ribosomal protein S20 to 3′-exonucleases dependent on oligoadenylation and RNA secondary structure J. Biol. Chem. 271 1996 15776 15781
    • (1996) J. Biol. Chem. , vol.271 , pp. 15776-15781
    • Coburn, G.A1    Mackie, G.A2
  • 23
    • 0027531685 scopus 로고
    • DNA sequencing and expression of the gene rnb encoding Escherichia coli ribonuclease II
    • R Zilhao L Camelo C.M Arraiano DNA sequencing and expression of the gene rnb encoding Escherichia coli ribonuclease II Mol. Microbiol. 8 1993 43 51
    • (1993) Mol. Microbiol. , vol.8 , pp. 43-51
    • Zilhao, R1    Camelo, L2    Arraiano, C.M3
  • 24
    • 0030007719 scopus 로고    scopus 로고
    • PNPase modulates RNase II expression in Escherichia coli: implications for mRNA decay and cell metabolism
    • R Zilhao F Cairrao P Regnier C.M Arraiano PNPase modulates RNase II expression in Escherichia coli: implications for mRNA decay and cell metabolism Mol. Microbiol. 20 1996 1033 1042
    • (1996) Mol. Microbiol. , vol.20 , pp. 1033-1042
    • Zilhao, R1    Cairrao, F2    Regnier, P3    Arraiano, C.M4
  • 26
    • 0017567052 scopus 로고
    • Exoribonucleases in wild type Escherichia coli and RNase II-deficient mutants
    • T Kasai R.S Gupta D Schlessinger Exoribonucleases in wild type Escherichia coli and RNase II-deficient mutants J. Biol. Chem. 252 1977 8950 8956
    • (1977) J. Biol. Chem. , vol.252 , pp. 8950-8956
    • Kasai, T1    Gupta, R.S2    Schlessinger, D3
  • 27
    • 0031471204 scopus 로고    scopus 로고
    • The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold
    • M Bycroft T.J Hubbard M Proctor S.M Freund A.G Murzin The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold Cell 88 1997 235 242
    • (1997) Cell , vol.88 , pp. 235-242
    • Bycroft, M1    Hubbard, T.J2    Proctor, M3    Freund, S.M4    Murzin, A.G5
  • 28
    • 0026688006 scopus 로고
    • vacB, a novel chromosomal gene required for expression of virulence genes on the large plasmid of Shigella flexneri
    • T Tobe C Sasakawa N Okada Y Houma M Yoshikawa vacB, a novel chromosomal gene required for expression of virulence genes on the large plasmid of Shigella flexneri J. Bacteriol. 174 1992 6359 6367
    • (1992) J. Bacteriol. , vol.174 , pp. 6359-6367
    • Tobe, T1    Sasakawa, C2    Okada, N3    Houma, Y4    Yoshikawa, M5
  • 29
    • 0030002447 scopus 로고    scopus 로고
    • Properties of a Bacillus subtilis polynucleotide phosphorylase deletion strain
    • W Wang D.H Bechhofer Properties of a Bacillus subtilis polynucleotide phosphorylase deletion strain J. Bacteriol. 178 1996 2375 2382
    • (1996) J. Bacteriol. , vol.178 , pp. 2375-2382
    • Wang, W1    Bechhofer, D.H2
  • 30
    • 0031734294 scopus 로고    scopus 로고
    • Decay of ermC mRNA in a polynucleotide phosphorylase mutant of Bacillus subtilis
    • D.H Bechhofer W Wang Decay of ermC mRNA in a polynucleotide phosphorylase mutant of Bacillus subtilis J. Bacteriol. 180 1998 5968 5977
    • (1998) J. Bacteriol. , vol.180 , pp. 5968-5977
    • Bechhofer, D.H1    Wang, W2
  • 31
    • 0030702085 scopus 로고    scopus 로고
    • The exosome: a conserved eukaryotic RNA processing complex containing multiple 3′→5′ exoribonucleases
    • P Mitchell E Petfalski A Shevchenko M Mann D Tollervey The exosome: a conserved eukaryotic RNA processing complex containing multiple 3′→5′ exoribonucleases Cell 91 1997 457 466
    • (1997) Cell , vol.91 , pp. 457-466
    • Mitchell, P1    Petfalski, E2    Shevchenko, A3    Mann, M4    Tollervey, D5
  • 33
    • 0024007279 scopus 로고
    • Cold-sensitive and caffeine-supersensitive mutants of the Schizosaccharoinyces pombe dis genes implicated in sister chromatid separation during mitosis
    • H Ohkura Y Adachi N Kinoshita O Niwa T Toda M Yanagida Cold-sensitive and caffeine-supersensitive mutants of the Schizosaccharoinyces pombe dis genes implicated in sister chromatid separation during mitosis EMBO J. 7 1988 1465 1473
    • (1988) EMBO J. , vol.7 , pp. 1465-1473
    • Ohkura, H1    Adachi, Y2    Kinoshita, N3    Niwa, O4    Toda, T5    Yanagida, M6
  • 34
    • 0025932537 scopus 로고
    • The fission yeast dis3+ gene encodes a 110-kDa essential protein implicated in mitotic control
    • + gene encodes a 110-kDa essential protein implicated in mitotic control Mol. Cell Biol. 11 1991 5839 5847
    • (1991) Mol. Cell Biol. , vol.11 , pp. 5839-5847
    • Kinoshita, N1    Goebl, M2    Yanagida, M3
  • 35
    • 0031970587 scopus 로고    scopus 로고
    • Human Dis3p, which binds to either GTP- or GDP-Ran, complements Saccharomyces cerevisiae dis3
    • T Shiomi K Fukushima N Suzuki N Nakashima E Noguchi T Nishimoto Human Dis3p, which binds to either GTP- or GDP-Ran, complements Saccharomyces cerevisiae dis3 J. Biochem. (Tokyo) 123 1998 883 890
    • (1998) J. Biochem. (Tokyo) , vol.123 , pp. 883-890
    • Shiomi, T1    Fukushima, K2    Suzuki, N3    Nakashima, N4    Noguchi, E5    Nishimoto, T6
  • 36
    • 0026078476 scopus 로고
    • The SIT4 protein phosphatase functions in late G1 for progression into S phase
    • A Sutton D Immanuel K.T Arndt The SIT4 protein phosphatase functions in late G1 for progression into S phase Mol. Cell Biol. 11 1991 2133 2148
    • (1991) Mol. Cell Biol. , vol.11 , pp. 2133-2148
    • Sutton, A1    Immanuel, D2    Arndt, K.T3
  • 37
    • 0025865009 scopus 로고
    • The Saccharomyces cerevisiae SRKI gene, a suppressor of bcyl and insl, may be involved in protein phosphatase function
    • R.B Wilson A.A Brenner T.B White M.J Engler J.P Gaughran K Tatchell The Saccharomyces cerevisiae SRKI gene, a suppressor of bcyl and insl, may be involved in protein phosphatase function Mol. Cell Biol. 11 1991 3369 3373
    • (1991) Mol. Cell Biol. , vol.11 , pp. 3369-3373
    • Wilson, R.B1    Brenner, A.A2    White, T.B3    Engler, M.J4    Gaughran, J.P5    Tatchell, K6
  • 38
    • 0028214278 scopus 로고
    • The MCS11SSDIISRKIISSLI gene is involved in stable maintenance of the chromosome in yeast
    • Y Uesono A Fujita A Toh-e Y Kikuchi The MCS11SSDIISRKIISSLI gene is involved in stable maintenance of the chromosome in yeast Gene 143 1994 135 138
    • (1994) Gene , vol.143 , pp. 135-138
    • Uesono, Y1    Fujita, A2    Toh-e, A3    Kikuchi, Y4
  • 39
    • 0031010042 scopus 로고    scopus 로고
    • Ssdlp of Saccharomyces cerevisiae associates with RNA
    • Y Uesono A Toh-e Y Kikuchi Ssdlp of Saccharomyces cerevisiae associates with RNA J. Biol. Chem. 272 1997 16103 16109
    • (1997) J. Biol. Chem. , vol.272 , pp. 16103-16109
    • Uesono, Y1    Toh-e, A2    Kikuchi, Y3
  • 40
    • 0344172814 scopus 로고    scopus 로고
    • A conditional U5 snRNA mutation affecting pre-mRNA splicing and nuclear pre-mRNA retention identifies SSDl/SRKI as a general splicing mutant suppressor
    • B.G Luukkonen B Seraphin A conditional U5 snRNA mutation affecting pre-mRNA splicing and nuclear pre-mRNA retention identifies SSDl/SRKI as a general splicing mutant suppressor Nucleic Acids Res. 27 1999 3455 3465
    • (1999) Nucleic Acids Res. , vol.27 , pp. 3455-3465
    • Luukkonen, B.G1    Seraphin, B2
  • 41
    • 0025932828 scopus 로고
    • Characterization of a novel NTP-dependent 3′ exoribonuclease from yeast mitochondria
    • J.J Min H.P Zassenhaus Characterization of a novel NTP-dependent 3′ exoribonuclease from yeast mitochondria SAAS Bull. Biochem. Biotechnol. 4 1991 1 5
    • (1991) SAAS Bull. Biochem. Biotechnol. , vol.4 , pp. 1-5
    • Min, J.J1    Zassenhaus, H.P2
  • 42
    • 0029089849 scopus 로고
    • The novel nuclear gene DSS-1 of Saccharomyces cerevisiae is necessary for mitocbondrial biogenesis
    • A Dmochowska P Golik P.P Stepien The novel nuclear gene DSS-1 of Saccharomyces cerevisiae is necessary for mitocbondrial biogenesis Curr Genet. 28 1995 108 112
    • (1995) Curr Genet. , vol.28 , pp. 108-112
    • Dmochowska, A1    Golik, P2    Stepien, P.P3
  • 43
    • 0031725399 scopus 로고    scopus 로고
    • The yeast nuclear gene DSS1, which codes for a putative RNase II, is necessary for the function of the mitochondria) degradosome in processing and turnover of RNA
    • A Dziembowski M Malewiez M Minczuk P Golik A Dmochowska P.P Stepien The yeast nuclear gene DSS1, which codes for a putative RNase II, is necessary for the function of the mitochondria) degradosome in processing and turnover of RNA Mol. Gen. Genet. 260 1998 108 114
    • (1998) Mol. Gen. Genet. , vol.260 , pp. 108-114
    • Dziembowski, A1    Malewiez, M2    Minczuk, M3    Golik, P4    Dmochowska, A5    Stepien, P.P6
  • 44
    • 0026584861 scopus 로고
    • A protein required for RNA processing and splicing in Neurospora mitochondria is related to gene products involved in cell cycle protein phosphatase functions
    • B Turcq K.F Dobinson N Serizawa A.M Lambowitz A protein required for RNA processing and splicing in Neurospora mitochondria is related to gene products involved in cell cycle protein phosphatase functions 6th ed. Proc. Natl. Acad. Sci. USA 89 1992 1676 1680
