메뉴 건너뛰기




Volumn 23, Issue 3, 1999, Pages 371-390

Function, mechanism and regulation of bacterial ribonucleases

Author keywords

Bacterial ribonuclease; Post transcriptional regulation; Ribonuclease III; RNA decay; RNA maturation

Indexed keywords

EXORIBONUCLEASE; NUCLEASE; PANCREATIC RIBONUCLEASE; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE; RIBONUCLEASE; RIBONUCLEASE III; RIBONUCLEASE P;

EID: 0032932638     PISSN: 01686445     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-6445(99)00013-3     Document Type: Review
Times cited : (210)

References (148)
  • 1
    • 0002860014 scopus 로고
    • mRNA degradation in bacterial cells: An overview
    • (Belasco, J.G. and Brawerman, G., Eds.), Academic Press, New York
    • Belasco, J.G. (1993) mRNA degradation in bacterial cells: An overview. In: Control of Messenger RNA Stability (Belasco, J.G. and Brawerman, G., Eds.), pp. 3-12. Academic Press, New York.
    • (1993) In: Control of Messenger RNA Stability , pp. 3-12
    • Belasco, J.G.1
  • 2
    • 0022981322 scopus 로고
    • Nucleolytic processing of ribonucleic acid transcripts in procaryotes
    • King T.C., Sirdeskmukh R., Schlessinger D. Nucleolytic processing of ribonucleic acid transcripts in procaryotes. Microbiol. Rev. 50:1986;428-451.
    • (1986) Microbiol. Rev. , vol.50 , pp. 428-451
    • King, T.C.1    Sirdeskmukh, R.2    Schlessinger, D.3
  • 3
    • 0010459080 scopus 로고
    • RNA maturation nucleases
    • (Linn, S.M., Lloyd, R.S. and Roberts, R.J., Eds.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Deutscher, M.P. (1993) RNA maturation nucleases. In: Nucleases: 2nd edn. (Linn, S.M., Lloyd, R.S. and Roberts, R.J., Eds.), pp. 377-406. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1993) In: Nucleases: 2nd Edn. , pp. 377-406
    • Deutscher, M.P.1
  • 4
    • 0027518120 scopus 로고
    • Ribonuclease multiplicity, diversity and complexity
    • Deutscher M.P. Ribonuclease multiplicity, diversity and complexity. J. Biol. Chem. 268:1993;13011-13014.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13011-13014
    • Deutscher, M.P.1
  • 5
    • 0001899053 scopus 로고    scopus 로고
    • Escherichia coli ribonucleases: Paradigms for understanding cellular RNA metabolism and regulation
    • (D'Alessio, G. and Riordan, J.F., Eds.), Academic Press, New York
    • Nicholson, A.W. (1997) Escherichia coli ribonucleases: paradigms for understanding cellular RNA metabolism and regulation. In: Ribonucleases: Structures and Functions (D'Alessio, G. and Riordan, J.F., Eds.), pp. 1-49. Academic Press, New York.
    • (1997) In: Ribonucleases: Structures and Functions , pp. 1-49
    • Nicholson, A.W.1
  • 6
    • 0030576503 scopus 로고    scopus 로고
    • Maturation pathways for E. coli tRNA precursors a random multienzyme process in vivo
    • Li A., Deutscher M.P. 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, A.1    Deutscher, M.P.2
  • 7
    • 0025153770 scopus 로고
    • Mechanism and regulation of bacterial ribosomal RNA processing
    • Srivastava A.K., Schlessinger D. Mechanism and regulation of bacterial ribosomal RNA processing. Annu. Rev. Microbiol. 44:1990;105-129.
    • (1990) Annu. Rev. Microbiol. , vol.44 , pp. 105-129
    • Srivastava, A.K.1    Schlessinger, D.2
  • 8
    • 0032539857 scopus 로고    scopus 로고
    • 3′ exoribonucleolytic trimming is a common feature of the maturation of small, stable RNAs in Escherichia coli
    • Li Z., Pandit S., Deutscher M.P. 3′ exoribonucleolytic trimming is a common feature of the maturation of small, stable RNAs in Escherichia coli. Proc. Natl. Acad. Sci. USA. 95:1998;2856-2861.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2856-2861
    • Li, Z.1    Pandit, S.2    Deutscher, M.P.3
  • 9
    • 0020964297 scopus 로고
    • Complete nucleotide sequence of bacteriophage T7 DNA and the location of T7 genetic elements
    • Dunn J.J., Studier F.W. Complete nucleotide sequence of bacteriophage T7 DNA and the location of T7 genetic elements. J. Mol. Biol. 166:1983;477-535.
    • (1983) J. Mol. Biol. , vol.166 , pp. 477-535
    • Dunn, J.J.1    Studier, F.W.2
  • 10
    • 0029059329 scopus 로고
    • Prokaryotic introns and inteins: A panoply of form and function
    • Belfort M., Reaban M.E., Coetzee T., Dalgaard J.Z. Prokaryotic introns and inteins: a panoply of form and function. J. Bacteriol. 177:1995;3897-3903.
    • (1995) J. Bacteriol. , vol.177 , pp. 3897-3903
    • Belfort, M.1    Reaban, M.E.2    Coetzee, T.3    Dalgaard, J.Z.4
  • 12
    • 0032617132 scopus 로고    scopus 로고
    • Degradation of mRNA in Escherichia coli: An old problem with some new twists
    • Coburn G.A., Mackie G.A. Degradation of mRNA in Escherichia coli: an old problem with some new twists. Prog. Nucleic Acids Res. Mol. Biol. 62:1999;55-108.
    • (1999) Prog. Nucleic Acids Res. Mol. Biol. , vol.62 , pp. 55-108
    • Coburn, G.A.1    Mackie, G.A.2
  • 13
    • 0032569032 scopus 로고    scopus 로고
    • Reconstitution of the degradation of the mRNA for ribosomal protein S20 with purified enzymes
    • Coburn G.A., Mackie G.A. Reconstitution of the degradation of the mRNA for ribosomal protein S20 with purified enzymes. J. Mol. Biol. 279:1998;1061-1074.
    • (1998) J. Mol. Biol. , vol.279 , pp. 1061-1074
    • Coburn, G.A.1    Mackie, G.A.2
  • 14
    • 0003011967 scopus 로고
    • Translation and mRNA stability in bacteria: A complex relationship
    • (Belasco, J.G. and Brawerman, G., Eds.), Academic Press, New York
    • Petersen, C. (1993) Translation and mRNA stability in bacteria: a complex relationship. In: Control of mRNA stability (Belasco, J.G. and Brawerman, G., Eds.), pp. 117-145. Academic Press, New York.
    • (1993) In: Control of Mrna Stability , pp. 117-145
    • Petersen, C.1
  • 15
    • 0032541436 scopus 로고    scopus 로고
    • Ribosomes inhibit an RNase E cleavage which induces the decay of the rpsO mRNA of Escherichia coli
    • Braun F., Le Derout J., Régnier P. Ribosomes inhibit an RNase E cleavage which induces the decay of the rpsO mRNA of Escherichia coli. EMBO J. 17:1998;4790-4797.
    • (1998) EMBO J. , vol.17 , pp. 4790-4797
    • Braun, F.1    Le Derout, J.2    Régnier, P.3
  • 16
    • 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., Ehretsman C., Krisch H.M. Copurification of E. coli RNase 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.J.1    Van Houwe, G.2    Ehretsman, C.3    Krisch, H.M.4
  • 17
    • 0027945686 scopus 로고
    • A protein complex mediating mRNA degradation in Escherichia coli
    • Py B., Causton H., Mudd E.A., Higgins C.F. A protein complex mediating mRNA degradation in Escherichia coli. Mol. Microbiol. 14:1994;717-729.
