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Volumn 33, Issue 12, 2011, Pages 2337-2350

Current perspectives of the Escherichia coli RNA degradosome

Author keywords

Cytoskeleton; DnaK; GroEL; RNA degradosome; RNA metabolism; RNase E

Indexed keywords

CYTOSKELETONS; DNAK; GROEL; RNA METABOLISM; RNASE E;

EID: 81155133973     PISSN: 01415492     EISSN: 15736776     Source Type: Journal    
DOI: 10.1007/s10529-011-0713-6     Document Type: Review
Times cited : (12)

References (115)
  • 3
    • 0002612868 scopus 로고
    • Experimental approaches to the study of mRNA decay
    • J. G. Belasco and G. Brawerman (Eds.), New York: Academic Press
    • Belasco JG, Brawerman G (1993) Experimental approaches to the study of mRNA decay. In: Belasco JG, Brawerman G (eds) Control of messenger RNA stability. Academic Press, New York.
    • (1993) Control of Messenger RNA Stability
    • Belasco, J.G.1    Brawerman, G.2
  • 4
    • 0037162469 scopus 로고    scopus 로고
    • Global analysis of mRNA decay and abundance in Escherichia coli at single-gene resolution using two-color fluorescent DNA microarrays
    • Bernstein JA, Khodursky AB, Lin P-H, Lin-Chao S, Cohen SN (2002) Global analysis of mRNA decay and abundance in Escherichia coli at single-gene resolution using two-color fluorescent DNA microarrays. Proc Natl Acad Sci 99: 9697-9702.
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 9697-9702
    • Bernstein, J.A.1    Khodursky, A.B.2    Lin, P.-H.3    Lin-Chao, S.4    Cohen, S.N.5
  • 5
    • 1542267833 scopus 로고    scopus 로고
    • Global analysis of Escherichia coli RNA degradosome function using DNA microarrays
    • Bernstein JA, Lin P-H, Cohen SN, Lin-Chao S (2004) Global analysis of Escherichia coli RNA degradosome function using DNA microarrays. Proc Natl Acad Sci 101: 2758-2763.
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 2758-2763
    • Bernstein, J.A.1    Lin, P.-H.2    Cohen, S.N.3    Lin-Chao, S.4
  • 6
    • 0030779484 scopus 로고    scopus 로고
    • Polyphosphate kinase is a component of the Escherichia coli RNA degradosome
    • Blum E, Py B, Carpousis AJ, Higgens CF (1997) Polyphosphate kinase is a component of the Escherichia coli RNA degradosome. Mol Microbiol 26: 387-398.
    • (1997) Mol Microbiol , vol.26 , pp. 387-398
    • Blum, E.1    Py, B.2    Carpousis, A.J.3    Higgens, C.F.4
  • 7
    • 0026492668 scopus 로고
    • Control of RNase E-mediated RNA degradation by 5′-terminal base pairing in Escherichia coli
    • Bouvet P, Belasco JG (1992) Control of RNase E-mediated RNA degradation by 5′-terminal base pairing in Escherichia coli. Nature 360: 488-491.
    • (1992) Nature , vol.360 , pp. 488-491
    • Bouvet, P.1    Belasco, J.G.2
  • 8
    • 33644752796 scopus 로고    scopus 로고
    • Identification and analysis of Escherichia coli ribonuclease E dominant-negative mutants
    • Briegel K, Baker A, Jain C (2005) Identification and analysis of Escherichia coli ribonuclease E dominant-negative mutants. Genetics 172: 7-15.
    • (2005) Genetics , vol.172 , pp. 7-15
    • Briegel, K.1    Baker, A.2    Jain, C.3
  • 9
    • 27144495430 scopus 로고    scopus 로고
    • Structure of Escherichia coli RNase E catalytic domain and implications for RNA turnover