    • (1992) , pp. 1676-1680
    • Turcq, B1    Dobinson, K.F2    Serizawa, N3    Lambowitz, A.M4
  • 45
    • 0021246897 scopus 로고
    • RNA splicing in Neurospora mitochondria: nuclear mutants defective in both splicing and 3′ end synthesis of the large rRNA
    • G Garriga H Bertrand A.M Lambowitz RNA splicing in Neurospora mitochondria: nuclear mutants defective in both splicing and 3′ end synthesis of the large rRNA Cell 36 1984 623 634
    • (1984) Cell , vol.36 , pp. 623-634
    • Garriga, G1    Bertrand, H2    Lambowitz, A.M3
  • 46
    • 0019974860 scopus 로고
    • RNA splicing in Neurospora mitochondria. Characterization of new nuclear mutants with defects in splicing the mitochondrial large rRNA
    • H Bertrand P Bridge R.A Collins G Garriga A.M Lambowitz RNA splicing in Neurospora mitochondria. Characterization of new nuclear mutants with defects in splicing the mitochondrial large rRNA Cell 29 1982 517 526
    • (1982) Cell , vol.29 , pp. 517-526
    • Bertrand, H1    Bridge, P2    Collins, R.A3    Garriga, G4    Lambowitz, A.M5
  • 47
    • 0024446150 scopus 로고
    • Mutations in nuclear gene cyt-4 of Neurospora crassa result in pleiotropic defects in processing and splicing of mitochondria) RNAs
    • K.F Dobinson M Henderson R.L Kelley R.A Collins A.M Lambowitz Mutations in nuclear gene cyt-4 of Neurospora crassa result in pleiotropic defects in processing and splicing of mitochondria) RNAs Genetics 123 1989 97 108
    • (1989) Genetics , vol.123 , pp. 97-108
    • Dobinson, K.F1    Henderson, M2    Kelley, R.L3    Collins, R.A4    Lambowitz, A.M5
  • 48
    • 0031574363 scopus 로고    scopus 로고
    • The proofreading domain of Escherichia coli DNA polymerase I and other DNA and/or RNA exonuclease domains
    • M.J Moser W.R Holley A Chatterjee I.S Mian The proofreading domain of Escherichia coli DNA polymerase I and other DNA and/or RNA exonuclease domains Nucleic Acids Res. 25 1997 5110 5118
    • (1997) Nucleic Acids Res. , vol.25 , pp. 5110-5118
    • Moser, M.J1    Holley, W.R2    Chatterjee, A3    Mian, I.S4
  • 49
    • 0027318640 scopus 로고
    • RNase T shares conserved sequence motifs with DNA proofreading exonucleases
    • E.V Koonin M.P Deutscher RNase T shares conserved sequence motifs with DNA proofreading exonucleases Nucleic Acids Res. 21 1993 2521 2522
    • (1993) Nucleic Acids Res. , vol.21 , pp. 2521-2522
    • Koonin, E.V1    Deutscher, M.P2
  • 50
    • 0027184481 scopus 로고
    • A general two-metal-ion mechanism for catalytic RNA
    • T.A Steitz J.A Steitz A general two-metal-ion mechanism for catalytic RNA 6th ed. Proc. Natl. Acad. Sci. USA 90 1993 6498 6502
    • (1993) , pp. 6498-6502
    • Steitz, T.A1    Steitz, J.A2
  • 51
    • 0018182763 scopus 로고
    • Purification of potential 3′ processing nucleases using synthetic tRNA precursors
    • R.K Ghosh M.P Deutscher Purification of potential 3′ processing nucleases using synthetic tRNA precursors Nucleic Acids Res. 5 1978 3831 3842
    • (1978) Nucleic Acids Res. , vol.5 , pp. 3831-3842
    • Ghosh, R.K1    Deutscher, M.P2
  • 52
    • 0019518885 scopus 로고
    • Escherichia coli RNase D. Purification and structural characterization of a putative processing nuclease
    • H Cudny R Zaniewski M.P Deutscher Escherichia coli RNase D. Purification and structural characterization of a putative processing nuclease J. Biol. Chem. 256 1981 5627 5632
    • (1981) J. Biol. Chem. , vol.256 , pp. 5627-5632
    • Cudny, H1    Zaniewski, R2    Deutscher, M.P3
  • 53
    • 0019455383 scopus 로고
    • Escherichia coli RNase D. Catalytic properties and substrate specificity
    • H Cudny R Zaniewski M.P Deutscher Escherichia coli RNase D. Catalytic properties and substrate specificity J. Biol. Chem. 256 1981 5633 5637
    • (1981) J. Biol. Chem. , vol.256 , pp. 5633-5637
    • Cudny, H1    Zaniewski, R2    Deutscher, M.P3
  • 54
    • 0017817515 scopus 로고
    • Identification of an Escherichia coli nuclease acting on structurally altered transfer RNA molecules
    • R.K Ghosh M.P Deutscher Identification of an Escherichia coli nuclease acting on structurally altered transfer RNA molecules J. Biol. Chem. 253 1978 997 1000
    • (1978) J. Biol. Chem. , vol.253 , pp. 997-1000
    • Ghosh, R.K1    Deutscher, M.P2
  • 55
    • 0018980250 scopus 로고
    • Apparent involvement of ribonuclease D in the 3′ processing of tRNA precursors
    • H Cudny M.P Deutscher Apparent involvement of ribonuclease D in the 3′ processing of tRNA precursors 6th ed. Proc. Natl. Acad. Sci. USA 77 1980 837 841
    • (1980) , pp. 837-841
    • Cudny, H1    Deutscher, M.P2
  • 56
    • 0023705439 scopus 로고
    • Escherichia coli RNase D: sequencing of the rnd structural gene and purification of the overexpressed protein
    • J.R Zhang M.P Deutscher Escherichia coli RNase D: sequencing of the rnd structural gene and purification of the overexpressed protein Nucleic Acids Res. 16 1988 6265 6278
    • (1988) Nucleic Acids Res. , vol.16 , pp. 6265-6278
    • Zhang, J.R1    Deutscher, M.P2
  • 57
    • 0020583360 scopus 로고
    • Ribonuclease D is not essential for the normal growth of Escherichia coli or bacteriophage T4 or for the biosynthesis of a T4 suppressor tRNA
    • R.T Blouin R Zaniewski M.P Deutscher Ribonuclease D is not essential for the normal growth of Escherichia coli or bacteriophage T4 or for the biosynthesis of a T4 suppressor tRNA J. Biol. Chem. 258 1983 1423 1426
    • (1983) J. Biol. Chem. , vol.258 , pp. 1423-1426
    • Blouin, R.T1    Zaniewski, R2    Deutscher, M.P3
  • 58
    • 0027393081 scopus 로고
    • Multiple exoribonucleases are required for the 3′ processing of Escherichia coli tRNA precursors in vivo
    • N.B Reuven M.P Deutscher Multiple exoribonucleases are required for the 3′ processing of Escherichia coli tRNA precursors in vivo FASEB J. 7 1993 143 148
    • (1993) FASEB J. , vol.7 , pp. 143-148
    • Reuven, N.B1    Deutscher, M.P2
  • 59
    • 0020036487 scopus 로고
    • Genetic mapping of mutation in Escherichia coli leading to a temperature-sensitive RNase D
    • R Zaniewski M.P Deutscher Genetic mapping of mutation in Escherichia coli leading to a temperature-sensitive RNase D Mol. Gen. Genet. 185 1982 142 147
    • (1982) Mol. Gen. Genet. , vol.185 , pp. 142-147
    • Zaniewski, R1    Deutscher, M.P2
  • 60
    • 0024452693 scopus 로고
    • Analysis of the upstream region of the Escherichia coli rnd gene encoding RNase D. Evidence for translational regulation of a putative tRNA processing enzyme
    • J.R Zhang M.P Deutscher Analysis of the upstream region of the Escherichia coli rnd gene encoding RNase D. Evidence for translational regulation of a putative tRNA processing enzyme J. Biol. Chem. 264 1989 18228 18233
    • (1989) J. Biol. Chem. , vol.264 , pp. 18228-18233
    • Zhang, J.R1    Deutscher, M.P2
  • 61
    • 0026509195 scopus 로고
    • A uridine-rich sequence required for translation of prokaryotic mRNA
    • J.R Zhang M.P Deutscher A uridine-rich sequence required for translation of prokaryotic mRNA 6th ed. Proc. Natl. Acad. Sci. USA 89 1992 2605 2609
    • (1992) , pp. 2605-2609
    • Zhang, J.R1    Deutscher, M.P2
  • 62
    • 0039535081 scopus 로고    scopus 로고
    • Poly(A) tail shortening by a mammalian poly(A)-specific 3′ exoribonuclease
    • C.G Korner E Wahle Poly(A) tail shortening by a mammalian poly(A)-specific 3′ exoribonuclease J. Biol. Chem. 272 1997 10448 10456
    • (1997) J. Biol. Chem. , vol.272 , pp. 10448-10456
    • Korner, C.G1    Wahle, E2
  • 63
    • 0040126630 scopus 로고    scopus 로고
    • The deadenylating nuclease (DAN) is involved in poly(A) tail removal during the meiotic maturation of Xenopus oocytes
    • C.G Korner M Wormington M Muckenthaler S Schneider E Dehlin E Wahle The deadenylating nuclease (DAN) is involved in poly(A) tail removal during the meiotic maturation of Xenopus oocytes EMBO J. 17 1998 5427 5437
    • (1998) EMBO J. , vol.17 , pp. 5427-5437
    • Korner, C.G1    Wormington, M2    Muckenthaler, M3    Schneider, S4    Dehlin, E5    Wahle, E6
  • 64
    • 0032557455 scopus 로고    scopus 로고
    • Rrp6p, the yeast homologue of the human PM-Scl 100-kDa autoantigen, is essential for efficient 5.8 S rRNA 3′ end formation
    • M.W Briggs K.T Burkard J.S Butler Rrp6p, the yeast homologue of the human PM-Scl 100-kDa autoantigen, is essential for efficient 5.8 S rRNA 3′ end formation J. Biol. Chem. 273 1998 13255 13263
    • (1998) J. Biol. Chem. , vol.273 , pp. 13255-13263
    • Briggs, M.W1    Burkard, K.T2    Butler, J.S3
  • 66
    • 0033567131 scopus 로고    scopus 로고
    • The yeast exosome and human PM-Scl are related complexes of 3′→5′ exonucleases
    • C Allmang E Petfalski A Podtelejnikov M Mann D Tollervey P Mitchell The yeast exosome and human PM-Scl are related complexes of 3′→5′ exonucleases Genes Dev. 13 1999 2148 2158
    • (1999) Genes Dev. , vol.13 , pp. 2148-2158
