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Volumn 192, Issue 5, 2010, Pages 1344-1352

Escherichia coli RNase R has dual activities, helicase and RNase

Author keywords

[No Author keywords available]

Indexed keywords

COLD SHOCK PROTEIN; EXORIBONUCLEASE; HELICASE; MUTANT PROTEIN; RIBONUCLEASE; RIBONUCLEASE R; UNCLASSIFIED DRUG;

EID: 77749279767     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01368-09     Document Type: Article
Times cited : (59)

References (62)
  • 1
    • 12544252211 scopus 로고    scopus 로고
    • A single mutation in Escherichia coli ribonuclease II inactivates the enzyme without affecting RNA binding
    • Amblar, M., and C. M. Arraiano. 2005. A single mutation in Escherichia coli ribonuclease II inactivates the enzyme without affecting RNA binding. FEBS J. 272:363-374.
    • (2005) FEBS J , vol.272 , pp. 363-374
    • Amblar, M.1    Arraiano, C.M.2
  • 2
    • 50249085426 scopus 로고    scopus 로고
    • RNase activity of polynucleotide phosphorylase is critical at low temperature in Escherichia coli and is complemented by RNase II
    • Awano, N., M. Inouye, and S. Phadtare. 2008. RNase activity of polynucleotide phosphorylase is critical at low temperature in Escherichia coli and is complemented by RNase II. J. Bacteriol. 190:5924-5933.
    • (2008) J. Bacteriol , vol.190 , pp. 5924-5933
    • Awano, N.1    Inouye, M.2    Phadtare, S.3
  • 3
    • 34547756386 scopus 로고    scopus 로고
    • Complementation analysis of the cold-sensitive phenotype of the Escherichia coli csdA deletion strain
    • Awano, N., C. Xu, H. Ke, K. Inoue, M. Inouye, and S. Phadtare. 2007. Complementation analysis of the cold-sensitive phenotype of the Escherichia coli csdA deletion strain. J. Bacteriol. 189:5808- 5815.
    • (2007) J. Bacteriol , vol.189 , pp. 5808-5815
    • Awano, N.1    Xu, C.2    Ke, H.3    Inoue, K.4    Inouye, M.5    Phadtare, S.6
  • 4
    • 0030827628 scopus 로고    scopus 로고
    • CspA, the major cold shock protein of Escherichia coli, negatively regulates its own gene expression
    • Bae, W., P. G. Jones, and M. Inouye. 1997. CspA, the major cold shock protein of Escherichia coli, negatively regulates its own gene expression. J. Bacteriol. 179:7081-7088.
    • (1997) J. Bacteriol , vol.179 , pp. 7081-7088
    • Bae, W.1    Jones, P.G.2    Inouye, M.3
  • 5
    • 45149086359 scopus 로고    scopus 로고
    • New insights into the mechanism of RNA degradation by ribonuclease II: Identification of the residue responsible for setting the RNase II end product
    • Barbas, A., R. G. Matos, M. Amblar, E. Lopez-Vinas, P. Gomez-Puertas, and C. M. Arraiano. 2008. New insights into the mechanism of RNA degradation by ribonuclease II: identification of the residue responsible for setting the RNase II end product. J. Biol. Chem. 283:13070-13076.
    • (2008) J. Biol. Chem , vol.283 , pp. 13070-13076
    • Barbas, A.1    Matos, R.G.2    Amblar, M.3    Lopez-Vinas, E.4    Gomez-Puertas, P.5    Arraiano, C.M.6
  • 6
    • 2942754127 scopus 로고    scopus 로고
    • Studies on three E. coli DEAD-box helicases point to an unwinding mechanism different from that of model DNA helicases
    • Bizebard, T., I. Ferlenghi, I. Iost, and M. Dreyfus. 2004. Studies on three E. coli DEAD-box helicases point to an unwinding mechanism different from that of model DNA helicases. Biochemistry 43:7857-7866.
    • (2004) Biochemistry , vol.43 , pp. 7857-7866
    • Bizebard, T.1    Ferlenghi, I.2    Iost, I.3    Dreyfus, M.4
  • 7
    • 0344394977 scopus 로고    scopus 로고
    • Cold shock induction of RNase R and its role in the maturation of the quality control mediator SsrA/tmRNA
    • Cairrao, F., A. Cruz, H. Mori, and C. M. Arraiano. 2003. Cold shock induction of RNase R and its role in the maturation of the quality control mediator SsrA/tmRNA. Mol. Microbiol. 50:1349-1360.