    • Callaghan AJ, Marcaida MJ, Stead JA, McDowall KJ, Scott WG, Luisi BF (2005) Structure of Escherichia coli RNase E catalytic domain and implications for RNA turnover. Nature 437: 1187-1191.
    • (2005) Nature , vol.437 , pp. 1187-1191
    • Callaghan, A.J.1    Marcaida, M.J.2    Stead, J.A.3    McDowall, K.J.4    Scott, W.G.5    Luisi, B.F.6
  • 10
    • 33845619142 scopus 로고    scopus 로고
    • The bacterial actin-like cytoskeleton
    • Carballido-Lopez R (2006) The bacterial actin-like cytoskeleton. Microbiol Mol Biol Rev 70: 888-909.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 888-909
    • Carballido-Lopez, R.1
  • 11
    • 77953753696 scopus 로고    scopus 로고
    • Small RNA-mediated regulation at the level of transcript stability
    • Caron M-P, Lafontaine DA, Massé E (2010) Small RNA-mediated regulation at the level of transcript stability. RNA Biol 7: 1-5.
    • (2010) RNA Biol , vol.7 , pp. 1-5
    • Caron, M.-P.1    Lafontaine, D.A.2    Massé, E.3
  • 12
    • 0036549769 scopus 로고    scopus 로고
    • The Escherichia coli RNA degradosome: structure, function and relationship to other ribonucleolytic multienzyme complexes
    • Carpousis AJ (2002) The Escherichia coli RNA degradosome: structure, function and relationship to other ribonucleolytic multienzyme complexes. Biochem Soc Trans 30: 150-154.
    • (2002) Biochem Soc Trans , vol.30 , pp. 150-154
    • Carpousis, A.J.1
  • 13
    • 35548995356 scopus 로고    scopus 로고
    • The RNA degradosome of Escherichia coli: an mRNA-degrading machine assembled on RNase E
    • Carpousis AJ (2007) The RNA degradosome of Escherichia coli: an mRNA-degrading machine assembled on RNase E. Annu Rev Microbiol 61: 71-87.
    • (2007) Annu Rev Microbiol , vol.61 , pp. 71-87
    • Carpousis, A.J.1
  • 14
    • 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 AJ, van Houwe G, Ehretsmann C, Krisch HM (1994) Copurification of E. coli RNase E and PNPase: evidence for a specific association between two enzymes important in RNA processing and degradation. Cell 76: 889-900.
    • (1994) Cell , vol.76 , pp. 889-900
    • Carpousis, A.J.1    van Houwe, G.2    Ehretsmann, C.3    Krisch, H.M.4
  • 15
    • 0032916509 scopus 로고    scopus 로고
    • mRNA degradation. A tale of poly(A) and multiprotein machines
    • Carpousis AJ, Vanzo NF, Raynal LC (1999) mRNA degradation. A tale of poly(A) and multiprotein machines. Trends Genet 15: 24-28.
    • (1999) Trends Genet , vol.15 , pp. 24-28
    • Carpousis, A.J.1    Vanzo, N.F.2    Raynal, L.C.3
  • 16
    • 58249084639 scopus 로고    scopus 로고
    • Co-immunopurification of multiprotein complexes containing RNA-degrading enzymes
    • Carpousis AJ, Khemici V, Ait-Bara S, Poljak L (2008) Co-immunopurification of multiprotein complexes containing RNA-degrading enzymes. Methods Enzymol 447: 65-82.
    • (2008) Methods Enzymol , vol.447 , pp. 65-82
    • Carpousis, A.J.1    Khemici, V.2    Ait-Bara, S.3    Poljak, L.4
  • 17
    • 0026447906 scopus 로고
    • Cloning and analysis of the entire Escherichia coli ams gene, ams is identical to hmp1 and encodes a 114 kDa protein that migrates as a 180 kDa protein