    • (1994) Mol. Microbiol. , vol.14 , pp. 717-729
    • Py, B.1    Causton, H.2    Mudd, E.A.3    Higgins, C.F.4
  • 18
    • 1842367307 scopus 로고    scopus 로고
    • Processing of the rne transcript by an RNase E-independent amino acid-dependent mechanism
    • Woo W.-M., Lin-Chao S. Processing of the rne transcript by an RNase E-independent amino acid-dependent mechanism. J. Biol. Chem. 272:1997;15516-15520.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15516-15520
    • Woo, W.-M.1    Lin-Chao, S.2
  • 19
    • 0031951386 scopus 로고    scopus 로고
    • MRNA stabilization by the ompA 5′ untranslated region: Two protective elements hinder distinct pathways for mRNA degradation
    • Arnold T.E., Yu J., Belasco J.G. mRNA stabilization by the ompA 5′ untranslated region: two protective elements hinder distinct pathways for mRNA degradation. RNA. 4:1998;319-330.
    • (1998) RNA , vol.4 , pp. 319-330
    • Arnold, T.E.1    Yu, J.2    Belasco, J.G.3
  • 21
    • 0031894053 scopus 로고    scopus 로고
    • Escherichia coli mrsC is an allele of hflB, encoding a membrane-associated ATPase and protease that is required for mRNA decay
    • Wang R.-F., O'Hara E.B., Aldea M., Bargmann C.I., Gromley H., Kushner S.R. Escherichia coli mrsC is an allele of hflB, encoding a membrane-associated ATPase and protease that is required for mRNA decay. J. Bacteriol. 180:1998;1929-1938.
    • (1998) J. Bacteriol. , vol.180 , pp. 1929-1938
    • Wang, R.-F.1    O'Hara, E.B.2    Aldea, M.3    Bargmann, C.I.4    Gromley, H.5    Kushner, S.R.6
  • 22
    • 0030702085 scopus 로고    scopus 로고
    • The exosome: A conserved eukaryotic RNA processing complex containing multiple 3′→5′ exoribonucleases
    • Mitchell P., Petfalski E., Shevchenko A., Mann M., Tollervey D. 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, P.1    Petfalski, E.2    Shevchenko, A.3    Mann, M.4    Tollervey, D.5
  • 23
    • 0345494900 scopus 로고
    • Eukaryotic nucleases and mRNA turnover
    • (Belasco, J.G. and Brawerman, G., Eds.), Academic Press, New York
    • Stevens, A. (1993) Eukaryotic nucleases and mRNA turnover. In: Control of Messenger RNA Stability (Belasco, J.G. and Brawerman, G., Eds.), pp. 449-471. Academic Press, New York.
    • (1993) In: Control of Messenger RNA Stability , pp. 449-471
    • Stevens, A.1
  • 24
    • 0023088853 scopus 로고
    • Nucleotide sequence of the pnp gene of Escherichia coli encoding polynucleotide phosphorylase
    • Régnier P., Grunberg-Manago M., Portier C. Nucleotide sequence of the pnp gene of Escherichia coli encoding polynucleotide phosphorylase. J. Biol. Chem. 262:1987;63-68.
    • (1987) J. Biol. Chem. , vol.262 , pp. 63-68
    • Régnier, P.1    Grunberg-Manago, M.2    Portier, C.3
  • 25
    • 77956896894 scopus 로고
    • Polynucleotide Phosphorylase
    • (Boyer, P., Ed.), Academic Press, New York
    • Littauer, U.Z. and Soreq, H. (1982) Polynucleotide Phosphorylase. In: The Enzymes (Boyer, P., Ed.), pp. 517-553. Academic Press, New York.
    • (1982) In: The Enzymes , pp. 517-553
    • Littauer, U.Z.1    Soreq, H.2
  • 26
    • 0030023583 scopus 로고    scopus 로고
    • In vitro processing activity of Bacillus subtilis polynucleotide phosphorylase
    • Mitra S., Hue K., Bechhofer D.H. In vitro processing activity of Bacillus subtilis polynucleotide phosphorylase. Mol. Microbiol. 19:1996;329-342.
    • (1996) Mol. Microbiol. , vol.19 , pp. 329-342
    • Mitra, S.1    Hue, K.2    Bechhofer, D.H.3
  • 27
    • 0031734294 scopus 로고    scopus 로고
    • Decay of ermC mRNA in a polynucleotide phosphorylase mutant of Bacillus subtilis
    • Bechhofer D.H., Wang W. 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.H.1    Wang, W.2
  • 28
    • 0026334860 scopus 로고
    • Enzymatic basis for hydrolytic versus phosphorolytic mRNA degradation in Escherichia coli and Bacillus subtilis
    • Deutscher M.P., Reuven N.B. Enzymatic basis for hydrolytic versus phosphorolytic mRNA degradation in Escherichia coli and Bacillus subtilis. Proc. Natl. Acad. Sci. USA. 88:1991;3277-3280.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3277-3280
    • Deutscher, M.P.1    Reuven, N.B.2
  • 29
    • 0031468077 scopus 로고    scopus 로고
    • Functional overlap of tRNA nucleotidyltransferase, poly(A) polymerase I, and polynucleotide phosphorylase
    • Reuven N.B., Zhou Z., Deutscher M.P. 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.B.1    Zhou, Z.2    Deutscher, M.P.3
  • 30
    • 0031939953 scopus 로고    scopus 로고
    • Polyribonucleotide phosphorylase is a double-stranded DNA-binding protein
    • Zhang P., Vigne J.-L., Mellon S.H. Polyribonucleotide phosphorylase is a double-stranded DNA-binding protein. DNA Cell Biol. 17:1998;169-175.
    • (1998) DNA Cell Biol. , vol.17 , pp. 169-175
    • Zhang, P.1    Vigne, J.-L.2    Mellon, S.H.3
  • 31
    • 0030047027 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase is necessary for competence development in Bacillus subtilis
    • Luttinger A., Hahn J., Dubnau D. 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, A.1    Hahn, J.2    Dubnau, D.3
  • 32
    • 0030002447 scopus 로고    scopus 로고
    • Properties of a Bacillus subtilis polynucleotide phosphorylase deletion strain
    • Wang W., Bechhofer D.H. Properties of a Bacillus subtilis polynucleotide phosphorylase deletion strain. J. Bacteriol. 178:1996;2375-2382.
    • (1996) J. Bacteriol. , vol.178 , pp. 2375-2382
    • Wang, W.1    Bechhofer, D.H.2
  • 33
    • 0023099212 scopus 로고
    • Tn5 insertion in the polynucleotide phosphorylase (pnp) gene in Escherichia coli increases susceptibility to antibiotics
    • McMurray L.M., Levy S.B. Tn5 insertion in the polynucleotide phosphorylase (pnp) gene in Escherichia coli increases susceptibility to antibiotics. J. Bacteriol. 169:1987;1321-1324.
    • (1987) J. Bacteriol. , vol.169 , pp. 1321-1324
    • McMurray, L.M.1    Levy, S.B.2
  • 34
    • 0023186464 scopus 로고
    • Induction of proteins in response to low temperature in Escherichia coli
    • Jones P.G., vanBogelen R.A., Neidhardt F.C. 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.G.1    Vanbogelen, R.A.2    Neidhardt, F.C.3
  • 35
    • 0028286232 scopus 로고
    • The gene coding for polynucleotide phosphorylase in Photorhabdus sp. strain K122 is induced at low temperatures
    • Clarke D.J., Dowds B.C.A. The gene coding for polynucleotide 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.J.1    Dowds, B.C.A.2
  • 36
    • 7144226568 scopus 로고    scopus 로고
    • The psychrotrophic bacterium Yersinia enterocolitica requires expression of pnp, the gene for polynucleotide phosphorylase, for growth at low temperature (5°C)
    • Goverde R.L.J., Huis in't Veld J.H.J., Kusters J.G., Mooi F.R. The psychrotrophic bacterium Yersinia enterocolitica requires expression of pnp, the gene for polynucleotide phosphorylase, for growth at low temperature (5°C). Mol. Microbiol. 28:1998;555-569.