    • (2003) Mol. Microbiol , vol.50 , pp. 1349-1360
    • Cairrao, F.1    Cruz, A.2    Mori, H.3    Arraiano, C.M.4
  • 8
    • 2542557396 scopus 로고    scopus 로고
    • CsdA, a cold-shock RNA helicase from Escherichia coli, is involved in the biogenesis of 50S ribosomal subunit
    • Charollais, J., M. Dreyfus, and I. Iost. 2004. CsdA, a cold-shock RNA helicase from Escherichia coli, is involved in the biogenesis of 50S ribosomal subunit. Nucleic Acids Res. 32:2751-2759.
    • (2004) Nucleic Acids Res , vol.32 , pp. 2751-2759
    • Charollais, J.1    Dreyfus, M.2    Iost, I.3
  • 10
    • 0037077311 scopus 로고    scopus 로고
    • Purification and characterization of the Escherichia coli exoribonuclease RNase R. Comparison with RNase II
    • Cheng, Z. F., and M. P. Deutscher. 2002. Purification and characterization of the Escherichia coli exoribonuclease RNase R. Comparison with RNase II. J. Biol. Chem. 277:21624-21629.
    • (2002) J. Biol. Chem , vol.277 , pp. 21624-21629
    • Cheng, Z.F.1    Deutscher, M.P.2
  • 11
    • 0038652098 scopus 로고    scopus 로고
    • Quality control of ribosomal RNA mediated by polynucleotide phosphorylase and RNase R
    • Cheng, Z. F., and M. P. Deutscher. 2003. Quality control of ribosomal RNA mediated by polynucleotide phosphorylase and RNase R. Proc. Natl. Acad. Sci. U. S. A. 100:6388-6393.
    • (2003) Proc. Natl. Acad. Sci. U. S. A , vol.100 , pp. 6388-6393
    • Cheng, Z.F.1    Deutscher, M.P.2
  • 12
    • 0028906075 scopus 로고
    • Suppression of a cold-sensitive mutation in 16S rRNA by overexpression of a novel ribosome-binding factor, RbfA
    • Dammel, C. S., and H. F. Noller. 1995. Suppression of a cold-sensitive mutation in 16S rRNA by overexpression of a novel ribosome-binding factor, RbfA. Genes Dev. 9:626-637.
    • (1995) Genes Dev , vol.9 , pp. 626-637
    • Dammel, C.S.1    Noller, H.F.2
  • 13
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and B. L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. U. S. A. 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. U. S. A , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 14
    • 0028036767 scopus 로고
    • The nucleoid-associated DNA-binding protein H-NS is required for the efficient adaptation of Escherichia coli K-12 to a cold environment
    • Dersch, P., S. Kneip, and E. Bremer. 1994. The nucleoid-associated DNA-binding protein H-NS is required for the efficient adaptation of Escherichia coli K-12 to a cold environment. Mol. Gen. Genet. 245:255-259.
    • (1994) Mol. Gen. Genet , vol.245 , pp. 255-259
    • Dersch, P.1    Kneip, S.2    Bremer, E.3
  • 15
    • 0003395950 scopus 로고
    • Polynucleotide phosphorylase and ribonuclease II are required for cell viability and mRNA turnover in Escherichia coli K-12
    • Donovan, W. P., and S. R. Kushner. 1986. Polynucleotide phosphorylase and ribonuclease II are required for cell viability and mRNA turnover in Escherichia coli K-12. Proc. Natl. Acad. Sci. U. S. A. 83:120-124.
    • (1986) Proc. Natl. Acad. Sci. U. S. A , vol.83 , pp. 120-124
    • Donovan, W.P.1    Kushner, S.R.2
  • 16
    • 33846068920 scopus 로고    scopus 로고
    • A single subunit, Dis3, is essentially responsible for yeast exosome core activity
    • Dziembowski, A., E. Lorentzen, E. Conti, and B. Seraphin. 2007. A single subunit, Dis3, is essentially responsible for yeast exosome core activity. Nat. Struct. Mol. Biol. 14:15-22.