    • Casaregola S, Jacq A, Laoudj D, McGurk G, Margar-Son S, Tempete M, Norris V, Holland IB (1992) Cloning and analysis of the entire Escherichia coli ams gene, ams is identical to hmp1 and encodes a 114 kDa protein that migrates as a 180 kDa protein. J Mol Biol 228: 30-40.
    • (1992) J Mol Biol , vol.228 , pp. 30-40
    • Casaregola, S.1    Jacq, A.2    Laoudj, D.3    McGurk, G.4    Margar-Son, S.5    Tempete, M.6    Norris, V.7    Holland, I.B.8
  • 19
    • 33645097025 scopus 로고    scopus 로고
    • Recognition of enolase in the Escherichia coli RNA degradosome
    • Chandran V, Luisi BF (2006) Recognition of enolase in the Escherichia coli RNA degradosome. J Mol Biol 358: 8-15.
    • (2006) J Mol Biol , vol.358 , pp. 8-15
    • Chandran, V.1    Luisi, B.F.2
  • 20
    • 0034693061 scopus 로고    scopus 로고
    • Poly(A) tail-dependent exonuclease AtRrp41p from Arabidopsis thaliana rescues 5.8S rRNA processing and mRNA decay defects of the yeast ski6 mutant and is found in an exosome-sized complex in plant and yeast cells
    • Chekanova JA, Shaw RJ, Wills MA, Belostotsky DA (2000) Poly(A) tail-dependent exonuclease AtRrp41p from Arabidopsis thaliana rescues 5. 8S rRNA processing and mRNA decay defects of the yeast ski6 mutant and is found in an exosome-sized complex in plant and yeast cells. J Biol Chem 275: 33158-33166.
    • (2000) J Biol Chem , vol.275 , pp. 33158-33166
    • Chekanova, J.A.1    Shaw, R.J.2    Wills, M.A.3    Belostotsky, D.A.4
  • 21
    • 0032617132 scopus 로고    scopus 로고
    • Degradation of mRNA in Escherichia coli: an old problem with some new twists
    • Coburn GA, Mackie GA (1999) Degradation of mRNA in Escherichia coli: an old problem with some new twists. Prog Nucleic Acids Res Mol Biol 62: 55-108.
    • (1999) Prog Nucleic Acids Res Mol Biol , vol.62 , pp. 55-108
    • Coburn, G.A.1    Mackie, G.A.2
  • 22
    • 0033214259 scopus 로고    scopus 로고
    • Reconstitution of a minimal RNA degradosome demonstrates functional coordination between a 3′-exonuclease and a DEAD-box RNA helicase
    • Coburn GA, Miao X, Briant DJ, Mackie GA (1999) Reconstitution of a minimal RNA degradosome demonstrates functional coordination between a 3′-exonuclease and a DEAD-box RNA helicase. Genes Dev 13: 2594-2603.
    • (1999) Genes Dev , vol.13 , pp. 2594-2603
    • Coburn, G.A.1    Miao, X.2    Briant, D.J.3    Mackie, G.A.4
  • 23
    • 0031000662 scopus 로고    scopus 로고
    • RNase E: still a wonderfully mysterious enzyme
    • Cohen SN, McDowall KJ (1997) RNase E: still a wonderfully mysterious enzyme. Mol Microbiol 23: 1099-1106.
    • (1997) Mol Microbiol , vol.23 , pp. 1099-1106
    • Cohen, S.N.1    McDowall, K.J.2
  • 25
    • 0037977118 scopus 로고    scopus 로고
    • RNA processing and degradation in Bacillus subtilis
    • Condon C (2003) RNA processing and degradation in Bacillus subtilis. MicrobiolMol Biol Rev 67: 157-174.
    • (2003) MicrobiolMol Biol Rev , vol.67 , pp. 157-174
    • Condon, C.1
  • 26
    • 50049097448 scopus 로고    scopus 로고
    • Intrinsic disorder in scaffold proteins: getting more from less
    • Cortese MS, Uversky VN, Dunker AK (2008) Intrinsic disorder in scaffold proteins: getting more from less. Prog Biophys Mol Biol 98: 85-106.
    • (2008) Prog Biophys Mol Biol , vol.98 , pp. 85-106
    • Cortese, M.S.1    Uversky, V.N.2    Dunker, A.K.3