    • Allmang, C1    Petfalski, E2    Podtelejnikov, A3    Mann, M4    Tollervey, D5    Mitchell, P6
  • 67
    • 0026706745 scopus 로고
    • Cloning and characterization of the cDNA coding for a polymyositis-scleroderma overlap syndrome-related nucleolar 100-kD protein
    • M Bluthner F.A Bautz Cloning and characterization of the cDNA coding for a polymyositis-scleroderma overlap syndrome-related nucleolar 100-kD protein J. Exp. Med. 176 1992 973 980
    • (1992) J. Exp. Med. , vol.176 , pp. 973-980
    • Bluthner, M1    Bautz, F.A2
  • 68
    • 0026707334 scopus 로고
    • Cloning of a complementary DNA coding for the 100-kD antigenic protein of the PM-Scl autoantigen
    • Q Ge M.B Frank C O'Brien I.N Targoff Cloning of a complementary DNA coding for the 100-kD antigenic protein of the PM-Scl autoantigen J. Clin. Invest. 90 1992 559 570
    • (1992) J. Clin. Invest. , vol.90 , pp. 559-570
    • Ge, Q1    Frank, M.B2    O'Brien, C3    Targoff, I.N4
  • 69
    • 0021169997 scopus 로고
    • Ribonuclease T: new exoribonuclease possibly involved in end-turnover of tRNA
    • M.P Deutscher C.W Marlor R Zaniewski Ribonuclease T: new exoribonuclease possibly involved in end-turnover of tRNA 6th ed. Proc. Natl. Acad. Sci. USA 81 1984 4290 4293
    • (1984) , pp. 4290-4293
    • Deutscher, M.P1    Marlor, C.W2    Zaniewski, R3
  • 70
    • 0025617209 scopus 로고
    • Ribonucleases, tRNA nucleotidyltransferase, and the 3′ processing of tRNA
    • M.P Deutscher Ribonucleases, tRNA nucleotidyltransferase, and the 3′ processing of tRNA Prog. Nucleic Acid Res. Mol. Biol. 39 1990 209 240
    • (1990) Prog. Nucleic Acid Res. Mol. Biol. , vol.39 , pp. 209-240
    • Deutscher, M.P1
  • 71
    • 0022366980 scopus 로고
    • RNase T is responsible for the end-turnover of tRNA in Escherichia coli
    • M.P Deutscher C.W Marlor R Zaniewski RNase T is responsible for the end-turnover of tRNA in Escherichia coli 6th ed. Proc. Natl. Acad. Sci. USA 82 1985 6427 6430
    • (1985) , pp. 6427-6430
    • Deutscher, M.P1    Marlor, C.W2    Zaniewski, R3
  • 72
    • 0026012161 scopus 로고
    • RNase T affects Escherichia coli growth and recovery from metabolic stress
    • K.P Padmanabha M.P Deutscher RNase T affects Escherichia coli growth and recovery from metabolic stress J. Bacteriol. 173 1991 1376 1381
    • (1991) J. Bacteriol. , vol.173 , pp. 1376-1381
    • Padmanabha, K.P1    Deutscher, M.P2
  • 73
    • 0021875024 scopus 로고
    • Purification and characterization of Escherichia coli RNase T
    • M.P Deutscher C.W Marlor Purification and characterization of Escherichia coli RNase T J. Biol. Chem. 260 1985 7067 7071
    • (1985) J. Biol. Chem. , vol.260 , pp. 7067-7071
    • Deutscher, M.P1    Marlor, C.W2
  • 74
    • 0030029157 scopus 로고    scopus 로고
    • The role of individual cysteine residues in the activity of Escherichia coli RNase T
    • Z Li L Zhan M.P Deutscher The role of individual cysteine residues in the activity of Escherichia coli RNase T J. Biol. Chem. 271 1996 1127 1132
    • (1996) J. Biol. Chem. , vol.271 , pp. 1127-1132
    • Li, Z1    Zhan, L2    Deutscher, M.P3
  • 75
    • 0026489712 scopus 로고
    • Sequence and transcriptional analysis of the Escherichia coli rut gene encoding RNase T
    • S Huang M.P Deutscher Sequence and transcriptional analysis of the Escherichia coli rut gene encoding RNase T J. Biol. Chem. 267 1992 25609 25613
    • (1992) J. Biol. Chem. , vol.267 , pp. 25609-25613
    • Huang, S1    Deutscher, M.P2
  • 76
    • 0030021182 scopus 로고    scopus 로고
    • Escherichia coli RNase T functions in vivo as a dimer dependent on cysteine 168
    • Z Li L Zhan M.P Deutscher Escherichia coli RNase T functions in vivo as a dimer dependent on cysteine 168 J. Biol. Chem. 271 1996 1133 1137
    • (1996) J. Biol. Chem. , vol.271 , pp. 1133-1137
    • Li, Z1    Zhan, L2    Deutscher, M.P3
  • 77
    • 0032567535 scopus 로고    scopus 로고
    • Identification of a potent DNase activity associated with RNase T of Escherichia coli
    • M Viswanathan K.W Dower S.T Lovett Identification of a potent DNase activity associated with RNase T of Escherichia coli J. Biol. Chem. 273 1998 35126 35131
    • (1998) J. Biol. Chem. , vol.273 , pp. 35126-35131
    • Viswanathan, M1    Dower, K.W2    Lovett, S.T3
  • 78
    • 0033057293 scopus 로고    scopus 로고
    • Identification of RNase T as a high-copy suppressor of the UV sensitivity associated with single-strand DNA exonuclease deficiency in Escherichia coli
    • M Viswanathan A Lanjuin S.T Lovett Identification of RNase T as a high-copy suppressor of the UV sensitivity associated with single-strand DNA exonuclease deficiency in Escherichia coli Genetics 151 1999 929 934
    • (1999) Genetics , vol.151 , pp. 929-934
    • Viswanathan, M1    Lanjuin, A2    Lovett, S.T3
  • 79
    • 0033569848 scopus 로고    scopus 로고
    • The DNase activity of RNase T and its application to DNA cloning
    • Y Zuo M.P Deutscher The DNase activity of RNase T and its application to DNA cloning Nucleic Acids Res. 27 1999 4077 4082
    • (1999) Nucleic Acids Res. , vol.27 , pp. 4077-4082
    • Zuo, Y1    Deutscher, M.P2
  • 80
    • 0024453570 scopus 로고
    • Localization of the Escherichia coli rat gene encoding RNase T by using a combination of physical and genetic mapping
    • L.M Case X.N Chen M.P Deutscher Localization of the Escherichia coli rat gene encoding RNase T by using a combination of physical and genetic mapping J. Bacteriol. 171 1989 5736 5737
    • (1989) J. Bacteriol. , vol.171 , pp. 5736-5737
    • Case, L.M1    Chen, X.N2    Deutscher, M.P3
  • 81
    • 0029563447 scopus 로고
    • The gene for the longest known Escherichia coli protein is a member of helicase superfamily II
    • N.B Reuven E.V Koonin K.E Rudd M.P Deutscher The gene for the longest known Escherichia coli protein is a member of helicase superfamily II J. Bacteriol. 177 1995 5393 5400
    • (1995) J. Bacteriol. , vol.177 , pp. 5393-5400
    • Reuven, N.B1    Koonin, E.V2    Rudd, K.E3    Deutscher, M.P4
  • 82
    • 0030070804 scopus 로고    scopus 로고
    • The yeast Pant protein is required for poly(A)-binding protein-stimulated poly(A)-nuclease activity
    • R Boeck S.Z Tarun Jr. M Rieger J.A Deardorff S Muller-Auer A.B Sachs The yeast Pant protein is required for poly(A)-binding protein-stimulated poly(A)-nuclease activity J. Biol. Chem. 271 1996 432 438
    • (1996) J. Biol. Chem. , vol.271 , pp. 432-438
    • Boeck, R1    Tarun, S.Z2    Rieger, M3    Deardorff, J.A4    Muller-Auer, S5    Sachs, A.B6
  • 83
    • 0029811599 scopus 로고    scopus 로고
    • PANS encodes a subunit of the Pablp-dependent poly(A) nuclease in Saccharomyces cerevisiae
    • C.E Brown S.Z Tarun Jr. R Boeck A.B Sachs PANS encodes a subunit of the Pablp-dependent poly(A) nuclease in Saccharomyces cerevisiae Mol. Cell Biol. 16 1996 5744 5753
    • (1996) Mol. Cell Biol. , vol.16 , pp. 5744-5753
    • Brown, C.E1    Tarun, S.Z2    Boeck, R3    Sachs, A.B4
  • 84
    • 0016817098 scopus 로고
    • A novel oligoribonuclease of Escherichia coli. I. Isolation and properties
    • S.K Niyogi A.K Datta A novel oligoribonuclease of Escherichia coli . I. Isolation and properties J. Biol. Chem. 250 1975 7307 7312
    • (1975) J. Biol. Chem. , vol.250 , pp. 7307-7312
    • Niyogi, S.K1    Datta, A.K2
  • 85
    • 0016711596 scopus 로고
    • A novel oligoribonuclease of Escherichia coli. II. Mechanism of action
    • A.K Datta S.K Niyogi A novel oligoribonuclease of Escherichia coli . II. Mechanism of action J. Biol. Chem. 250 1975 7313 7319
    • (1975) J. Biol. Chem. , vol.250 , pp. 7313-7319
    • Datta, A.K1    Niyogi, S.K2
  • 86
    • 0029046231 scopus 로고
    • Oligoribonuclease is distinct from the other known exoribonueleases of Escherichia coli
    • D Yu M.P Deutscher Oligoribonuclease is distinct from the other known exoribonueleases of Escherichia coli J. Bacteriol. 177 1995 4137 4139
    • (1995) J. Bacteriol. , vol.177 , pp. 4137-4139
    • Yu, D1    Deutscher, M.P2
  • 87
    • 0031924593 scopus 로고    scopus 로고
    • Oligoribonuclease is encoded by a highly conserved gene in the 3′–5′ exonuclease superfamily
    • X Zhang L Zhu M.P Deutscher Oligoribonuclease is encoded by a highly conserved gene in the 3′–5′ exonuclease superfamily J. Bacteriol. 180 1998 2779 2781
    • (1998) J. Bacteriol. , vol.180 , pp. 2779-2781
    • Zhang, X1    Zhu, L2    Deutscher, M.P3
  • 88
    • 4244168844 scopus 로고
    • Polynucleotide phosphorylase
    • U.Z Littauer H Soreq Polynucleotide phosphorylase 6th ed. P.O Boyer The Enzymes Vol. XV 1982 Academic Press New York 518 553 part B
    • (1982) , pp. 518-553
    • Littauer, U.Z1    Soreq, H2
  • 89
    • 0031241595 scopus 로고    scopus 로고
    • A conserved ancient domain joins the growing superfamily of 3′–5′ exonucleases
    • E.V Koonin A conserved ancient domain joins the growing superfamily of 3′–5′ exonucleases Curr. Biol. 7 1997 R604 606