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 15-22
    • Dziembowski, A.1    Lorentzen, E.2    Conti, E.3    Seraphin, B.4
  • 17
    • 33748414894 scopus 로고    scopus 로고
    • Unravelling the dynamics of RNA degradation by ribonuclease II and its RNA-bound complex
    • Frazao, C., C. E. McVey, M. Amblar, A. Barbas, C. Vonrhein, C. M. Arraiano, and M. A. Carrondo. 2006. Unravelling the dynamics of RNA degradation by ribonuclease II and its RNA-bound complex. Nature 443:110-114.
    • (2006) Nature , vol.443 , pp. 110-114
    • Frazao, C.1    McVey, C.E.2    Amblar, M.3    Barbas, A.4    Vonrhein, C.5    Arraiano, C.M.6    Carrondo, M.A.7
  • 20
    • 0025365804 scopus 로고
    • Initiation of mRNA translation in prokaryotes
    • Gualerzi, C. O., and C. L. Pon. 1990. Initiation of mRNA translation in prokaryotes. Biochemistry 29:5881-5889.
    • (1990) Biochemistry , vol.29 , pp. 5881-5889
    • Gualerzi, C.O.1    Pon, C.L.2
  • 21
    • 33749125440 scopus 로고    scopus 로고
    • DEAD-box RNA helicases in Escherichia coli
    • Iost, I., and M. Dreyfus. 2006. DEAD-box RNA helicases in Escherichia coli. Nucleic Acids Res. 34:4189-4197.
    • (2006) Nucleic Acids Res , vol.34 , pp. 4189-4197
    • Iost, I.1    Dreyfus, M.2
  • 22
    • 38649135052 scopus 로고    scopus 로고
    • The E. coli RhlE RNA helicase regulates the function of related RNA helicases during ribosome assembly
    • Jain, C. 2008. The E. coli RhlE RNA helicase regulates the function of related RNA helicases during ribosome assembly. RNA 14:381-389.
    • (2008) RNA , vol.14 , pp. 381-389
    • Jain, C.1
  • 23
    • 0026641172 scopus 로고
    • DNA gyrase, CS7.4, and the cold shock response in Escherichia coli
    • Jones, P. G., R. Krah, S. R. Tafuri, and A. P. Wolffe. 1992. DNA gyrase, CS7.4, and the cold shock response in Escherichia coli. J. Bacteriol. 174: 5798-5802.
    • (1992) J. Bacteriol , vol.174 , pp. 5798-5802
    • Jones, P.G.1    Krah, R.2    Tafuri, S.R.3    Wolffe, A.P.4
  • 24
    • 0030043216 scopus 로고    scopus 로고
    • Cold shock induces a major ribosomal-associated protein that unwinds double-stranded RNA in Escherichia coli
    • Jones, P. G., M. Mitta, Y. Kim, W. Jiang, and M. Inouye. 1996. Cold shock induces a major ribosomal-associated protein that unwinds double-stranded RNA in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 93:76-80.
    • (1996) Proc. Natl. Acad. Sci. U. S. A , vol.93 , pp. 76-80
    • Jones, P.G.1    Mitta, M.2    Kim, Y.3    Jiang, W.4    Inouye, M.5
  • 25
    • 0023186464 scopus 로고
    • Induction of proteins in response to low temperature in Escherichia coli
    • Jones, P. G., R. A. VanBogelen, and F. C. Neidhardt. 1987. Induction of proteins in response to low temperature in Escherichia coli. J. Bacteriol. 169:2092-2095.
    • (1987) J. Bacteriol , vol.169 , pp. 2092-2095
    • Jones, P.G.1    VanBogelen, R.A.2    Neidhardt, F.C.3
  • 26
    • 0028339430 scopus 로고
    • Family of the major cold-shock protein, CspA (CS7.4), of Escherichia coli, whose members show a high sequence similarity with the eukaryotic Y-box binding proteins
    • Lee, S. J., A. Xie, W. Jiang, J. P. Etchegaray, P. G. Jones, and M. Inouye. 1994. Family of the major cold-shock protein, CspA (CS7.4), of Escherichia coli, whose members show a high sequence similarity with the eukaryotic Y-box binding proteins. Mol. Microbiol. 11:833-839.
    • (1994) Mol. Microbiol , vol.11 , pp. 833-839
    • Lee, S.J.1    Xie, A.2    Jiang, W.3    Etchegaray, J.P.4    Jones, P.G.5    Inouye, M.6
  • 27
    • 2542468381 scopus 로고    scopus 로고
    • The functional interaction of the hepatitis C virus helicase molecules is responsible for unwinding processivity
    • Levin, M. K., Y. H. Wang, and S. S. Patel. 2004. The functional interaction of the hepatitis C virus helicase molecules is responsible for unwinding processivity. J. Biol. Chem. 279:26005-26012.