    • (1998) Mol. Microbiol. , vol.28 , pp. 555-569
    • Goverde, R.L.J.1    Huis In't Veld, J.H.J.2    Kusters, J.G.3    Mooi, F.R.4
  • 37
    • 0002807705 scopus 로고
    • tRNA processing nucleases
    • (Söll, D. and RajBhandary, U., Eds.), ASM Press, Washington, DC
    • Deutscher, M.P. (1995) tRNA processing nucleases. In: tRNA: Structure, Biosynthesis and Function (Söll, D. and RajBhandary, U., Eds.), pp. 51-65. ASM Press, Washington, DC.
    • (1995) In: Trna: Structure, Biosynthesis and Function , pp. 51-65
    • Deutscher, M.P.1
  • 38
    • 0030836805 scopus 로고    scopus 로고
    • Comparative sequence analysis of ribonucleases HII, II, II, PH and D
    • Mian I.S. Comparative sequence analysis of ribonucleases HII, II, II, PH and D. Nucleic Acids Res. 25:1997;3187-3195.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3187-3195
    • Mian, I.S.1
  • 39
    • 0030860690 scopus 로고    scopus 로고
    • An essential function for the phosphate-dependent exoribonucleases RNase PH and polynucleotide phosphorylase
    • Zhou Z., Deutscher M.P. An essential function for the phosphate-dependent exoribonucleases RNase PH and polynucleotide phosphorylase. J. Bacteriol. 179:1997;4391-4395.
    • (1997) J. Bacteriol. , vol.179 , pp. 4391-4395
    • Zhou, Z.1    Deutscher, M.P.2
  • 40
    • 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
    • Benard L., Carroll K., Valle R.C.P., Wickner R.B. 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, L.1    Carroll, K.2    Valle, R.C.P.3    Wickner, R.B.4
  • 41
    • 0029071256 scopus 로고
    • Precise physical mapping of the Escherichia coli rnb gene, encoding ribonuclease II
    • Zilhao R., Caillet J., Regnier P., Arraiano C.M. Precise physical mapping of the Escherichia coli rnb gene, encoding ribonuclease II. Mol. Gen. Genet. 248:1995;242-246.
    • (1995) Mol. Gen. Genet. , vol.248 , pp. 242-246
    • Zilhao, R.1    Caillet, J.2    Regnier, P.3    Arraiano, C.M.4
  • 42
    • 77956939091 scopus 로고
    • RNases I, II and IV of Escherichia coli
    • (Boyer, P., Ed.), Academic Press, New York
    • Shen, V. and Schlessinger, D. (1982) RNases I, II and IV of Escherichia coli. In: The Enzymes (Boyer, P., Ed.), pp. 501-515. Academic Press, New York.
    • (1982) In: The Enzymes , pp. 501-515
    • Shen, V.1    Schlessinger, D.2
  • 43
    • 0030041546 scopus 로고    scopus 로고
    • Overexpression, purification and properties of Escherichia coli ribonuclease II
    • Coburn G.A., Mackie G.A. 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.A.1    Mackie, G.A.2
  • 44
    • 0003395950 scopus 로고
    • Polynucleotide phosphorylase and ribonuclease II are required for cell viability and mRNA turnover in Escherichia coli K-12
    • Donovan W.P., Kushner S.R. Polynucleotide phosphorylase and ribonuclease II are required for cell viability and mRNA turnover in Escherichia coli K-12. Proc. Natl. Acad. Sci. USA. 83:1986;120-124.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 120-124
    • Donovan, W.P.1    Kushner, S.R.2
  • 45
    • 0032486392 scopus 로고    scopus 로고
    • The vacB gene required for virulence in Shigella flexneri and Escherichia coli encodes the exoribonuclease RNase R
    • Cheng Z.-F., Zuo Y., Li Z., Rudd K.E., Deutscher M.P. 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.-F.1    Zuo, Y.2    Li, Z.3    Rudd, K.E.4    Deutscher, M.P.5
  • 46
    • 0023705439 scopus 로고
    • Escherichia coli RNase D: Sequencing of the rnd structural gene and purification of the overexpressed protein
    • Zhang J., Deutscher M.P. 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.1    Deutscher, M.P.2
  • 47
    • 0019455383 scopus 로고
    • Escherichia coli RNase D: Catalytic properties and substrate specificity
    • Cudny H., Zaniewski R., Deutscher M.P. 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, H.1    Zaniewski, R.2    Deutscher, M.P.3
  • 48
    • 0019482352 scopus 로고
    • Alteration of Escherichia coli RNase D by infection with bacteriophage T4
    • Cudny H., Roy P., Deutscher M.P. Alteration of Escherichia coli RNase D by infection with bacteriophage T4. Biochem. Biophys. Res. Commun. 98:1981;337-345.
    • (1981) Biochem. Biophys. Res. Commun. , vol.98 , pp. 337-345
    • Cudny, H.1    Roy, P.2    Deutscher, M.P.3
  • 49
    • 0031241595 scopus 로고    scopus 로고
    • A conserved ancient domain joins the growing superfamily of 3′-5′ exonucleases
    • Koonin E.V. A conserved ancient domain joins the growing superfamily of 3′-5′ exonucleases. Curr. Biol. 7:1997;R604-R606.
    • (1997) Curr. Biol. , vol.7
    • Koonin, E.V.1
  • 50
    • 0026489712 scopus 로고
    • Sequence and transcriptional analysis of the Escherichia coli rnt gene encoding RNase T
    • Huang S., Deutscher M.P. Sequence and transcriptional analysis of the Escherichia coli rnt gene encoding RNase T. J. Biol. Chem. 267:1992;25609-25613.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25609-25613
    • Huang, S.1    Deutscher, M.P.2
  • 51
    • 0031962032 scopus 로고    scopus 로고
    • RNase T is related to dnaQ and family C DNA polymerases
    • Ito J., Braithwaite D.K. RNase T is related to dnaQ and family C DNA polymerases. Mol. Microbiol. 27:1998;235-237.
    • (1998) Mol. Microbiol. , vol.27 , pp. 235-237
    • Ito, J.1    Braithwaite, D.K.2
  • 52
    • 0030447708 scopus 로고    scopus 로고
    • Identification and characterization of the Escherichia coli rbn gene encoding the tRNA processing enzyme RNase BN
    • Callahan C., Deutscher M.P. 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, C.1    Deutscher, M.P.2
  • 53
    • 0031924593 scopus 로고    scopus 로고
    • Oligoribonuclease is encoded by a highly conserved gene in the 3′-5′ exonuclease superfamily
    • Zhang X., Zhu L., Deutscher M.P. 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, X.1    Zhu, L.2    Deutscher, M.P.3
  • 54
    • 0025202569 scopus 로고
    • Cloning and sequencing of the gene encoding Escherichia coli ribonuclease I. Exact physical mapping using the genome library
    • Meador J., Kennell D. Cloning and sequencing of the gene encoding Escherichia coli ribonuclease I. Exact physical mapping using the genome library. Gene. 95:1990;1-7.
    • (1990) Gene , vol.95 , pp. 1-7
    • Meador, J.1    Kennell, D.2
  • 55
    • 0025923135 scopus 로고
    • RNase I*, a form of RNase I, and mRNA degradation in Escherichia coli
    • Cannistraro V.J., Kennell D. RNase I*, a form of RNase I, and mRNA degradation in Escherichia coli. J. Bacteriol. 173:1991;4653-4659.
    • (1991) J. Bacteriol. , vol.173 , pp. 4653-4659
    • Cannistraro, V.J.1    Kennell, D.2
  • 56
    • 0014528911 scopus 로고
    • Induction by mercuric ion of extensive degradation of cellular ribonucleic acid in Escherichia coli
    • Beppu T., Arima K. Induction by mercuric ion of extensive degradation of cellular ribonucleic acid in Escherichia coli. J. Bacteriol. 98:1969;888-897.