    • (1997) Curr. Biol. , vol.7 , pp. R604-606
    • Koonin, E.V1
  • 90
    • 0020529142 scopus 로고
    • Ribonuclease BN: identification and partial characterization of a new tRNA processing enzyme
    • P.K Asha R.T Blouin R Zaniewski M.P Deutscher Ribonuclease BN: identification and partial characterization of a new tRNA processing enzyme 6th ed. Proc. Natl. Acad. Sci. USA 80 1983 3301 3304
    • (1983) , pp. 3301-3304
    • Asha, P.K1    Blouin, R.T2    Zaniewski, R3    Deutscher, M.P4
  • 91
    • 0016539941 scopus 로고
    • A mutant of Escherichia coli defective in removing 3′ terminal nucleotides from some transfer RNA precursor molecules
    • J.G Seidman F.J Schmidt K Foss W.H McClain A mutant of Escherichia coli defective in removing 3′ terminal nucleotides from some transfer RNA precursor molecules Cell 5 1975 389 400
    • (1975) Cell , vol.5 , pp. 389-400
    • Seidman, J.G1    Schmidt, F.J2    Foss, K3    McClain, W.H4
  • 92
    • 0015911899 scopus 로고
    • Isolation of an Escherichia coli strain restricting bacteriophage suppressor
    • A.N Maisurian E.A Buyanovskaya Isolation of an Escherichia coli strain restricting bacteriophage suppressor Mol. Gen. Genet. 120 1973 227 229
    • (1973) Mol. Gen. Genet. , vol.120 , pp. 227-229
    • Maisurian, A.N1    Buyanovskaya, E.A2
  • 93
    • 0020553342 scopus 로고
    • Escherichia coli CAN lacks a tRNA-processing nuclease
    • P.K Asha M.P Deutscher Escherichia coli CAN lacks a tRNA-processing nuclease J. Bacteriol. 156 1983 419 420
    • (1983) J. Bacteriol. , vol.156 , pp. 419-420
    • Asha, P.K1    Deutscher, M.P2
  • 94
    • 0033972084 scopus 로고    scopus 로고
    • Purification and characterization of the tRNA processing enzyme RNase BN
    • C Callahan D Neri-Cortes M.P Deutscher Purification and characterization of the tRNA processing enzyme RNase BN J. Biol. Chem. 275 2000 1030 1034
    • (2000) J. Biol. Chem. , vol.275 , pp. 1030-1034
    • Callahan, C1    Neri-Cortes, D2    Deutscher, M.P3
  • 95
    • 0030447708 scopus 로고    scopus 로고
    • Identification and characterization of the Escherichia coli rbn gene encoding the tRNA processing enzyme RNase BN
    • C Callahan M.P Deutscher Identification and characterization of the Escherichia coli rbn gene encoding the tRNA processing enzyme RNase BN J. Bacteriol. 178 1996 7329 7332
    • (1996) J. Bacteriol. , vol.178 , pp. 7329-7332
    • Callahan, C1    Deutscher, M.P2
  • 96
    • 0031468077 scopus 로고    scopus 로고
    • Functional overlap of tRNA nucleotidyltransferase, poly(A) polymerase I, and polynucleotide phosphorylase
    • N.B Reuven Z Zhou M.P Deutscher Functional overlap of tRNA nucleotidyltransferase, poly(A) polymerase I, and polynucleotide phosphorylase J. Biol. Chem. 272 1997 33255 33259
    • (1997) J. Biol. Chem. , vol.272 , pp. 33255-33259
    • Reuven, N.B1    Zhou, Z2    Deutscher, M.P3
  • 97
    • 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.A1    Mackie, G.A2
  • 98
    • 0016438636 scopus 로고
    • Quaternary structure of Escherichia coli polynucleotide phosphorylase: new evidence for a trimeric structure
    • C Portier Quaternary structure of Escherichia coli polynucleotide phosphorylase: new evidence for a trimeric structure FEBS Lett. 50 1975 79 81
    • (1975) FEBS Lett. , vol.50 , pp. 79-81
    • Portier, C1
  • 99
    • 0023088853 scopus 로고
    • Nucleotide sequence of the pnp gene of Escherichia coli encoding polynucleotide phosphorylase. Homology of the primary structure of the protein with the RNA-binding domain of ribosomal protein S1
    • P Regnier M Grunberg-Manago C Portier Nucleotide sequence of the pnp gene of Escherichia coli encoding polynucleotide phosphorylase. Homology of the primary structure of the protein with the RNA-binding domain of ribosomal protein S1 J. Biol. Chem. 262 1987 63 68
    • (1987) J. Biol. Chem. , vol.262 , pp. 63-68
    • Regnier, P1    Grunberg-Manago, M2    Portier, C3
  • 100
    • 0016705035 scopus 로고
    • Quaternary structure of polynucleotide phosphorylase from Escherichia coli: evidence of a complex between two types of polypeptide chains
    • C Portier Quaternary structure of polynucleotide phosphorylase from Escherichia coli : evidence of a complex between two types of polypeptide chains Eur. J. Biochem. 55 1975 573 582
    • (1975) Eur. J. Biochem. , vol.55 , pp. 573-582
    • Portier, C1
  • 101
    • 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, B1    Higgins, C.F2    Krisch, H.M3    Carpousis, A.J4
  • 102
    • 0029976430 scopus 로고    scopus 로고
    • Proteins associated with RNase E in a multicomponent ribonucleolytic complex
    • A Miczak V.R Kaberdin C.L Wei S Lin-Chao Proteins associated with RNase E in a multicomponent ribonucleolytic complex 6th ed. Proc. Natl. Acad. Sci. USA 93 1996 3865 3869
    • (1996) , pp. 3865-3869
    • Miczak, A1    Kaberdin, V.R2    Wei, C.L3    Lin-Chao, S4
  • 103
    • 0028269435 scopus 로고
    • Copurification of E. coli RNAase E and PNPase: evidence for a specific association between two enzymes important in RNA processing and degradation
    • A.J Carpousis G Van Houwe C Ehretsmann H.M Krisch Copurification of E. coli RNAase E and PNPase: evidence for a specific association between two enzymes important in RNA processing and degradation Cell 76 1994 889 900
    • (1994) Cell , vol.76 , pp. 889-900
    • Carpousis, A.J1    Van Houwe, G2    Ehretsmann, C3    Krisch, H.M4
  • 104
    • 0025740223 scopus 로고
    • mRNA degradation by processine 3−5′ exoribonucleases in vitro and the implications for prokaryotic mRNA decay in vivo
    • R.S McLaren S.F Newbury G.S Dance H.C Causton C.F Higgins mRNA degradation by processine 3−5′ exoribonucleases in vitro and the implications for prokaryotic mRNA decay in vivo J. Mol. Biol. 221 1991 81 95
    • (1991) J. Mol. Biol. , vol.221 , pp. 81-95
    • McLaren, R.S1    Newbury, S.F2    Dance, G.S3    Causton, H.C4    Higgins, C.F5
  • 105
    • 0028945837 scopus 로고
    • RNA degradation in Escherichia coli regulated by 3′ adenylation and 5′ phosphorylation
    • F Xu S.N Cohen RNA degradation in Escherichia coli regulated by 3′ adenylation and 5′ phosphorylation Nature 374 1995 180 183
    • (1995) Nature , vol.374 , pp. 180-183
    • Xu, F1    Cohen, S.N2
  • 106
    • 0033560992 scopus 로고    scopus 로고
    • Preferential degradation of polyadenylated and polyuridinylated RNAs by the bacterial exoribonuclease polynucleotide phosphorylase
    • I Lisitsky G Schuster Preferential degradation of polyadenylated and polyuridinylated RNAs by the bacterial exoribonuclease polynucleotide phosphorylase Eur. J. Biochem. 261 1999 468 474
    • (1999) Eur. J. Biochem. , vol.261 , pp. 468-474
    • Lisitsky, I1    Schuster, G2
  • 107
    • 0031696840 scopus 로고    scopus 로고
    • Linkage map of Escherichia coli K-12, edition 10: the physical map
    • K.E Rudd Linkage map of Escherichia coli K-12, edition 10: the physical map Microbiol. Mol. Biol. Rev. 62 1998 985 1019
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 985-1019
    • Rudd, K.E1
  • 108
    • 0022323026 scopus 로고
    • Promoter activity and transcript mapping in the regulatory region for genes encoding ribosomal protein S15 and polynucleotide phosphorylase of Escherichia coli
    • S Evans P.P Dennis Promoter activity and transcript mapping in the regulatory region for genes encoding ribosomal protein S15 and polynucleotide phosphorylase of Escherichia coli Gene 40 1985 15 22
    • (1985) Gene , vol.40 , pp. 15-22
    • Evans, S1    Dennis, P.P2
  • 109
    • 0023370347 scopus 로고
    • The first step in the functional inactivation of the Escherichia coli polynucleotide phosphorylase messenger is a ribonuclease III processing at the 5′ end
    • C Portier L Dondon M Grunberg-Manago P Regnier The first step in the functional inactivation of the Escherichia coli polynucleotide phosphorylase messenger is a ribonuclease III processing at the 5′ end EMBO J. 6 1987 2165 2170
    • (1987) EMBO J. , vol.6 , pp. 2165-2170
    • Portier, C1    Dondon, L2    Grunberg-Manago, M3    Regnier, P4
  • 110
    • 0026654962 scopus 로고
    • E. coli polynucleotide phosphorylase expression is autoregulated through an RNase III-dependent mechanism
    • M Robert-Le Meur C Portier E. coli polynucleotide phosphorylase expression is autoregulated through an RNase III-dependent mechanism EMBO J. 11 1992 2633 2641
    • (1992) EMBO J. , vol.11 , pp. 2633-2641
    • Robert-Le Meur, M1    Portier, C2
  • 111
    • 0028358101 scopus 로고
    • Polynucleotide phosphorylase of Escherichia coli induces the degradation of its RNase III processed messenger by preventing its translation
    • M Robert-Le Meur C Portier Polynucleotide phosphorylase of Escherichia coli induces the degradation of its RNase III processed messenger by preventing its translation Nucleic Acids Res. 22 1994 397 403
    • (1994) Nucleic Acids Res. , vol.22 , pp. 397-403