    • (2004) J. Biol. Chem , vol.279 , pp. 26005-26012
    • Levin, M.K.1    Wang, Y.H.2    Patel, S.S.3
  • 28
    • 0036500552 scopus 로고    scopus 로고
    • RNA quality control: Degradation of defective transfer RNA
    • Li, Z., S. Reimers, S. Pandit, and M. P. Deutscher. 2002. RNA quality control: degradation of defective transfer RNA. EMBO J. 21:1132-1138.
    • (2002) EMBO J , vol.21 , pp. 1132-1138
    • Li, Z.1    Reimers, S.2    Pandit, S.3    Deutscher, M.P.4
  • 30
    • 40849106786 scopus 로고    scopus 로고
    • Structure of the active subunit of the yeast exosome core, Rrp44: Diverse modes of substrate recruitment in the RNase II nuclease family
    • Lorentzen, E., J. Basquin, R. Tomecki, A. Dziembowski, and E. Conti. 2008. Structure of the active subunit of the yeast exosome core, Rrp44: diverse modes of substrate recruitment in the RNase II nuclease family. Mol. Cell 29:717-728.
    • (2008) Mol. Cell , vol.29 , pp. 717-728
    • Lorentzen, E.1    Basquin, J.2    Tomecki, R.3    Dziembowski, A.4    Conti, E.5
  • 31
    • 70350111321 scopus 로고    scopus 로고
    • RNase R mutants elucidate the catalysis of structured RNA: RNA-binding domains select the RNAs targeted for degradation
    • Matos, R. G., A. Barbas, and C. M. Arraiano. 2009. RNase R mutants elucidate the catalysis of structured RNA: RNA-binding domains select the RNAs targeted for degradation. Biochem. J. 423:291-301.
    • (2009) Biochem. J , vol.423 , pp. 291-301
    • Matos, R.G.1    Barbas, A.2    Arraiano, C.M.3
  • 32
    • 33745684855 scopus 로고    scopus 로고
    • McVey, C. E., M. Amblar, A. Barbas, F. Cairrao, R. Coelho, C. Romao, C. M. Arraiano, M. A. Carrondo, and C. Frazao. 2006. Expression, purification, crystallization and preliminary diffraction data characterization of Escherichia coli ribonuclease II (RNase II). Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62:684-687.
    • McVey, C. E., M. Amblar, A. Barbas, F. Cairrao, R. Coelho, C. Romao, C. M. Arraiano, M. A. Carrondo, and C. Frazao. 2006. Expression, purification, crystallization and preliminary diffraction data characterization of Escherichia coli ribonuclease II (RNase II). Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62:684-687.
  • 33
    • 0027479161 scopus 로고
    • OB (oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences
    • Murzin, A. G. 1993. OB (oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences. EMBO J. 12:861-867.
    • (1993) EMBO J , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 34
    • 0029913775 scopus 로고    scopus 로고
    • A novel member of the cspA family of genes that is induced by cold shock in Escherichia coli
    • Nakashima, K., K. Kanamaru, T. Mizuno, and K. Horikoshi. 1996. A novel member of the cspA family of genes that is induced by cold shock in Escherichia coli. J. Bacteriol. 178:2994-2997.
    • (1996) J. Bacteriol , vol.178 , pp. 2994-2997
    • Nakashima, K.1    Kanamaru, K.2    Mizuno, T.3    Horikoshi, K.4
  • 35
    • 0025912715 scopus 로고
    • The assembly of prokaryotic ribosomes
    • Nierhaus, K. H. 1991. The assembly of prokaryotic ribosomes. Biochimie 73:739-755.
    • (1991) Biochimie , vol.73 , pp. 739-755
    • Nierhaus, K.H.1
  • 36
    • 1442277681 scopus 로고    scopus 로고
    • The mechanism of nucleic acid melting by a CspA family protein
    • Phadtare, S., M. Inouye, and K. Severinov. 2004. The mechanism of nucleic acid melting by a CspA family protein. J. Mol. Biol. 337:147-155.