    • (1969) J. Bacteriol. , vol.98 , pp. 888-897
    • Beppu, T.1    Arima, K.2
  • 57
    • 34250257369 scopus 로고
    • RNA processing and degradation by RNase III
    • (Belasco, J.G. and Brawerman, G., Eds.), Academic Press, New York
    • Court, D. (1993) RNA processing and degradation by RNase III. In: Control of Messenger RNA Stability (Belasco, J.G. and Brawerman, G., Eds.), pp. 71-116. Academic Press, New York.
    • (1993) In: Control of Messenger RNA Stability , pp. 71-116
    • Court, D.1
  • 58
    • 0029681842 scopus 로고    scopus 로고
    • Structure, reactivity and biology of double-stranded RNA
    • Nicholson A.W. Structure, reactivity and biology of double-stranded RNA. Prog. Nucleic Acids Res. Mol. Biol. 52:1996;1-65.
    • (1996) Prog. Nucleic Acids Res. Mol. Biol. , vol.52 , pp. 1-65
    • Nicholson, A.W.1
  • 59
    • 77956941091 scopus 로고
    • Ribonuclease III
    • (Boyer, P., Ed.), Academic Press, New York
    • Dunn, J.J. (1982). Ribonuclease III. In: The Enzymes (Boyer, P., Ed.), pp. 485-499. Academic Press, New York.
    • (1982) In: The Enzymes , pp. 485-499
    • Dunn, J.J.1
  • 60
    • 0017808494 scopus 로고
    • Altered mRNA metabolism in ribonuclease III-deficient strains of Escherichia coli
    • Talkad V., Achord D., Kennell D. Altered mRNA metabolism in ribonuclease III-deficient strains of Escherichia coli. J. Bacteriol. 135:1978;528-541.
    • (1978) J. Bacteriol. , vol.135 , pp. 528-541
    • Talkad, V.1    Achord, D.2    Kennell, D.3
  • 61
    • 0021347298 scopus 로고
    • RNase III cleavage is obligate for maturation but not for function of Escherichia coli pre-23S rRNA
    • King T.C., Sirdeshmukh R., Schlessinger D. RNase III cleavage is obligate for maturation but not for function of Escherichia coli pre-23S rRNA. Proc. Natl. Acad. Sci. USA. 81:1984;185-188.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 185-188
    • King, T.C.1    Sirdeshmukh, R.2    Schlessinger, D.3
  • 62
    • 0028829125 scopus 로고
    • The minimal gene complement of Mycoplasma genitalium
    • Fraser C.M., Gocayne J.D., Whaite O., et al. The minimal gene complement of Mycoplasma genitalium. Science. 270:1995;397-403.
    • (1995) Science , vol.270 , pp. 397-403
    • Fraser, C.M.1    Gocayne, J.D.2    Whaite, O.3
  • 63
    • 0029879217 scopus 로고    scopus 로고
    • Identification and analysis of the rnc gene for RNase III in Rhodobacter capsulatus
    • Rauhut R., Jager A., Conrad C., Klug G. Identification and analysis of the rnc gene for RNase III in Rhodobacter capsulatus. Nucleic Acids Res. 24:1996;1241-1251.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 1241-1251
    • Rauhut, R.1    Jager, A.2    Conrad, C.3    Klug, G.4
  • 64
    • 0032189582 scopus 로고    scopus 로고
    • Different cleavage specificities of RNases III from Rhodobacter capsulatus and Escherichia coli
    • Conrad C., Rauhut R., Klug G. Different cleavage specificities of RNases III from Rhodobacter capsulatus and Escherichia coli. Nucleic Acids Res. 26:1998;4446-4453.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4446-4453
    • Conrad, C.1    Rauhut, R.2    Klug, G.3
  • 65
    • 0030690925 scopus 로고    scopus 로고
    • Bacillus subtilis RNase III gene: Cloning, function of the gene in Escherichia coli, and construction of Bacillus subtilis strains with altered rnc loci
    • Wang W., Bechhofer D.H. Bacillus subtilis RNase III gene: cloning, function of the gene in Escherichia coli, and construction of Bacillus subtilis strains with altered rnc loci. J. Bacteriol. 179:1997;7379-7385.
    • (1997) J. Bacteriol. , vol.179 , pp. 7379-7385
    • Wang, W.1    Bechhofer, D.H.2
  • 66
    • 0027960972 scopus 로고
    • Substrate specificity of an RNase III-like activity from Bacillus subtilis
    • Mitra S., Bechhofer D.H. Substrate specificity of an RNase III-like activity from Bacillus subtilis. J. Biol. Chem. 269:1994;31450-31456.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31450-31456
    • Mitra, S.1    Bechhofer, D.H.2
  • 67
    • 0025133312 scopus 로고
    • Recognition of exon-intron boundaries by the Halobacterium volcanii tRNA intron endonuclease
    • Thompson L.D., Daniels C.J. Recognition of exon-intron boundaries by the Halobacterium volcanii tRNA intron endonuclease. J. Biol. Chem. 265:1990;18104-18111.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18104-18111
    • Thompson, L.D.1    Daniels, C.J.2
  • 68
    • 0030730242 scopus 로고    scopus 로고
    • Properties of H. volcanii tRNA intron endonuclease reveal a relationship between the Archaeal and Eucaryal tRNA intron processing systems
    • Kleman-Leyer K., Armbruster D.W., Daniels C.J. Properties of H. volcanii tRNA intron endonuclease reveal a relationship between the Archaeal and Eucaryal tRNA intron processing systems. Cell. 89:1997;839-847.
    • (1997) Cell , vol.89 , pp. 839-847
    • Kleman-Leyer, K.1    Armbruster, D.W.2    Daniels, C.J.3
  • 69
    • 0032502894 scopus 로고    scopus 로고
    • Crystal structure and evolution of a transfer RNA splicing enzyme
    • Li H., Trotta C.R., Abelson J. Crystal structure and evolution of a transfer RNA splicing enzyme. Science. 280:1998;279-284.
    • (1998) Science , vol.280 , pp. 279-284
    • Li, H.1    Trotta, C.R.2    Abelson, J.3
  • 70
    • 0029919935 scopus 로고    scopus 로고
    • RNase III cleaves eukaryotic preribosomal RNA at a U3 snoRNP-dependent site
    • Abou Elela S., Igel H., Ares M. RNase III cleaves eukaryotic preribosomal RNA at a U3 snoRNP-dependent site. Cell. 85:1996;115-124.
    • (1996) Cell , vol.85 , pp. 115-124
    • Abou Elela, S.1    Igel, H.2    Ares, M.3
  • 71
    • 0029931692 scopus 로고    scopus 로고
    • Purification and characterization of the Pac1 ribonuclease of Schizosaccharomyces pombe
    • Rotondo G., Frendewey D. Purification and characterization of the Pac1 ribonuclease of Schizosaccharomyces pombe. Nucleic Acids Res. 24:1996;2377-2386.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2377-2386
    • Rotondo, G.1    Frendewey, D.2
  • 72
    • 0030761010 scopus 로고    scopus 로고
    • Substrate structure requirements of the Pac1 ribonuclease from Schizosaccharomyces pombe
    • Rotondo G., Huang J.Y., Frendewey D. Substrate structure requirements of the Pac1 ribonuclease from Schizosaccharomyces pombe. RNA. 3:1997;1182-1193.
    • (1997) RNA , vol.3 , pp. 1182-1193
    • Rotondo, G.1    Huang, J.Y.2    Frendewey, D.3
  • 73
    • 0028285542 scopus 로고
    • Detection of dsRNA-binding domains in RNA helicase A and Drosophila maleless: Implications for monomeric RNA helicases
    • Gibson T.J., Thompson J.D. Detection of dsRNA-binding domains in RNA helicase A and Drosophila maleless: implications for monomeric RNA helicases. Nucleic Acids. Res. 22:1994;2552-2556.