    • Robert-Le Meur, M1    Portier, C2
  • 112
    • 0033066929 scopus 로고    scopus 로고
    • A novel mutation in the KH domain of polynueleotide phosphorylase affects autoregulation and mRNA decay in Escherichia coli
    • J Garcia-Mena A Das A Sanchez-Trujillo C Portier C Montanez A novel mutation in the KH domain of polynueleotide phosphorylase affects autoregulation and mRNA decay in Escherichia coli Mol. Microbiol. 33 1999 235 248
    • (1999) Mol. Microbiol. , vol.33 , pp. 235-248
    • Garcia-Mena, J1    Das, A2    Sanchez-Trujillo, A3    Portier, C4    Montanez, C5
  • 113
    • 0023099212 scopus 로고
    • Tn5 insertion in the polynueleotide phosphorylase (pnp) gene in Escherichia coli increases susceptibility to antibiotics
    • L.M McMurry S.B Levy Tn5 insertion in the polynueleotide phosphorylase (pnp) gene in Escherichia coli increases susceptibility to antibiotics J. Bacteriol. 169 1987 1321 1324
    • (1987) J. Bacteriol. , vol.169 , pp. 1321-1324
    • McMurry, L.M1    Levy, S.B2
  • 114
    • 0030047027 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase is necessary for competence development in Bacillus subtilis
    • A Luttinger J Hahn D Dubnau Polynucleotide phosphorylase is necessary for competence development in Bacillus subtilis Mol. Microbiol. 19 1996 343 356
    • (1996) Mol. Microbiol. , vol.19 , pp. 343-356
    • Luttinger, A1    Hahn, J2    Dubnau, D3
  • 115
    • 0023186464 scopus 로고
    • Induction of proteins in response to low temperature in Escherichia coli
    • P.G Jones R.A VanBogelen F.C Neidhardt Induction of proteins in response to low temperature in Escherichia coli J. Bacteriol. 169 1987 2092 2095
    • (1987) J. Bacteriol. , vol.169 , pp. 2092-2095
    • Jones, P.G1    VanBogelen, R.A2    Neidhardt, F.C3
  • 116
    • 0028286232 scopus 로고
    • The gene coding for polynueleotide phosphorylase in Photorhabdus sp. strain K122 is induced at low temperatures
    • D.J Clarke B.C Dowds The gene coding for polynueleotide phosphorylase in Photorhabdus sp. strain K122 is induced at low temperatures J. Bacteriol. 176 1994 3775 3784
    • (1994) J. Bacteriol. , vol.176 , pp. 3775-3784
    • Clarke, D.J1    Dowds, B.C2
  • 117
    • 7144226568 scopus 로고    scopus 로고
    • The psychrotrophic bacterium Yersinia enterocolitica requires expression of pap, the gene for polynueleotide phosphorylase, for growth at low temperature (5°C)
    • R.L Goverde J.H Huis in't Veld J.G Kusters F.R Mooi The psychrotrophic bacterium Yersinia enterocolitica requires expression of pap, the gene for polynueleotide phosphorylase, for growth at low temperature (5°C) Mol. Microbiol. 28 1998 555 569
    • (1998) Mol. Microbiol. , vol.28 , pp. 555-569
    • Goverde, R.L1    Huis in't Veld, J.H2    Kusters, J.G3    Mooi, F.R4
  • 118
    • 0030860690 scopus 로고    scopus 로고
    • An essential function for the phosphate-dependent exoribonucleases RNase PH and polynueleotide phosphorylase
    • Z Zhou M.P Deutscher An essential function for the phosphate-dependent exoribonucleases RNase PH and polynueleotide phosphorylase J. Bacteriol. 179 1997 4391 4395
    • (1997) J. Bacteriol. , vol.179 , pp. 4391-4395
    • Zhou, Z1    Deutscher, M.P2
  • 119
    • 0015505458 scopus 로고
    • Incorporation of water oxygens into intracellular nucleotides and RNA. II. Predominantly hydrolytic RNA turnover in Escherichia coli
    • S.G Chaney P.D Boyer Incorporation of water oxygens into intracellular nucleotides and RNA. II. Predominantly hydrolytic RNA turnover in Escherichia coli J. Mol. Biel. 64 1972 581 591
    • (1972) J. Mol. Biel. , vol.64 , pp. 581-591
    • Chaney, S.G1    Boyer, P.D2
  • 120
    • 0029974966 scopus 로고    scopus 로고
    • Guanosine pentaphosphate synthetase from Streptomyces antibioticus is also a polynueleotide phosphorylase
    • G.H Jones M.J Bibb Guanosine pentaphosphate synthetase from Streptomyces antibioticus is also a polynueleotide phosphorylase J. Bacteriol. 178 1996 4281 4288
    • (1996) J. Bacteriol. , vol.178 , pp. 4281-4288
    • Jones, G.H1    Bibb, M.J2
  • 121
    • 0029917715 scopus 로고    scopus 로고
    • Chloroplast mRNA 3′-end processing by a high molecular weight protein complex is regulated by nuclear encoded RNA binding proteins
    • R Hayes J Kudla G Schuster L Gabay P Maliga W Gruissem Chloroplast mRNA 3′-end processing by a high molecular weight protein complex is regulated by nuclear encoded RNA binding proteins EMBO J. 15 1996 1132 1141
    • (1996) EMBO J. , vol.15 , pp. 1132-1141
    • Hayes, R1    Kudla, J2    Schuster, G3    Gabay, L4    Maliga, P5    Gruissem, W6
  • 122
    • 0030748658 scopus 로고    scopus 로고
    • The mechanism of preferential degradation of polyadenylated RNA in the chloroplast. The exoribonuclease 100RNP/polynueleotide phosphorylase displays high binding affinity for poly(A) sequence
    • I Lisitsky A Kotler G Schuster The mechanism of preferential degradation of polyadenylated RNA in the chloroplast. The exoribonuclease 100RNP/polynueleotide phosphorylase displays high binding affinity for poly(A) sequence J. Biol. Chem. 272 1997 17648 17653
    • (1997) J. Biol. Chem. , vol.272 , pp. 17648-17653
    • Lisitsky, I1    Kotler, A2    Schuster, G3
  • 123
    • 15444345541 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase is a component of a novel plant poly(A) polymerase
    • Q.S Li J.D Gupta A.G Hunt Polynucleotide phosphorylase is a component of a novel plant poly(A) polymerase J. Biol. Chem. 273 1998 17539 17543
    • (1998) J. Biol. Chem. , vol.273 , pp. 17539-17543
    • Li, Q.S1    Gupta, J.D2    Hunt, A.G3
  • 124
    • 0023851706 scopus 로고
    • 3′ processing of tRNA precursors in ribonuclease-deficient Escherichia coli. Development and characterization of an in vitro processing system and evidence for a phosphate requirement
    • H Cudny M.P Deutscher 3′ processing of tRNA precursors in ribonuclease-deficient Escherichia coli . Development and characterization of an in vitro processing system and evidence for a phosphate requirement J. Biol. Chem. 263 1988 1518 1523
    • (1988) J. Biol. Chem. , vol.263 , pp. 1518-1523
    • Cudny, H1    Deutscher, M.P2
  • 125
    • 0024042164 scopus 로고
    • RNase PH: an Escherichia coli phosphatedependent nuclease distinct from polynueleotide phosphorylase
    • M.P Deutscher G.T Marshall H Cudny RNase PH: an Escherichia coli phosphatedependent nuclease distinct from polynueleotide phosphorylase 6th ed. Proc. Natl. Acad. Sci. USA 85 1988 4710 4714
    • (1988) , pp. 4710-4714
    • Deutscher, M.P1    Marshall, G.T2    Cudny, H3
  • 126
    • 0026079791 scopus 로고
    • Escherichia coli orfE (upstream of pyrE) encodes RNase PH
    • K.A Ost M.P Deutscher Escherichia coli orfE (upstream of pyrE) encodes RNase PH J. Bacteriol. 173 1991 5589 5591
    • (1991) J. Bacteriol. , vol.173 , pp. 5589-5591
    • Ost, K.A1    Deutscher, M.P2
  • 127
    • 0026794042 scopus 로고
    • Overexpression and rapid purification of the orjE/rph gene product, RNase PH of Escherichia coli
    • K.F Jensen J.T Andersen P Poulsen Overexpression and rapid purification of the orjE/rph gene product, RNase PH of Escherichia coli J. Biol. Chem. 267 1992 17147 17152
    • (1992) J. Biol. Chem. , vol.267 , pp. 17147-17152
    • Jensen, K.F1    Andersen, J.T2    Poulsen, P3
  • 128
    • 0026806544 scopus 로고
    • Characterization of Escherichia coli RNase PH
    • K.O Kelly M.P Deutscher Characterization of Escherichia coli RNase PH J. Biol. Chem. 267 1992 17153 17158
    • (1992) J. Biol. Chem. , vol.267 , pp. 17153-17158
    • Kelly, K.O1    Deutscher, M.P2
  • 129
    • 0021104916 scopus 로고
    • Nucleotide sequence of the Escherichia coli pyrE gene and of the DNA in front of the protein-coding region
    • P Poulsen K.F Jensen P Valentin-Hansen P Carlsson L.G Lundberg Nucleotide sequence of the Escherichia coli pyrE gene and of the DNA in front of the protein-coding region Eur. J. Biochem. 135 1983 223 229
    • (1983) Eur. J. Biochem. , vol.135 , pp. 223-229
    • Poulsen, P1    Jensen, K.F2    Valentin-Hansen, P3    Carlsson, P4    Lundberg, L.G5
  • 130
    • 0025610486 scopus 로고
    • RNase PH catalyzes a synthetic reaction, the addition of nucleotides to the 3′ end of RNA
    • K.A Ost M.P Deutscher RNase PH catalyzes a synthetic reaction, the addition of nucleotides to the 3′ end of RNA Biochimie 72 1990 813 818
    • (1990) Biochimie , vol.72 , pp. 813-818
    • Ost, K.A1    Deutscher, M.P2
  • 131
    • 0028100687 scopus 로고
    • The role of individual exoribonucleases in processing at the 3′ end of Escherichia coli tRNA precursors
    • Z Li M.P Deutscher The role of individual exoribonucleases in processing at the 3′ end of Escherichia coli tRNA precursors J. Biol. Chem. 269 1994 6064 6071
    • (1994) J. Biol. Chem. , vol.269 , pp. 6064-6071
    • Li, Z1    Deutscher, M.P2
  • 132
    • 0021473098 scopus 로고