    • (2004) J. Mol. Biol , vol.337 , pp. 147-155
    • Phadtare, S.1    Inouye, M.2    Severinov, K.3
  • 37
    • 0036510774 scopus 로고    scopus 로고
    • The nucleic acid melting activity of Escherichia coli CspE is critical for transcription antitermination and cold acclimation of cells
    • Phadtare, S., M. Inouye, and K. Severinov. 2002. The nucleic acid melting activity of Escherichia coli CspE is critical for transcription antitermination and cold acclimation of cells. J. Biol. Chem. 277:7239-7245.
    • (2002) J. Biol. Chem , vol.277 , pp. 7239-7245
    • Phadtare, S.1    Inouye, M.2    Severinov, K.3
  • 39
    • 27244460359 scopus 로고    scopus 로고
    • Nucleic acid melting by Escherichia coli CspE
    • Phadtare, S., and K. Severinov. 2005. Nucleic acid melting by Escherichia coli CspE. Nucleic Acids Res. 33:5583-5590.
    • (2005) Nucleic Acids Res , vol.33 , pp. 5583-5590
    • Phadtare, S.1    Severinov, K.2
  • 40
    • 2242461342 scopus 로고    scopus 로고
    • Three amino acids in Escherichia coli CspE surface-exposed aromatic patch are critical for nucleic acid melting activity leading to transcription antitermination and cold acclimation of cells
    • Phadtare, S., S. Tyagi, M. Inouye, and K. Severinov. 2002. Three amino acids in Escherichia coli CspE surface-exposed aromatic patch are critical for nucleic acid melting activity leading to transcription antitermination and cold acclimation of cells. J. Biol. Chem. 277:46706-46711.
    • (2002) J. Biol. Chem , vol.277 , pp. 46706-46711
    • Phadtare, S.1    Tyagi, S.2    Inouye, M.3    Severinov, K.4
  • 41
    • 9644284618 scopus 로고    scopus 로고
    • Prud'homme-Genereux, A., R. K. Beran, I. Iost, C. S. Ramey, G. A. Mackie, and R. W. Simons. 2004. Physical and functional interactions among RNase E, polynucleotide phosphorylase and the cold-shock protein, CsdA: evidence for a 'cold shock degradosome.' Mol. Microbiol. 54:1409-1421.
    • Prud'homme-Genereux, A., R. K. Beran, I. Iost, C. S. Ramey, G. A. Mackie, and R. W. Simons. 2004. Physical and functional interactions among RNase E, polynucleotide phosphorylase and the cold-shock protein, CsdA: evidence for a 'cold shock degradosome.' Mol. Microbiol. 54:1409-1421.
  • 42
    • 17644380001 scopus 로고    scopus 로고
    • Exoribonuclease R interacts with endoribonuclease E and an RNA helicase in the psychrotrophic bacterium Pseudomonas syringae Lz4W
    • Purusharth, R. I., F. Klein, S. Sulthana, S. Jager, M. V. Jagannadham, E. Evguenieva-Hackenberg, M. K. Ray, and G. Klug. 2005. Exoribonuclease R interacts with endoribonuclease E and an RNA helicase in the psychrotrophic bacterium Pseudomonas syringae Lz4W. J. Biol. Chem. 280: 14572-14578.
    • (2005) J. Biol. Chem , vol.280 , pp. 14572-14578
    • Purusharth, R.I.1    Klein, F.2    Sulthana, S.3    Jager, S.4    Jagannadham, M.V.5    Evguenieva-Hackenberg, E.6    Ray, M.K.7    Klug, G.8
  • 43
    • 0014483503 scopus 로고
    • Characterization of polynucleotide phosphorylase mutants of Escherichia coli
    • Reiner, A. M. 1969. Characterization of polynucleotide phosphorylase mutants of Escherichia coli. J. Bacteriol. 97:1437-1443.
    • (1969) J. Bacteriol , vol.97 , pp. 1437-1443
    • Reiner, A.M.1
  • 44
    • 0014477758 scopus 로고
    • Isolation and mapping of polynucleotide phosphorylase mutants of Escherichia coli
    • Reiner, A. M. 1969. Isolation and mapping of polynucleotide phosphorylase mutants of Escherichia coli. J. Bacteriol. 97:1431-1436.
    • (1969) J. Bacteriol , vol.97 , pp. 1431-1436
    • Reiner, A.M.1
  • 45
    • 0040142238 scopus 로고    scopus 로고
    • Biochemical and kinetic characterization of the RNA helicase activity of eukaryotic initiation factor 4A
    • Rogers, G. W., Jr., N. J. Richter, and W. C. Merrick. 1999. Biochemical and kinetic characterization of the RNA helicase activity of eukaryotic initiation factor 4A. J. Biol. Chem. 274:12236-12244.