    • (1994) Nucleic Acids. Res. , vol.22 , pp. 2552-2556
    • Gibson, T.J.1    Thompson, J.D.2
  • 74
    • 0030587386 scopus 로고    scopus 로고
    • Analysis of 76 kb of the Chlorella virus PBCV-1 330-kb genome: Map positions 182 to 258
    • Kutish G.F., Li Y., Lu Z., Furuta M., Rock D.L., van Etten J.L. Analysis of 76 kb of the Chlorella virus PBCV-1 330-kb genome: map positions 182 to 258. Virology. 223:1996;303-317.
    • (1996) Virology , vol.223 , pp. 303-317
    • Kutish, G.F.1    Li, Y.2    Lu, Z.3    Furuta, M.4    Rock, D.L.5    Van Etten, J.L.6
  • 75
    • 0028962136 scopus 로고
    • Evolutionary perspective on the structure and function of ribonuclease P, a ribozyme
    • Pace N.R., Brown J.W. Evolutionary perspective on the structure and function of ribonuclease P, a ribozyme. J. Bacteriol. 177:1995;1919-1928.
    • (1995) J. Bacteriol. , vol.177 , pp. 1919-1928
    • Pace, N.R.1    Brown, J.W.2
  • 76
    • 0031711821 scopus 로고    scopus 로고
    • Ribonuclease P: Unity and diversity in a tRNA processing ribozyme
    • Frank D.N., Pace N.R. Ribonuclease P: Unity and diversity in a tRNA processing ribozyme. Annu. Rev. Biochem. 67:1998;153-180.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 153-180
    • Frank, D.N.1    Pace, N.R.2
  • 77
    • 0031000662 scopus 로고    scopus 로고
    • RNase E: Still a wonderfully mysterious enzyme
    • Cohen S.N., McDowall K.J. RNase E: still a wonderfully mysterious enzyme. Mol. Microbiol. 23:1997;1099-1106.
    • (1997) Mol. Microbiol. , vol.23 , pp. 1099-1106
    • Cohen, S.N.1    McDowall, K.J.2
  • 78
    • 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
    • Kaberdin V.R., Miczak A., Jakobsen J.S., Lin-Chao S., McDowall K.J., von Gabain A. 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. Proc. Natl. Acad. Sci. USA. 95:1998;11637-11642.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11637-11642
    • Kaberdin, V.R.1    Miczak, A.2    Jakobsen, J.S.3    Lin-Chao, S.4    McDowall, K.J.5    Von Gabain, A.6
  • 79
    • 0031547969 scopus 로고    scopus 로고
    • Processing of the Bacillus subtilis thrS leader mRNA is RNase E-dependent in Escherichia coli
    • Condon C., Putzer H., Luo D., Grunberg-Manago M. Processing of the Bacillus subtilis thrS leader mRNA is RNase E-dependent in Escherichia coli. J. Mol. Biol. 268:1997;235-242.
    • (1997) J. Mol. Biol. , vol.268 , pp. 235-242
    • Condon, C.1    Putzer, H.2    Luo, D.3    Grunberg-Manago, M.4
  • 80
    • 0028099776 scopus 로고
    • Ard-1: A human gene that reverses the effects of temperature-sensitive and deletion mutations in the Escherichia coli rne gene and encodes an activity producing RNase E-like cleavages
    • Wang M., Cohen S.N. ard-1: A human gene that reverses the effects of temperature-sensitive and deletion mutations in the Escherichia coli rne gene and encodes an activity producing RNase E-like cleavages. Proc. Natl. Acad. Sci. USA. 91:1994;10591-10595.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10591-10595
    • Wang, M.1    Cohen, S.N.2
  • 81
    • 0029114532 scopus 로고
    • A human RNase E-like activity that cleaves RNA sequences involved in mRNA stability control
    • Wennborg A., Sohlberg B., Angerer D., Klein G., von Gabain A. A human RNase E-like activity that cleaves RNA sequences involved in mRNA stability control. Proc. Natl. Acad. Sci. USA. 92:1995;7322-7326.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7322-7326
    • Wennborg, A.1    Sohlberg, B.2    Angerer, D.3    Klein, G.4    Von Gabain, A.5
  • 82
    • 0030972187 scopus 로고    scopus 로고
    • ARD-1 cDNA from human cells encodes a site-specific single-strand endoribonuclease that functionally resembles Escherichia coli RNase E
    • Claverie-Martin F., Wang M., Cohen S.N. ARD-1 cDNA from human cells encodes a site-specific single-strand endoribonuclease that functionally resembles Escherichia coli RNase E. J. Biol. Chem. 272:1997;13823-13828.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13823-13828
    • Claverie-Martin, F.1    Wang, M.2    Cohen, S.N.3
  • 83
    • 0031952026 scopus 로고    scopus 로고
    • Poly(A)- And poly(U)-specific RNA 3′ tail shortening by E. coli ribonuclease E
    • Huang H., Liao J., Cohen S.N. Poly(A)- and poly(U)-specific RNA 3′ tail shortening by E. coli ribonuclease E. Nature. 391:1998;99-102.
    • (1998) Nature , vol.391 , pp. 99-102
    • Huang, H.1    Liao, J.2    Cohen, S.N.3
  • 84
    • 0029889965 scopus 로고    scopus 로고
    • RNase E polypeptides lacking a carboxyl-terminal half suppress a mukB mutation in Escherichia coli
    • Kido M., Yamanka, K., Mitani T., Niki H., Ogura T., Hiraga S. RNase E polypeptides lacking a carboxyl-terminal half suppress a mukB mutation in Escherichia coli. J. Bacteriol. 178:1996;3917-3925.
    • (1996) J. Bacteriol. , vol.178 , pp. 3917-3925
    • Kido, M.1    Yamanka, K.2    Mitani, T.3    Niki, H.4    Ogura, T.5    Hiraga, S.6
  • 86
    • 0029962989 scopus 로고    scopus 로고
    • The N-terminal domain of the rne gene product has RNase E activity and is non-overlapping with the arginine-rich RNA-binding site
    • McDowell K.J., Cohen S.N. The N-terminal domain of the rne gene product has RNase E activity and is non-overlapping with the arginine-rich RNA-binding site. J. Mol. Biol. 255:1996;349-355.
    • (1996) J. Mol. Biol. , vol.255 , pp. 349-355
    • McDowell, K.J.1    Cohen, S.N.2
  • 87
    • 0032531768 scopus 로고    scopus 로고
    • Ribonuclease E is a 5′-end-dependent endonuclease
    • Mackie G.A. Ribonuclease E is a 5′-end-dependent endonuclease. Nature. 395:1998;720-723.
    • (1998) Nature , vol.395 , pp. 720-723
    • Mackie, G.A.1
  • 88
    • 0002564378 scopus 로고
    • Ribonucleases H
    • (Linn, S.M., Lloyd, R.S. and Roberts, R.J., Eds.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Hostomsky, Z., Hostomska, Z. and Matthews, D.A. (1993) Ribonucleases H. In: Nucleases: 2nd edn. (Linn, S.M., Lloyd, R.S. and Roberts, R.J., Eds.), pp. 341-376. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1993) In: Nucleases: 2nd Edn. , pp. 341-376
    • Hostomsky, Z.1    Hostomska, Z.2    Matthews, D.A.3
  • 89
    • 0025147609 scopus 로고
    • Isolation and characterization of a second RNase H (RNase HII) of Escherichia coli K-12 encoded by the rnhB gene
    • Itaya M. Isolation and characterization of a second RNase H (RNase HII) of Escherichia coli K-12 encoded by the rnhB gene. Proc. Natl. Acad. Sci. USA. 87:1990;8587-8591.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8587-8591
    • Itaya, M.1
  • 91
    • 0026013117 scopus 로고
    • Bacteriophage T4 encodes an RNase H which removes RNA primers made by the T4 DNA replication system in vitro
    • Hollingsworth H.C., Nossal N.G. Bacteriophage T4 encodes an RNase H which removes RNA primers made by the T4 DNA replication system in vitro. J. Biol. Chem. 266:1991;1888-1897.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1888-1897
    • Hollingsworth, H.C.1    Nossal, N.G.2
  • 92
    • 0028104155 scopus 로고
    • The bacteriophage T4 regB ribonuclease. Stimulation of the purified enzyme by ribosomal protein S1
    • Ruckman J., Ringquist S., Brody E., Gold L. The bacteriophage T4 regB ribonuclease. Stimulation of the purified enzyme by ribosomal protein S1. J. Biol. Chem. 269:1994;26655-26662.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26655-26662
    • Ruckman, J.1    Ringquist, S.2    Brody, E.3    Gold, L.4
  • 93
    • 0027442208 scopus 로고
    • Dual role of the sequence-specific bacteriophage T4 endoribonuclease RegB
    • Sanson B., Uzan M. Dual role of the sequence-specific bacteriophage T4 endoribonuclease RegB. J. Mol. Biol. 233:1993;429-446.