    • Structure of the Escherichia coli pyrE operon and control of pyrE expression by a UTP modulated intercistronic attentuation
    • P Poulsen F Bonekamp K.F Jensen Structure of the Escherichia coli pyrE operon and control of pyrE expression by a UTP modulated intercistronic attentuation EMBO J. 3 1984 1783 1790
    • (1984) EMBO J. , vol.3 , pp. 1783-1790
    • Poulsen, P1    Bonekamp, F2    Jensen, K.F3
  • 133
    • 0027251266 scopus 로고
    • The Escherichia coli K-12 “wild types” W3110 and MG1655 have an rph frameshift mutation that leads to pyrimidine starvation due to low pyrE expression levels
    • K.F Jensen The Escherichia coli K-12 “wild types” W3110 and MG1655 have an rph frameshift mutation that leads to pyrimidine starvation due to low pyrE expression levels J. Bacteriol. 175 1993 3401 3407
    • (1993) J. Bacteriol. , vol.175 , pp. 3401-3407
    • Jensen, K.F1
  • 134
    • 0024635249 scopus 로고
    • Molecular and mutational analysis of three genes preceding pyrE on the Escherichia coli chromosome
    • P Poulsen J.T Andersen K.F Jensen Molecular and mutational analysis of three genes preceding pyrE on the Escherichia coli chromosome Mol. Microbiol. 3 1989 393 404
    • (1989) Mol. Microbiol. , vol.3 , pp. 393-404
    • Poulsen, P1    Andersen, J.T2    Jensen, K.F3
  • 135
    • 0026658531 scopus 로고
    • RNase PH is essential for tRNA processing and viability in RNase-deficient Escherichia coli cells
    • K.O Kelly N.B Reuven Z Li M.P Deutscher RNase PH is essential for tRNA processing and viability in RNase-deficient Escherichia coli cells J. Biol. Chem. 267 1992 16015 16018
    • (1992) J. Biol. Chem. , vol.267 , pp. 16015-16018
    • Kelly, K.O1    Reuven, N.B2    Li, Z3    Deutscher, M.P4
  • 136
    • 0026695513 scopus 로고
    • Identification of the rph (RNase PH) gene of Bacillus subtilis: evidence for suppression of cold-sensitive mutations in Escherichia coli
    • M.G Craven D.J Henner D Alessi A.T Schauer K.A Ost M.P Deutscher D.I Friedman Identification of the rph (RNase PH) gene of Bacillus subtilis : evidence for suppression of cold-sensitive mutations in Escherichia coli J. Bacteriol. 174 1992 4727 4735
    • (1992) J. Bacteriol. , vol.174 , pp. 4727-4735
    • Craven, M.G1    Henner, D.J2    Alessi, D3    Schauer, A.T4    Ost, K.A5    Deutscher, M.P6    Friedman, D.I7
  • 137
    • 0031897326 scopus 로고    scopus 로고
    • Ski6p is a homolog of RNA-processing enzymes that affects translation of non-poly(A) mRNAs and 60S ribosomal subunit biogenesis
    • L Benard K Carroll R.C Valle R.B Wickner Ski6p is a homolog of RNA-processing enzymes that affects translation of non-poly(A) mRNAs and 60S ribosomal subunit biogenesis Mol. Cell Biol. 18 1998 2688 2696
    • (1998) Mol. Cell Biol. , vol.18 , pp. 2688-2696
    • Benard, L1    Carroll, K2    Valle, R.C3    Wickner, R.B4
  • 138
    • 0000577868 scopus 로고    scopus 로고
    • The 3′ to 5′ degradation of yeast mRNAs is a general mechanism for mRNA turnover that requires the SKI2 DEVH box protein and 3′ to 5′ exonucleases of the exosome complex
    • J.S Jacobs A.R Anderson R.P Parker The 3′ to 5′ degradation of yeast mRNAs is a general mechanism for mRNA turnover that requires the SKI2 DEVH box protein and 3′ to 5′ exonucleases of the exosome complex EMBO J. 17 1998 1497 1506
    • (1998) EMBO J. , vol.17 , pp. 1497-1506
    • Jacobs, J.S1    Anderson, A.R2    Parker, R.P3
  • 139
    • 0033105059 scopus 로고    scopus 로고
    • The exosome subunit Rrp43p is required for the efficient maturation of 5.8S, 18S and 25S rRNA
    • N.I Zanchin D.S Goldfarb The exosome subunit Rrp43p is required for the efficient maturation of 5.8S, 18S and 25S rRNA Nucleic Acids Res. 27 1999 1283 1288
    • (1999) Nucleic Acids Res. , vol.27 , pp. 1283-1288
    • Zanchin, N.I1    Goldfarb, D.S2
  • 140
    • 0032794289 scopus 로고    scopus 로고
    • Active-site mutations in the Xrn1p exoribonuclease of Saccharomyces cerevisiae reveal a specific role in meiosis
    • J.A Solinger D Pascolini W.D Heyer Active-site mutations in the Xrn1p exoribonuclease of Saccharomyces cerevisiae reveal a specific role in meiosis Mol. Cell Biol. 19 1999 5930 5942
    • (1999) Mol. Cell Biol. , vol.19 , pp. 5930-5942
    • Solinger, J.A1    Pascolini, D2    Heyer, W.D3
  • 141
    • 0029871812 scopus 로고    scopus 로고
    • Mechanisms and control of mRNA turnover in Saccharomyces cerevisiae
    • G Caponigro R Parker Mechanisms and control of mRNA turnover in Saccharomyces cerevisiae Microbiol. Rev. 60 1996 233 249
    • (1996) Microbiol. Rev. , vol.60 , pp. 233-249
    • Caponigro, G1    Parker, R2
  • 142
    • 0017842570 scopus 로고
    • An exoribonuclease from Saccharomyces cerevisiae: effect of modifications of 5′ end groups on the hydrolysis of substrates to 5′ mononucleotides
    • A Stevens An exoribonuclease from Saccharomyces cerevisiae : effect of modifications of 5′ end groups on the hydrolysis of substrates to 5′ mononucleotides Biochem. Biophys. Res. Commun. 81 1978 656 661
    • (1978) Biochem. Biophys. Res. Commun. , vol.81 , pp. 656-661
    • Stevens, A1
  • 143
    • 0018332459 scopus 로고
    • Evidence for a 5′ leads to 3′ direction of hydrolysis by a 5' mononucleotide-producing exoribonuclease from Saccharomyces cerevisiae
    • A Stevens Evidence for a 5′ leads to 3′ direction of hydrolysis by a 5' mononucleotide-producing exoribonuclease from Saccharomyces cerevisiae Biochem. Biophys. Res. Commun. 86 1979 1126 1132
    • (1979) Biochem. Biophys. Res. Commun. , vol.86 , pp. 1126-1132
    • Stevens, A1
  • 144
    • 0018902741 scopus 로고
    • Purification and characterization of a Saccharomyces cerevisiae exoribonuclease which yields 5′-mononucleotides by a 5′ to 3′ mode of hydrolysis
    • A Stevens Purification and characterization of a Saccharomyces cerevisiae exoribonuclease which yields 5′-mononucleotides by a 5′ to 3′ mode of hydrolysis J. Biol. Chem. 255 1980 3080 3085
    • (1980) J. Biol. Chem. , vol.255 , pp. 3080-3085
    • Stevens, A1
  • 145
    • 0023164983 scopus 로고
    • A 5′-3′ exoribonuclease of Saccharomyces cerevisiae: size and novel substrate specificity
    • A Stevens M.K Maupin A 5′-3′ exoribonuclease of Saccharomyces cerevisiae : size and novel substrate specificity Arch. Biochem. Biophys. 252 1987 339 347
    • (1987) Arch. Biochem. Biophys. , vol.252 , pp. 339-347
    • Stevens, A1    Maupin, M.K2
  • 146
    • 0025252545 scopus 로고
    • Disruption of the gene XRN1, coding for a 5′→3′ exoribonuclease, restricts yeast cell growth
    • F.W Larimer A Stevens Disruption of the gene XRN1, coding for a 5′→3′ exoribonuclease, restricts yeast cell growth Gene 95 1990 85 90
    • (1990) Gene , vol.95 , pp. 85-90
    • Larimer, F.W1    Stevens, A2
  • 147
    • 0026782452 scopus 로고
    • Characterization of the XRN1 gene encoding a 5′→3′ exoribonuclease: sequence data and analysis of disparate protein and mRNA levels of gene-disrupted yeast cells
    • F.W Larimer C.L Hsu M.K Maupin A Stevens Characterization of the XRN1 gene encoding a 5′→3′ exoribonuclease: sequence data and analysis of disparate protein and mRNA levels of gene-disrupted yeast cells Gene 120 1992 51 57
    • (1992) Gene , vol.120 , pp. 51-57
    • Larimer, F.W1    Hsu, C.L2    Maupin, M.K3    Stevens, A4
  • 148
    • 0028929369 scopus 로고
    • Regulation and intracellular localization of Saccharomyces cerevisiae strand exchange protein 1 (Sep1/XrnI/Keml), a multifunctional exonuclease
    • W.D Heyer A.W Johnson U Reinhart R.D Kolodner Regulation and intracellular localization of Saccharomyces cerevisiae strand exchange protein 1 (Sep1/XrnI/Keml), a multifunctional exonuclease Mol. Cell Biol. 15 1995 2728 2736
    • (1995) Mol. Cell Biol. , vol.15 , pp. 2728-2736
    • Heyer, W.D1    Johnson, A.W2    Reinhart, U3    Kolodner, R.D4
  • 149
    • 0025674401 scopus 로고
    • kem mutations affect nuclear fusion in Saccharomyces cerevisiae
    • J Kim P.O Ljungdahl G.R Fink kem mutations affect nuclear fusion in Saccharomyces cerevisiae Genetics 126 1990 799 812
    • (1990) Genetics , vol.126 , pp. 799-812
    • Kim, J1    Ljungdahl, P.O2    Fink, G.R3
  • 150
    • 0027214097 scopus 로고
    • Yeast cells lacking 5′→3′ exoribonuclease 1 contain mRNA species that are poly(A) deficient and partially lack the 5′ cap structure
    • C.L Hsu A Stevens Yeast cells lacking 5′→3′ exoribonuclease 1 contain mRNA species that are poly(A) deficient and partially lack the 5′ cap structure Mol. Cell Biol. 13 1993 4826 4835
    • (1993) Mol. Cell Biol. , vol.13 , pp. 4826-4835
    • Hsu, C.L1    Stevens, A2
  • 151
    • 0028202495 scopus 로고
    • Deadenylation of the unstable mRNA encoded by the yeast MFA2 gene leads to decapping followed by 5′→3′ digestion of the transcript
    • D Muhlrad C.J Decker R Parker Deadenylation of the unstable mRNA encoded by the yeast MFA2 gene leads to decapping followed by 5′→3′ digestion of the transcript Genes Dev. 8 1994 855 866