    • (1999) J. Biol. Chem , vol.274 , pp. 12236-12244
    • Rogers Jr., G.W.1    Richter, N.J.2    Merrick, W.C.3
  • 46
    • 0014004365 scopus 로고
    • Polysomes extracted from Escherichia coli by freeze-thaw-lysozyme lysis
    • Ron, E. Z., R. E. Kohler, and B. D. Davis. 1966. Polysomes extracted from Escherichia coli by freeze-thaw-lysozyme lysis. Science 153:1119-1120.
    • (1966) Science , vol.153 , pp. 1119-1120
    • Ron, E.Z.1    Kohler, R.E.2    Davis, B.D.3
  • 47
    • 34447300418 scopus 로고    scopus 로고
    • The exosome subunit Rrp44 plays a direct role in RNA substrate recognition
    • Schneider, C., J. T. Anderson, and D. Tollervey. 2007. The exosome subunit Rrp44 plays a direct role in RNA substrate recognition. Mol. Cell 27:324-331.
    • (2007) Mol. Cell , vol.27 , pp. 324-331
    • Schneider, C.1    Anderson, J.T.2    Tollervey, D.3
  • 48
    • 0025153770 scopus 로고
    • Mechanism and regulation of bacterial ribosomal RNA processing
    • Srivastava, A. K., and D. Schlessinger. 1990. Mechanism and regulation of bacterial ribosomal RNA processing. Annu. Rev. Microbiol. 44:105-129.
    • (1990) Annu. Rev. Microbiol , vol.44 , pp. 105-129
    • Srivastava, A.K.1    Schlessinger, D.2
  • 49
    • 0025733344 scopus 로고
    • deaD, a new Escherichia coli gene encoding a presumed ATP-dependent RNA helicase, can suppress a mutation in rpsB, the gene encoding ribosomal protein S2
    • Toone, W. M., K. E. Rudd, and J. D. Friesen. 1991. deaD, a new Escherichia coli gene encoding a presumed ATP-dependent RNA helicase, can suppress a mutation in rpsB, the gene encoding ribosomal protein S2. J. Bacteriol. 173:3291-3302.
    • (1991) J. Bacteriol , vol.173 , pp. 3291-3302
    • Toone, W.M.1    Rudd, K.E.2    Friesen, J.D.3
  • 50
    • 34147169852 scopus 로고    scopus 로고
    • Mutational analysis of the Escherichia coli DEAD box protein CsdA
    • Turner, A. M., C. F. Love, R. W. Alexander, and P. G. Jones. 2007. Mutational analysis of the Escherichia coli DEAD box protein CsdA. J. Bacteriol. 189:2769-2776.
    • (2007) J. Bacteriol , vol.189 , pp. 2769-2776
    • Turner, A.M.1    Love, C.F.2    Alexander, R.W.3    Jones, P.G.4
  • 51
    • 62049085767 scopus 로고    scopus 로고
    • Insights into how RNase R degrades structured RNA: Analysis of the nuclease domain
    • Vincent, H. A., and M. P. Deutscher. 2009. Insights into how RNase R degrades structured RNA: analysis of the nuclease domain. J. Mol. Biol. 387:570-583.
    • (2009) J. Mol. Biol , vol.387 , pp. 570-583
    • Vincent, H.A.1    Deutscher, M.P.2
  • 52
    • 58649092877 scopus 로고    scopus 로고
    • The roles of individual domains of RNase R in substrate binding and exoribonuclease activity: The nuclease domain is sufficient for digestion of structured RNA
    • Vincent, H. A., and M. P. Deutscher. 2009. The roles of individual domains of RNase R in substrate binding and exoribonuclease activity: the nuclease domain is sufficient for digestion of structured RNA. J. Biol. Chem. 284: 486-494.
    • (2009) J. Biol. Chem , vol.284 , pp. 486-494
    • Vincent, H.A.1    Deutscher, M.P.2
  • 53
    • 33749578566 scopus 로고    scopus 로고
    • Substrate recognition and catalysis by the exoribonuclease RNase R
    • Vincent, H. A., and M. P. Deutscher. 2006. Substrate recognition and catalysis by the exoribonuclease RNase R. J. Biol. Chem. 281:29769-29775.