    • (1993) J. Mol. Biol. , vol.233 , pp. 429-446
    • Sanson, B.1    Uzan, M.2
  • 94
    • 0030031442 scopus 로고    scopus 로고
    • In vitro selection of RNA specifically cleaved by bacteriophage T4 RegB endonuclease
    • Jayasena V.K., Brown D., Shtatland T., Gold L. In vitro selection of RNA specifically cleaved by bacteriophage T4 RegB endonuclease. Biochemistry. 35:1996;2349-2356.
    • (1996) Biochemistry , vol.35 , pp. 2349-2356
    • Jayasena, V.K.1    Brown, D.2    Shtatland, T.3    Gold, L.4
  • 95
    • 0028006021 scopus 로고
    • Cloning of a gene involved in rRNA precursor processing and 23S rRNA cleavage in Rhodobacter capsulatus
    • Kordes E., Jock S., Fritsch J., Bosch F., Klug G. Cloning of a gene involved in rRNA precursor processing and 23S rRNA cleavage in Rhodobacter capsulatus. J. Bacteriol. 176:1994;1121-1127.
    • (1994) J. Bacteriol. , vol.176 , pp. 1121-1127
    • Kordes, E.1    Jock, S.2    Fritsch, J.3    Bosch, F.4    Klug, G.5
  • 96
    • 0025169751 scopus 로고
    • The excision of intervening sequences from Salmonella 23S ribosomal RNA
    • Burgin A.B., Parodis K., Lane D.J., Pace N.R. The excision of intervening sequences from Salmonella 23S ribosomal RNA. Cell. 60:1990;405-414.
    • (1990) Cell , vol.60 , pp. 405-414
    • Burgin, A.B.1    Parodis, K.2    Lane, D.J.3    Pace, N.R.4
  • 97
    • 0032519898 scopus 로고    scopus 로고
    • RNase III deficient Salmonella typhimurium LT2 contains intervening sequences (IVSs) in its 23S rRNA
    • Mattatal N.R., Sanderson K.E. RNase III deficient Salmonella typhimurium LT2 contains intervening sequences (IVSs) in its 23S rRNA. FEMS Microbiol. Lett. 159:1998;179-185.
    • (1998) FEMS Microbiol. Lett. , vol.159 , pp. 179-185
    • Mattatal, N.R.1    Sanderson, K.E.2
  • 98
    • 0028067224 scopus 로고
    • Degradation of rRNA in Salmonella strains: A novel mechanism to regulate the concentrations of rRNA and ribosomes
    • Hsu D., Shih L.-M., Zee Y.C. Degradation of rRNA in Salmonella strains: a novel mechanism to regulate the concentrations of rRNA and ribosomes. J. Bacteriol. 176:1994;4761-4765.
    • (1994) J. Bacteriol. , vol.176 , pp. 4761-4765
    • Hsu, D.1    Shih, L.-M.2    Zee, Y.C.3
  • 99
    • 0032562647 scopus 로고    scopus 로고
    • The role of the 3′ external transcribed spacer in yeast pre-rRNA processing
    • Allmang C., Tollervey D. The role of the 3′ external transcribed spacer in yeast pre-rRNA processing. J. Mol. Biol. 278:1998;67-78.
    • (1998) J. Mol. Biol. , vol.278 , pp. 67-78
    • Allmang, C.1    Tollervey, D.2
  • 100
    • 0030855788 scopus 로고    scopus 로고
    • The ribosomal-RNA-processing pathway in Schizosaccharomyces pombe
    • Good L., Intine R.V.A., Nazar R.N. The ribosomal-RNA-processing pathway in Schizosaccharomyces pombe. Eur. J. Biochem. 247:1997;314-321.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 314-321
    • Good, L.1    Intine, R.V.A.2    Nazar, R.N.3
  • 101
    • 0031558810 scopus 로고    scopus 로고
    • Interdependence in the processing of ribosomal RNAs in Schizosaccharomyces pombe
    • Good L., Intine R.V.A., Nazar R.N. Interdependence in the processing of ribosomal RNAs in Schizosaccharomyces pombe. J. Mol. Biol. 273:1997;782-788.
    • (1997) J. Mol. Biol. , vol.273 , pp. 782-788
    • Good, L.1    Intine, R.V.A.2    Nazar, R.N.3
  • 102
    • 0003386153 scopus 로고
    • T4 transfer RNAs: Paradigmatic system for the study of RNA processing
    • (Matthews, C.K., Kutter, E.M., Mosig, G. and Berget, P.B., Eds.), ASM Press, Washington, DC
    • Schmidt, F.J. and Apirion, D.A. (1983) T4 transfer RNAs: paradigmatic system for the study of RNA processing. In: Bacteriophage T4 (Matthews, C.K., Kutter, E.M., Mosig, G. and Berget, P.B., Eds.), pp. 208-217. ASM Press, Washington, DC.
    • (1983) In: Bacteriophage T4 , pp. 208-217
    • Schmidt, F.J.1    Apirion, D.A.2
  • 103
    • 0020568530 scopus 로고
    • Interplay among processing and degradative enzymes and a precursor ribonucleic acid in the selective maturation and maintenance of ribonucleic acid molecules
    • Gurevitz M., Apirion D. Interplay among processing and degradative enzymes and a precursor ribonucleic acid in the selective maturation and maintenance of ribonucleic acid molecules. Biochemistry. 22:1983;4000-4005.
    • (1983) Biochemistry , vol.22 , pp. 4000-4005
    • Gurevitz, M.1    Apirion, D.2
  • 104
    • 0032584720 scopus 로고    scopus 로고
    • Bacillus subtilis RNase III cleaves both 5′- And 3′-sites of the small cytoplasmic RNA precursor
    • Oguro A., Kakeshita H., Makamura K., Yamane K., Wang W., Bechhofer D.H. Bacillus subtilis RNase III cleaves both 5′- and 3′-sites of the small cytoplasmic RNA precursor. J. Biol. Chem. 273:1998;19542-19547.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19542-19547
    • Oguro, A.1    Kakeshita, H.2    Makamura, K.3    Yamane, K.4    Wang, W.5    Bechhofer, D.H.6
  • 105
    • 0005820503 scopus 로고    scopus 로고
    • Depletion of yeast RNase III blocks correct U2 3′ end formation and results in polyadenylated but functional U2 snRNA
    • Abou Elela S., Ares M. Depletion of yeast RNase III blocks correct U2 3′ end formation and results in polyadenylated but functional U2 snRNA. EMBO J. 17:1998;3738-3746.
    • (1998) EMBO J. , vol.17 , pp. 3738-3746
    • Abou Elela, S.1    Ares, M.2
  • 106
    • 0030859441 scopus 로고    scopus 로고
    • Alternative 3′ end processing of U5 snRNA by RNase III
    • Chanfreau G., Abou Elela S., Ares M. Jr., Guthrie C. Alternative 3′ end processing of U5 snRNA by RNase III. Genes Dev. 11:1997;2741-2751.