    • (1994) Genes Dev. , vol.8 , pp. 855-866
    • Muhlrad, D1    Decker, C.J2    Parker, R3
  • 152
    • 0027320701 scopus 로고
    • A turnover pathway for both stable and unstable mRNAs in yeast: evidence for a requirement for deadenylation
    • C.J Decker R Parker A turnover pathway for both stable and unstable mRNAs in yeast: evidence for a requirement for deadenylation Genes Dev. 7 1993 1632 1643
    • (1993) Genes Dev. , vol.7 , pp. 1632-1643
    • Decker, C.J1    Parker, R2
  • 153
    • 0028342849 scopus 로고
    • The 5′ end of yeast 5.8S rRNA is generated by exonucleases from an upstream cleavage site
    • Y Henry H Wood J.P Morrissey E Petfalski S Kearsey D Tollervey The 5′ end of yeast 5.8S rRNA is generated by exonucleases from an upstream cleavage site EMBO J. 13 1994 2452 2463
    • (1994) EMBO J. , vol.13 , pp. 2452-2463
    • Henry, Y1    Wood, H2    Morrissey, J.P3    Petfalski, E4    Kearsey, S5    Tollervey, D6
  • 154
    • 0031935899 scopus 로고    scopus 로고
    • Processing of the precursors to small nucleolar RNAs and rRNAs requires common components
    • E Petfalski T Dandekar Y Henry D Tollervey Processing of the precursors to small nucleolar RNAs and rRNAs requires common components Mol. Cell Biol. 18 1998 1181 1189
    • (1998) Mol. Cell Biol. , vol.18 , pp. 1181-1189
    • Petfalski, E1    Dandekar, T2    Henry, Y3    Tollervey, D4
  • 155
    • 0025720230 scopus 로고
    • Fragments of the internal transcribed spacer 1 of pre-rRNA accumulate in Saccharomyces cerevisiae lacking 5′-3′ exoribonuclease I
    • A Stevens C.L Hsu K.R Isham F.W Larimer Fragments of the internal transcribed spacer 1 of pre-rRNA accumulate in Saccharomyces cerevisiae lacking 5′-3′ exoribonuclease I J. Bacteriol. 173 1991 7024 7028
    • (1991) J. Bacteriol. , vol.173 , pp. 7024-7028
    • Stevens, A1    Hsu, C.L2    Isham, K.R3    Larimer, F.W4
  • 156
    • 0024003702 scopus 로고
    • mRNA-decapping enzyme from Saccharomyces cerevisiae: purification and unique specificity for long RNA chains
    • A Stevens mRNA-decapping enzyme from Saccharomyces cerevisiae : purification and unique specificity for long RNA chains Mol. Cell Biol. 8 1988 2005 2010
    • (1988) Mol. Cell Biol. , vol.8 , pp. 2005-2010
    • Stevens, A1
  • 157
    • 0027392423 scopus 로고
    • An essential yeast gene with homology to the exonuclease-encoding XRN1/KEM 1 gene also encodes a protein with exoribonuclease activity
    • M Kenna A Stevens M McCammon M.G Douglas An essential yeast gene with homology to the exonuclease-encoding XRN1/KEM 1 gene also encodes a protein with exoribonuclease activity Mol. Cell Biol. 13 1993 341 350
    • (1993) Mol. Cell Biol. , vol.13 , pp. 341-350
    • Kenna, M1    Stevens, A2    McCammon, M3    Douglas, M.G4
  • 158
    • 0027207247 scopus 로고
    • TAPI, a yeast gene that activates the expression of a tRNA gene with a defective internal promoter
    • G Di Segni B.L McConaughy R.A Shapiro T.L Aldrich B.D Hall TAPI, a yeast gene that activates the expression of a tRNA gene with a defective internal promoter Mol. Cell Biol. 13 1993 3424 3433
    • (1993) Mol. Cell Biol. , vol.13 , pp. 3424-3433
    • Di Segni, G1    McConaughy, B.L2    Shapiro, R.A3    Aldrich, T.L4    Hall, B.D5
  • 159
    • 0026655521 scopus 로고
    • Isolation and characterization of RATI: an essential gene of Saccharomyces cerevisiae required for the efficient nucleocytoplasmic trafficking of mRNA
    • D.C Amberg A.L Goldstein C.N Cole Isolation and characterization of RATI: an essential gene of Saccharomyces cerevisiae required for the efficient nucleocytoplasmic trafficking of mRNA Genes Dev. 6 1992 1173 1189
    • (1992) Genes Dev. , vol.6 , pp. 1173-1189
    • Amberg, D.C1    Goldstein, A.L2    Cole, C.N3
  • 160
    • 0029439305 scopus 로고
    • Comparison of features of the RNase activity of 5′-exonuclease1 and 5′-exonuclease-2 of Saccharomyces cerevisiae
    • T.L Poole A Stevens Comparison of features of the RNase activity of 5′-exonuclease1 and 5′-exonuclease-2 of Saccharomyces cerevisiae 6th ed. Nucleic Acids Symp. Ser. 33 1995 79 81
    • (1995) , pp. 79-81
    • Poole, T.L1    Stevens, A2
  • 161
    • 0029024239 scopus 로고
    • 5′-exonuclease-2 of Saccharomyces cerevisiae. Purification and features of ribonuclease activity with comparison to 5′-exonuclease-1
    • A Stevens T.L Poole 5′-exonuclease-2 of Saccharomyces cerevisiae . Purification and features of ribonuclease activity with comparison to 5′-exonuclease-1 J. Biol. Chem. 270 1995 16063 16069
    • (1995) J. Biol. Chem. , vol.270 , pp. 16063-16069
    • Stevens, A1    Poole, T.L2
  • 162
    • 0031587993 scopus 로고    scopus 로고
    • Structural modifications of RNA influence the 5′ exoribonucleolytie hydrolysis by XRN1 and HKEI of Saccharomyces cerevisiae
    • T.L Poole A Stevens Structural modifications of RNA influence the 5′ exoribonucleolytie hydrolysis by XRN1 and HKEI of Saccharomyces cerevisiae Biochem. Biophys. Res. Commun. 235 1997 799 805
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 799-805
    • Poole, T.L1    Stevens, A2
  • 163
    • 0030764692 scopus 로고    scopus 로고
    • Ratlp and Xrnlp are functionally interchangeable exoribonucleases that are restricted to and required in the nucleus and cytoplasm, respectively
    • A.W Johnson Ratlp and Xrnlp are functionally interchangeable exoribonucleases that are restricted to and required in the nucleus and cytoplasm, respectively Mol. Cell Biol. 17 1997 6122 6130
    • (1997) Mol. Cell Biol. , vol.17 , pp. 6122-6130
    • Johnson, A.W1
  • 164
    • 0028348193 scopus 로고
    • Molecular analysis of the dhpl+ gene of Schizosaccharomyces pombe: an essential gene that has homology to the DST2 and RATI genes of Saccharomyces cerevisiae
    • + gene of Schizosaccharomyces pombe : an essential gene that has homology to the DST2 and RATI genes of Saccharomyces cerevisiae Mol. Gen. Genet. 243 1994 1 8
    • (1994) Mol. Gen. Genet. , vol.243 , pp. 1-8
    • Sugano, S1    Shobuike, T2    Takeda, T3    Sugino, A4    Ikeda, H5
  • 165
    • 0028913850 scopus 로고
    • Characterization of cDNA encoding mouse bomolog of fission yeast dhpl+ gene: structural and functional conservation
    • + gene: structural and functional conservation Nucleic Acids Res. 23 1995 357 361
    • (1995) Nucleic Acids Res. , vol.23 , pp. 357-361
    • Shobuike, T1    Sugano, S2    Yamashita, T3    Ikeda, H4
  • 166
    • 0033566223 scopus 로고    scopus 로고
    • Cloning and mapping of the XRN2 gene to human chromosome 20p11.1-p11.2
    • M Zhang L Yu Y Xin P Hu Q Fu C Yu S Zhao Cloning and mapping of the XRN2 gene to human chromosome 20p11.1-p11.2 Genomics 59 1999 252 254
    • (1999) Genomics , vol.59 , pp. 252-254
    • Zhang, M1    Yu, L2    Xin, Y3    Hu, P4    Fu, Q5    Yu, C6    Zhao, S7
  • 167
    • 0029939247 scopus 로고    scopus 로고
    • The 3′ end of yeast 5.8S rRNA is generated by an exonuclease processing mechanism
    • P Mitchell E Petfalski D Tollervey The 3′ end of yeast 5.8S rRNA is generated by an exonuclease processing mechanism Genes Dev. 10 1996 502 513
    • (1996) Genes Dev. , vol.10 , pp. 502-513
    • Mitchell, P1    Petfalski, E2    Tollervey, D3
  • 168
    • 0021972197 scopus 로고
    • Purification and properties of a novel nucleolar exoribonuclease capable of degrading both single-stranded and double-stranded RNA
    • D.C Eichler S.J Eales Purification and properties of a novel nucleolar exoribonuclease capable of degrading both single-stranded and double-stranded RNA Biochemistry 24 1985 686 691
    • (1985) Biochemistry , vol.24 , pp. 686-691
    • Eichler, D.C1    Eales, S.J2
  • 169
    • 0021914961 scopus 로고
    • Purification and mode of action of a microsomal exoribonuclease from rat liver
    • H Kumagai M Nakamura N Ozaki K Igarashi S Hirose Purification and mode of action of a microsomal exoribonuclease from rat liver Biochim. Biophys. Acta 827 1985 431 438
    • (1985) Biochim. Biophys. Acta , vol.827 , pp. 431-438
    • Kumagai, H1    Nakamura, M2    Ozaki, N3    Igarashi, K4    Hirose, S5
  • 170
    • 0017689775 scopus 로고
    • A cytoplasmic exoribonuclease from HeLa cells
    • C.N Kwan A cytoplasmic exoribonuclease from HeLa cells Biochim. Biophys. Acta 479 1977 322 331
    • (1977) Biochim. Biophys. Acta , vol.479 , pp. 322-331
    • Kwan, C.N1
  • 171
    • 0026630153 scopus 로고
    • Properties of a HeLa cell 3′ exonuclease specific for degrading poly(A) tails of mammalian mRNA
    • J Aström A Aström A Virtanen Properties of a HeLa cell 3′ exonuclease specific for degrading poly(A) tails of mammalian mRNA J. Biol. Chem. 267 1992 18154 18159
    • (1992) J. Biol. Chem. , vol.267 , pp. 18154-18159
    • Aström, J1    Aström, A2    Virtanen, A3
  • 172
    • 0028151423 scopus 로고
    • Purification of a human polyribosome-associated 3′ to 5′ exoribonuclease