    • (2006) J. Biol. Chem , vol.281 , pp. 29769-29775
    • Vincent, H.A.1    Deutscher, M.P.2
  • 54
    • 0021320685 scopus 로고
    • Mutagenesis and inducible responses to deoxyribonucleic acid damage in Escherichia coli
    • Walker, G. C. 1984. Mutagenesis and inducible responses to deoxyribonucleic acid damage in Escherichia coli. Microbiol. Rev. 48:60-93.
    • (1984) Microbiol. Rev , vol.48 , pp. 60-93
    • Walker, G.C.1
  • 55
    • 0033027458 scopus 로고    scopus 로고
    • CspI, the ninth member of the CspA family of Escherichia coli, is induced upon cold shock
    • Wang, N., K. Yamanaka, and M. Inouye. 1999. CspI, the ninth member of the CspA family of Escherichia coli, is induced upon cold shock. J. Bacteriol. 181:1603-1609.
    • (1999) J. Bacteriol , vol.181 , pp. 1603-1609
    • Wang, N.1    Yamanaka, K.2    Inouye, M.3
  • 56
    • 0035205430 scopus 로고    scopus 로고
    • Complementation of cold shock proteins by translation initiation factor IF1 in vivo
    • Weber, M. H., C. L. Beckering, and M. A. Marahiel. 2001. Complementation of cold shock proteins by translation initiation factor IF1 in vivo. J. Bacteriol. 183:7381-7386.
    • (2001) J. Bacteriol , vol.183 , pp. 7381-7386
    • Weber, M.H.1    Beckering, C.L.2    Marahiel, M.A.3
  • 57
    • 0037321039 scopus 로고    scopus 로고
    • After the ribosome structures: How are the subunits assembled?
    • Williamson, J. R. 2003. After the ribosome structures: how are the subunits assembled? RNA 9:165-167.
    • (2003) RNA , vol.9 , pp. 165-167
    • Williamson, J.R.1
  • 58
    • 0035048662 scopus 로고    scopus 로고
    • Acquirement of cold sensitivity by quadruple deletion of the cspA family and its suppression by PNPase S1 domain in Escherichia coli
    • Xia, B., H. Ke, and M. Inouye. 2001. Acquirement of cold sensitivity by quadruple deletion of the cspA family and its suppression by PNPase S1 domain in Escherichia coli. Mol. Microbiol. 40:179-188.
    • (2001) Mol. Microbiol , vol.40 , pp. 179-188
    • Xia, B.1    Ke, H.2    Inouye, M.3
  • 59
    • 0035046480 scopus 로고    scopus 로고
    • Selective mRNA degradation by polynucleotide phosphorylase in cold shock adaptation in Escherichia coli
    • Yamanaka, K., and M. Inouye. 2001. Selective mRNA degradation by polynucleotide phosphorylase in cold shock adaptation in Escherichia coli. J. Bacteriol. 183:2808-2816.
    • (2001) J. Bacteriol , vol.183 , pp. 2808-2816
    • Yamanaka, K.1    Inouye, M.2
  • 60
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 61
    • 0033923957 scopus 로고    scopus 로고
    • Transcriptional and post-transcriptional control of polynucleotide phosphorylase during cold acclimation in Escherichia coli
    • Zangrossi, S., F. Briani, D. Ghisotti, M. E. Regonesi, P. Tortora, and G. Deho. 2000. Transcriptional and post-transcriptional control of polynucleotide phosphorylase during cold acclimation in Escherichia coli. Mol. Microbiol. 36:1470-1480.
    • (2000) Mol. Microbiol , vol.36 , pp. 1470-1480
    • Zangrossi, S.1    Briani, F.2    Ghisotti, D.3    Regonesi, M.E.4    Tortora, P.5    Deho, G.6
  • 62
    • 33749072017 scopus 로고    scopus 로고
    • Structural basis for processivity and single-strand specificity of RNase II
    • Zuo, Y., H. A. Vincent, J. Zhang, Y. Wang, M. P. Deutscher, and A. Malhotra. 2006. Structural basis for processivity and single-strand specificity of RNase II. Mol. Cell 24:149-156.
    • (2006) Mol. Cell , vol.24 , pp. 149-156
    • Zuo, Y.1    Vincent, H.A.2    Zhang, J.3    Wang, Y.4    Deutscher, M.P.5    Malhotra, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.