    • (1997) Genes Dev. , vol.11 , pp. 2741-2751
    • Chanfreau, G.1    Abou Elela, S.2    Ares M., Jr.3    Guthrie, C.4
  • 107
    • 0032126735 scopus 로고    scopus 로고
    • Processing of a dicistronic small nucleolar RNA precursor by the RNA endonuclease Rnt1
    • Chanfreau G., Rotondo G., Legrain P., Jacquier A. Processing of a dicistronic small nucleolar RNA precursor by the RNA endonuclease Rnt1. EMBO J. 17:1998;3726-3737.
    • (1998) EMBO J. , vol.17 , pp. 3726-3737
    • Chanfreau, G.1    Rotondo, G.2    Legrain, P.3    Jacquier, A.4
  • 108
    • 0032509095 scopus 로고    scopus 로고
    • Yeast RNase III as a key processing enzyme in small nucleolar RNAs metabolism
    • Chanfreau G., Legrain P., Jacquier A. Yeast RNase III as a key processing enzyme in small nucleolar RNAs metabolism. J. Mol. Biol. 284:1998;975-988.
    • (1998) J. Mol. Biol. , vol.284 , pp. 975-988
    • Chanfreau, G.1    Legrain, P.2    Jacquier, A.3
  • 109
    • 0022423266 scopus 로고
    • Cleavage within an RNase III site can control mRNA stability and protein synthesis in vivo
    • Panayotatos N., Truong K. Cleavage within an RNase III site can control mRNA stability and protein synthesis in vivo. Nucleic Acids Res. 13:1985;2227-2240.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 2227-2240
    • Panayotatos, N.1    Truong, K.2
  • 111
    • 0031009317 scopus 로고
    • Polyadenylation of mRNA in prokaryotes
    • Sarkar N. Polyadenylation of mRNA in prokaryotes. Annu. Rev. Biochem. 66:1987;173-197.
    • (1987) Annu. Rev. Biochem. , vol.66 , pp. 173-197
    • Sarkar, N.1
  • 113
    • 0030682405 scopus 로고    scopus 로고
    • Escherichia coli RNase III (rnc) autoregulation occurs independently of rnc gene translation
    • Matsunaga J., Simons E.L., Simons R.W. Escherichia coli RNase III (rnc) autoregulation occurs independently of rnc gene translation. Mol. Microbiol. 26:1997;1125-1135.
    • (1997) Mol. Microbiol. , vol.26 , pp. 1125-1135
    • Matsunaga, J.1    Simons, E.L.2    Simons, R.W.3
  • 114
    • 0029856238 scopus 로고    scopus 로고
    • E. coli RNase III autoregulation structure and function of rncO, the posttranscriptional 'operator'
    • Matsunaga J., Simons E.L., Simons R.W. E. coli RNase III autoregulation structure and function of rncO, the posttranscriptional 'operator'. RNA. 2:1996;1228-1240.
    • (1996) RNA , vol.2 , pp. 1228-1240
    • Matsunaga, J.1    Simons, E.L.2    Simons, R.W.3
  • 115
    • 0025649204 scopus 로고
    • RNase III cleavages in non-coding leaders of Escherichia coli transcripts control mRNA stability and genetic expression
    • Regnier P., Grunberg-Manago M. RNase III cleavages in non-coding leaders of Escherichia coli transcripts control mRNA stability and genetic expression. Biochimie. 72:1990;825-834.
    • (1990) Biochimie , vol.72 , pp. 825-834
    • Regnier, P.1    Grunberg-Manago, M.2
  • 116
    • 0020322144 scopus 로고
    • Retroregulation: Control of gene expression from sites distal to the gene
    • Gottesman M., Openheim A., Court D. Retroregulation: Control of gene expression from sites distal to the gene. Cell. 29:1982;727-728.
    • (1982) Cell , vol.29 , pp. 727-728
    • Gottesman, M.1    Openheim, A.2    Court, D.3
  • 117
    • 85041131924 scopus 로고
    • Antisense RNA control in bacteria, phages and plasmids
    • Wagner E.G.H., Simons R.W. Antisense RNA control in bacteria, phages and plasmids. Annu. Rev. Biochem. 48:1994;713-742.
    • (1994) Annu. Rev. Biochem. , vol.48 , pp. 713-742
    • Wagner, E.G.H.1    Simons, R.W.2
  • 118
    • 0029945236 scopus 로고    scopus 로고
    • Translation of the adhE transcript to produce ethanol dehydrogenase requires RNase III cleavage in Escherichia coli
    • Aristarkhov A., Mikuslkis A., Belasco J.G., Linn E.C.C. Translation of the adhE transcript to produce ethanol dehydrogenase requires RNase III cleavage in Escherichia coli. J. Bacteriol. 178:1996;4327-4332.
    • (1996) J. Bacteriol. , vol.178 , pp. 4327-4332
    • Aristarkhov, A.1    Mikuslkis, A.2    Belasco, J.G.3    Linn, E.C.C.4
  • 121
    • 0020464846 scopus 로고
    • Escherichia coli ribonuclease III cleavage sites
    • Robertson H.D. Escherichia coli ribonuclease III cleavage sites. Cell. 30:1982;669-672.
    • (1982) Cell , vol.30 , pp. 669-672
    • Robertson, H.D.1
  • 122
    • 0027249769 scopus 로고
    • Mutational analysis of a ribonuclease III processing signal
    • Chelladurai B.S., Li H.-L., Zhang K., Nicholson A.W. Mutational analysis of a ribonuclease III processing signal. Biochemistry. 32:1993;7549-7558.
    • (1993) Biochemistry , vol.32 , pp. 7549-7558
    • Chelladurai, B.S.1    Li, H.-L.2    Zhang, K.3    Nicholson, A.W.4
  • 123
    • 0025033465 scopus 로고
    • The cleavage specificity of RNase III
    • Krinke L., Wulff D.L. The cleavage specificity of RNase III. Nucleic Acids Res. 18:1990;4809-4815.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 4809-4815
    • Krinke, L.1    Wulff, D.L.2
  • 124
    • 0031470503 scopus 로고    scopus 로고
    • Regulation of ribonuclease III processing by double-stranded helical sequence antideterminants
    • Zhang K., Nicholson A.W. Regulation of ribonuclease III processing by double-stranded helical sequence antideterminants. Proc. Natl. Acad. Sci. USA. 94:1997;13437-13441.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13437-13441
    • Zhang, K.1    Nicholson, A.W.2
  • 125
    • 0028919939 scopus 로고
    • Bulged-out nucleotides protect an antisense RNA from RNase III cleavage
    • Hjält T.A.H., Wagner E.G.H. Bulged-out nucleotides protect an antisense RNA from RNase III cleavage. Nucleic Acids Res. 23:1995;571-579.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 571-579
    • Hjält, T.A.H.1    Wagner, E.G.H.2
  • 126
    • 0030719864 scopus 로고    scopus 로고
    • Rescue of the RNA phage genome from RNase III cleavage
    • Klovins J., van Duin J., Olsthoorn R.C.L. Rescue of the RNA phage genome from RNase III cleavage. Nucleic Acids Res. 25:1997;4201-4208.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4201-4208
    • Klovins, J.1    Van Duin, J.2    Olsthoorn, R.C.L.3
  • 128
    • 0002404647 scopus 로고
    • The role of the 3′ end in mRNA stability and decay
    • (Belasco J.G. and Brawerman, G., Eds.), Academic Press, New York
    • Higgins, C.F., Causton, H.C., Dance, G.S.C. and Mudd, E.A. (1993) The role of the 3′ end in mRNA stability and decay. In: Control of Messenger RNA Stability (Belasco J.G. and Brawerman, G., Eds.), pp. 13-30. Academic Press, New York.
    • (1993) In: Control of Messenger RNA Stability , pp. 13-30
    • Higgins, C.F.1    Causton, H.C.2    Dance, G.S.C.3    Mudd, E.A.4
  • 129
    • 0026492668 scopus 로고
    • Control of RNase E-mediated RNA degradation by 5′-terminal base pairing in E. coli
    • Bouvet P., Belasco J.G. Control of RNase E-mediated RNA degradation by 5′-terminal base pairing in E. coli. Nature. 360:1992;488-491.