    • N Caruccio J Ross Purification of a human polyribosome-associated 3′ to 5′ exoribonuclease J. Biol. Chem. 269 1994 31814 31821
    • (1994) J. Biol. Chem. , vol.269 , pp. 31814-31821
    • Caruccio, N1    Ross, J2
  • 173
    • 0030436198 scopus 로고    scopus 로고
    • Pre-tRNA 3′-processing in Saccharomyces cerevisiae. Purification and characterization of exo- and endoribonucleases
    • A Papadimitriou H.J Gross Pre-tRNA 3′-processing in Saccharomyces cerevisiae . Purification and characterization of exo- and endoribonucleases Eur. J. Biochem. 242 1996 747 759
    • (1996) Eur. J. Biochem. , vol.242 , pp. 747-759
    • Papadimitriou, A1    Gross, H.J2
  • 174
    • 0021921384 scopus 로고
    • Simultaneous isolation of cytoplasmic endoribonuclease and exoribonuclease of Trypanosoma brucei
    • G.O Gbenle Simultaneous isolation of cytoplasmic endoribonuclease and exoribonuclease of Trypanosoma brucei Mol. Biochem. Parasitol. 15 1985 37 47
    • (1985) Mol. Biochem. Parasitol. , vol.15 , pp. 37-47
    • Gbenle, G.O1
  • 175
    • 0017739098 scopus 로고
    • Purification and mode of action of exoribonuclease from bovine brain
    • A Cuba Purification and mode of action of exoribonuclease from bovine brain J. Biol. Chem. 252 1977 6416 6420
    • (1977) J. Biol. Chem. , vol.252 , pp. 6416-6420
    • Cuba, A1
  • 176
    • 0025893886 scopus 로고
    • A nuclear micrococcal-sensitive, ATP-dependent exoribonuclease degrades uncapped but not capped RNA substrates
    • K.G Murthy P Park J.L Manley A nuclear micrococcal-sensitive, ATP-dependent exoribonuclease degrades uncapped but not capped RNA substrates Nucleic Acids Res. 19 1991 2685 2692
    • (1991) Nucleic Acids Res. , vol.19 , pp. 2685-2692
    • Murthy, K.G1    Park, P2    Manley, J.L3
  • 177
    • 14444284102 scopus 로고    scopus 로고
    • Identification and characterization of a nuclease specific for the 3′ end of the U6 small nuclear RNA
    • B.L Booth Jr. B.F Pugh Identification and characterization of a nuclease specific for the 3′ end of the U6 small nuclear RNA J. Biol. Chem. 272 1997 984 991
    • (1997) J. Biol. Chem. , vol.272 , pp. 984-991
    • Booth, B.L1    Pugh, B.F2
  • 178
    • 0027156340 scopus 로고
    • A 5′ exoribonuclease from cytoplasmic extracts of mouse sarcoma 180 ascites cells
    • M Coutts G Brawerman A 5′ exoribonuclease from cytoplasmic extracts of mouse sarcoma 180 ascites cells Biochim. Biophys. Acta 1173 1993 57 62
    • (1993) Biochim. Biophys. Acta , vol.1173 , pp. 57-62
    • Coutts, M1    Brawerman, G2
  • 179
    • 0029921407 scopus 로고    scopus 로고
    • Purification and characterization of a 5′ to 3′ exoribonuclease from rabbit reticulocytes that degrades capped and uncapped RNAs
    • S Somoskeoy M.N Rao L.I Slobin Purification and characterization of a 5′ to 3′ exoribonuclease from rabbit reticulocytes that degrades capped and uncapped RNAs Eur. J. Biochem. 237 1996 171 179
    • (1996) Eur. J. Biochem. , vol.237 , pp. 171-179
    • Somoskeoy, S1    Rao, M.N2    Slobin, L.I3
  • 180
    • 0025391233 scopus 로고
    • Oligonucleotidase activity of phosphodiesterase from the fruit body of Flammulina velutipes
    • S Kurosawa A.M Shimabuku H Ishizawa K Sen Oligonucleotidase activity of phosphodiesterase from the fruit body of Flammulina velutipes Agric. Biol. Chem. 54 1990 587 592
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 587-592
    • Kurosawa, S1    Shimabuku, A.M2    Ishizawa, H3    Sen, K4
  • 181
    • 0030893062 scopus 로고    scopus 로고
    • A ribonuclease specific for inosine-containing RNA: a potential role in antiviral defence?
    • A.D Scadden C.W Smith A ribonuclease specific for inosine-containing RNA: a potential role in antiviral defence? EMBO J. 16 1997 2140 2149
    • (1997) EMBO J. , vol.16 , pp. 2140-2149
    • Scadden, A.D1    Smith, C.W2
  • 182
    • 0030779484 scopus 로고    scopus 로고
    • Polyphosphate kinase is a component of the Escherichia coli RNA degradosome
    • E Blum B Py A.J Carpousis C.F Higgins Polyphosphate kinase is a component of the Escherichia coli RNA degradosome Mol. Microbiol. 26 1997 387 398
    • (1997) Mol. Microbiol. , vol.26 , pp. 387-398
    • Blum, E1    Py, B2    Carpousis, A.J3    Higgins, C.F4
  • 183
    • 0032539906 scopus 로고    scopus 로고
    • RNA components of Escherichia coli degradosome: evidence for rRNA decay
    • D.A Bessarab V.R Kaberdin C.L Wei G.G Lion S Lin-Chao RNA components of Escherichia coli degradosome: evidence for rRNA decay 6th ed. Proc. Natl. Acad. Sci. USA 95 1998 3157 3161
    • (1998) , pp. 3157-3161
    • Bessarab, D.A1    Kaberdin, V.R2    Wei, C.L3    Lion, G.G4    Lin-Chao, S5
  • 185
    • 0032578486 scopus 로고    scopus 로고
    • The endoribonucleolytic N-terminal half of Escherichia coli RNase E is evolutionarily conserved in Synechocystis sp. and other bacteria but not the C-terminal half, which is sufficient for degradosome assembly
    • V.R Kaberdin A Miczak J.S Jakobsen S Lin-Chao K.J McDowall A von Gabain The endoribonucleolytic N-terminal half of Escherichia coli RNase E is evolutionarily conserved in Synechocystis sp. and other bacteria but not the C-terminal half, which is sufficient for degradosome assembly 6th ed. Proc. Natl. Acad. Sci. USA 95 1998 11637 11642
    • (1998) , pp. 11637-11642
    • Kaberdin, V.R1    Miczak, A2    Jakobsen, J.S3    Lin-Chao, S4    McDowall, K.J5    von Gabain, A6
  • 186
    • 0033214259 scopus 로고    scopus 로고
    • Reconstitution of a minimal RNA degradosome demonstrates functional coordination between a 3′ exonuclease and a DEADbox RNA helicase
    • G.A Coburn X Miao D.J Briant G.A Mackie Reconstitution of a minimal RNA degradosome demonstrates functional coordination between a 3′ exonuclease and a DEADbox RNA helicase Genes Dev. 13 1999 2594 2603
    • (1999) Genes Dev. , vol.13 , pp. 2594-2603
    • Coburn, G.A1    Miao, X2    Briant, D.J3    Mackie, G.A4
  • 187
    • 0018582283 scopus 로고
    • RNase E, an RNA processing enzyme from Escherichia coli
    • T.K Misra D Apirion RNase E, an RNA processing enzyme from Escherichia coli J. Biol. Chem. 254 1979 11154 11159
    • (1979) J. Biol. Chem. , vol.254 , pp. 11154-11159
    • Misra, T.K1    Apirion, D2
  • 188
    • 0033577789 scopus 로고    scopus 로고
    • RNase G (CafA protein) and RNase E are both required for the 5′ maturation of 16S ribosomal RNA
    • Z Li S Pandit M.P Deutscher RNase G (CafA protein) and RNase E are both required for the 5′ maturation of 16S ribosomal RNA EMBO J. 18 1999 2878 2885
    • (1999) EMBO J. , vol.18 , pp. 2878-2885
    • Li, Z1    Pandit, S2    Deutscher, M.P3
  • 189
    • 0030468099 scopus 로고    scopus 로고
    • Polyadenylation accelerates degradation of chloroplast mRNA
    • J Kudla R Hayes W Gruissem Polyadenylation accelerates degradation of chloroplast mRNA EMBO J. 15 1996 7137 7146
    • (1996) EMBO J. , vol.15 , pp. 7137-7146
    • Kudla, J1    Hayes, R2    Gruissem, W3
  • 190
    • 0033133680 scopus 로고    scopus 로고
    • Degrading chloroplast mRNA: the role of polyadenylation
    • R Hayes J Kudla W Gruissem Degrading chloroplast mRNA: the role of polyadenylation Trends Biochem. Sci. 24 1999 199 202
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 199-202
    • Hayes, R1    Kudla, J2    Gruissem, W3
  • 191
    • 0028813371 scopus 로고
    • Characterization of a novel plant poly(A) polymerise
    • J Das Gupta Q Li A.B Thompson A.G Hunt Characterization of a novel plant poly(A) polymerise Plant Sci. 110 1995 215 226
    • (1995) Plant Sci. , vol.110 , pp. 215-226
    • Das Gupta, J1    Li, Q2    Thompson, A.B3    Hunt, A.G4
  • 192
    • 0029807307 scopus 로고    scopus 로고
    • A plant poly(A) polymerase requires a novel RNAbinding protein for activity
    • Q.S Li J.D Gupta A.G Hunt A plant poly(A) polymerase requires a novel RNAbinding protein for activity J. Biol. Chem. 271 1996 19831 19835
    • (1996) J. Biol. Chem. , vol.271 , pp. 19831-19835
    • Li, Q.S1    Gupta, J.D2    Hunt, A.G3
  • 193
    • 0027512243 scopus 로고
    • Isolation and characterization of an NTPdependent 3′-exoribonuclease from mitochondria of Saccharomyces cerevisiae
    • J Min R.M Heuertz H.P Zassenhaus Isolation and characterization of an NTPdependent 3′-exoribonuclease from mitochondria of Saccharomyces cerevisiae J. Biol. Chem. 268 1993 7350 7357
    • (1993) J. Biol. Chem. , vol.268 , pp. 7350-7357
    • Min, J1    Heuertz, R.M2    Zassenhaus, H.P3
  • 194
    • 0030034498 scopus 로고    scopus 로고
    • The DExH box protein Suv3p is a component of a yeast mitochondrial 3′-to-5′ exoribonuclease that suppresses group I intron toxicity
    • S.P Margossian H Li H.P Zassenhaus R.A Butow The DExH box protein Suv3p is a component of a yeast mitochondrial 3′-to-5′ exoribonuclease that suppresses group I intron toxicity Cell 84 1996 199 209
    • (1996) Cell , vol.84 , pp. 199-209
    • Margossian, S.P1    Li, H2    Zassenhaus, H.P3    Butow, R.A4


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