    • (1992) Nature , vol.360 , pp. 488-491
    • Bouvet, P.1    Belasco, J.G.2
  • 130
    • 0028282567 scopus 로고
    • The ompA untranslated region impedes a major pathway for mRNA degradation in Escherichia coli
    • Hansen M.J., Chen L-H., Fejzo M.L.S., Belasco J.G. The ompA untranslated region impedes a major pathway for mRNA degradation in Escherichia coli. Mol. Microbiol. 12:1994;707-716.
    • (1994) Mol. Microbiol. , vol.12 , pp. 707-716
    • Hansen, M.J.1    Chen, L.-H.2    Fejzo, M.L.S.3    Belasco, J.G.4
  • 131
    • 0029976320 scopus 로고    scopus 로고
    • Defining the enzyme binding domain of a ribonuclease III processing signal. Ethylation interference and hydroxyl radical footprinting using catalytically inactive RNase III mutants
    • Li H., Nicholson A.W. Defining the enzyme binding domain of a ribonuclease III processing signal. Ethylation interference and hydroxyl radical footprinting using catalytically inactive RNase III mutants. EMBO J. 15:1996;1421-1433.
    • (1996) EMBO J. , vol.15 , pp. 1421-1433
    • Li, H.1    Nicholson, A.W.2
  • 133
  • 134
    • 0029041105 scopus 로고
    • NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5
    • Bycroft M., Grunert S., Murzin A.G., Proctor M., St. Johnston D. NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5. EMBO J. 14:1995;3563-3571.
    • (1995) EMBO J. , vol.14 , pp. 3563-3571
    • Bycroft, M.1    Grunert, S.2    Murzin, A.G.3    Proctor, M.4    St. Johnston, D.5
  • 135
    • 0032530310 scopus 로고    scopus 로고
    • Structure of the double-stranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation
    • Nanduri S., Carpick B.W., Yang Y., Williams B.R.G., Qin J. Structure of the double-stranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation. EMBO J. 17:1998;5458-5465.
    • (1998) EMBO J. , vol.17 , pp. 5458-5465
    • Nanduri, S.1    Carpick, B.W.2    Yang, Y.3    Williams, B.R.G.4    Qin, J.5
  • 136
    • 0032535613 scopus 로고    scopus 로고
    • Molecular basis of double-stranded RNA-protein interactions: Structure of a dsRNA-binding domain complexed with dsRNA
    • Ryter J.M., Schultz S.C. Molecular basis of double-stranded RNA-protein interactions: structure of a dsRNA-binding domain complexed with dsRNA. EMBO J. 17:1998;7505-7513.
    • (1998) EMBO J. , vol.17 , pp. 7505-7513
    • Ryter, J.M.1    Schultz, S.C.2
  • 137
    • 0027191132 scopus 로고
    • Ribonuclease III cleavage of a bacteriophage T7 processing signal. Divalent cation specificity, and specific anion effects
    • Li H., Chelladurai B.S., Zhang K., Nicholson A.W. Ribonuclease III cleavage of a bacteriophage T7 processing signal. Divalent cation specificity, and specific anion effects. Nucleic Acids Res. 21:1993;1919-1925.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 1919-1925
    • Li, H.1    Chelladurai, B.S.2    Zhang, K.3    Nicholson, A.W.4
  • 138
    • 0031980568 scopus 로고    scopus 로고
    • Genetic uncoupling of the dsRNA-binding and RNA cleavage activities of the Escherichia coli endoribonucleases RNase III - The effect of dsRNA binding on gene expression
    • Dasgupta S., Fernandez L., Kameyama L., Inada T., Nakamira Y., Pappas A., Court D.L. Genetic uncoupling of the dsRNA-binding and RNA cleavage activities of the Escherichia coli endoribonucleases RNase III - the effect of dsRNA binding on gene expression. Mol. Microbiol. 28:1998;629-640.
    • (1998) Mol. Microbiol. , vol.28 , pp. 629-640
    • Dasgupta, S.1    Fernandez, L.2    Kameyama, L.3    Inada, T.4    Nakamira, Y.5    Pappas, A.6    Court, D.L.7
  • 139
    • 0029858708 scopus 로고    scopus 로고
    • The production and characterization of artificial heterodimers of the restriction endonuclease EcoRV
    • Wende W., Stahl F., Pingoud A. The production and characterization of artificial heterodimers of the restriction endonuclease EcoRV. Biol. Chem. 377:1996;625-632.
    • (1996) Biol. Chem. , vol.377 , pp. 625-632
    • Wende, W.1    Stahl, F.2    Pingoud, A.3
  • 140
    • 0021099474 scopus 로고
    • RNase III is positively regulated by T7 protein kinase
    • Mayer J.E., Schweiger M. RNase III is positively regulated by T7 protein kinase. J. Biol. Chem. 258:1983;5340-5343.
    • (1983) J. Biol. Chem. , vol.258 , pp. 5340-5343
    • Mayer, J.E.1    Schweiger, M.2
  • 141
    • 0028175657 scopus 로고
    • Phosphorylation of elongation factor G and ribosomal protein S6 in bacteriophage T7-infected E. coli
    • Robertson E.S., Aggison L.A., Nicholson A.W. Phosphorylation of elongation factor G and ribosomal protein S6 in bacteriophage T7-infected E. coli. Mol. Microbiol. 11:1994;1045-1057.
    • (1994) Mol. Microbiol. , vol.11 , pp. 1045-1057
    • Robertson, E.S.1    Aggison, L.A.2    Nicholson, A.W.3
  • 142
    • 0021821599 scopus 로고
    • Suppressors of temperature-sensitive mutations in a ribosomal protein gene, rpsL (S12), of Escherichia coli K12
    • Nashimoto H., Miura A., Saito H., Uchida H. Suppressors of temperature-sensitive mutations in a ribosomal protein gene, rpsL (S12), of Escherichia coli K12. Mol. Gen. Genet. 199:1985;381-387.
    • (1985) Mol. Gen. Genet. , vol.199 , pp. 381-387
    • Nashimoto, H.1    Miura, A.2    Saito, H.3    Uchida, H.4
  • 143
    • 0014408286 scopus 로고
    • Purification and properties of ribonuclease III from Escherichia coli
    • Robertson H.D., Webster R.E., Zinder N.D. Purification and properties of ribonuclease III from Escherichia coli. J. Biol. Chem. 243:1968;82-91.
    • (1968) J. Biol. Chem. , vol.243 , pp. 82-91
    • Robertson, H.D.1    Webster, R.E.2    Zinder, N.D.3
  • 145
    • 0030908706 scopus 로고    scopus 로고
    • Ribosome targeting of PKR is mediated by two double-stranded RNA-binding domains and facilitates the in vivo phosphorylation of eukaryotic initiation factor-2
    • Zhu S., Romano P.R., Wek R.S. Ribosome targeting of PKR is mediated by two double-stranded RNA-binding domains and facilitates the in vivo phosphorylation of eukaryotic initiation factor-2. J. Biol. Chem. 272:1997;14434-14441.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14434-14441
    • Zhu, S.1    Romano, P.R.2    Wek, R.S.3
  • 147
    • 0025268124 scopus 로고
    • In vitro inhibition of HeLa cell nuclear ribonucleases by ADP-ribosylation
    • Quesada P., Merola M., Farina B., Leone E. In vitro inhibition of HeLa cell nuclear ribonucleases by ADP-ribosylation. Mol. Cell. Biochem. 94:1990;53-60.
    • (1990) Mol. Cell. Biochem. , vol.94 , pp. 53-60
    • Quesada, P.1    Merola, M.2    Farina, B.3    Leone, E.4
  • 148
    • 0032489015 scopus 로고    scopus 로고
    • The cell as a collection of protein machines: Preparing the next generation of molecular biologists
    • Alberts B. The cell as a collection of protein machines: preparing the next generation of molecular biologists. Cell. 92:1998;291-294.
    • (1998) Cell , vol.92 , pp. 291-294
    • Alberts, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.