  • 27
    • 0035354581 scopus 로고    scopus 로고
    • A nonconventional role of molecular chaperones: involvement in the cytoarchitecture
    • Csermely P (2001) A nonconventional role of molecular chaperones: involvement in the cytoarchitecture. News Physiol 15: 123-126.
    • (2001) News Physiol , vol.15 , pp. 123-126
    • Csermely, P.1
  • 28
    • 32644435694 scopus 로고    scopus 로고
    • Degradation of RNA in bacteria: comparison of mRNA and stable RNA
    • Deutscher MP (2006) Degradation of RNA in bacteria: comparison of mRNA and stable RNA. Nucleic Acids Res 34: 659-666.
    • (2006) Nucleic Acids Res , vol.34 , pp. 659-666
    • Deutscher, M.P.1
  • 29
    • 0035193362 scopus 로고    scopus 로고
    • Exoribonucleases and their multiple roles in RNA metabolism
    • Deutscher MP, Li Z (2001) Exoribonucleases and their multiple roles in RNA metabolism. Prog Nucleic Acids Res Mol Biol 66: 67-105.
    • (2001) Prog Nucleic Acids Res Mol Biol , vol.66 , pp. 67-105
    • Deutscher, M.P.1    Li, Z.2
  • 30
    • 78651197328 scopus 로고
    • Characterization of polyphosphate-AMP phosphotransferase in Corynebacterium serosis
    • Dirheimer G, Ebel JP (1965) Characterization of polyphosphate-AMP phosphotransferase in Corynebacterium serosis. CR Acad Sci (Paris) 260: 3787-3790.
    • (1965) CR Acad Sci (Paris) , vol.260 , pp. 3787-3790
    • Dirheimer, G.1    Ebel, J.P.2
  • 31
    • 0003395950 scopus 로고
    • Polynucleotide phosphorylase and ribonuclease II are required for cell viability and mRNA turnover in Escherichia coli K-12
    • Donovan WP, Kushner SR (1986) Polynucleotide phosphorylase and ribonuclease II are required for cell viability and mRNA turnover in Escherichia coli K-12. Proc Natl Acad Sci 83: 124.
    • (1986) Proc Natl Acad Sci , vol.83 , pp. 124
    • Donovan, W.P.1    Kushner, S.R.2
  • 32
    • 0030928059 scopus 로고    scopus 로고
    • Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells
    • Eggers DK, Welch WJ, Hansen WJ (1997) Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells. Mol Biol Cell 8: 1559-1573.
    • (1997) Mol Biol Cell , vol.8 , pp. 1559-1573
    • Eggers, D.K.1    Welch, W.J.2    Hansen, W.J.3
  • 33
    • 78650023635 scopus 로고    scopus 로고
    • Analysis of the RNA degradosome complex in Vibrio angustum S14
    • Erce MA, Low JKK, Wilkins MR (2010) Analysis of the RNA degradosome complex in Vibrio angustum S14. FEBS J 277: 5161-5173.
    • (2010) FEBS J , vol.277 , pp. 5161-5173
    • Erce, M.A.1    Low, J.K.K.2    Wilkins, M.R.3
  • 34
    • 0035898660 scopus 로고    scopus 로고
    • The exosome of Trypanosoma brucei
    • Estévez AM, Kempf T, Clayton C (2001) The exosome of Trypanosoma brucei. EMBO J 20: 3831-3839.
    • (2001) EMBO J , vol.20 , pp. 3831-3839
    • Estévez, A.M.1    Kempf, T.2    Clayton, C.3
  • 36
    • 0024554107 scopus 로고
    • The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures
    • Fayet O, Ziegelhoffer T, Georgopoulos C (1989) The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures. J Bacteriol 171: 1379-1385.
    • (1989) J Bacteriol , vol.171 , pp. 1379-1385
    • Fayet, O.1    Ziegelhoffer, T.2    Georgopoulos, C.3
  • 37
    • 0035943737 scopus 로고    scopus 로고
    • Escherichia coli poly(A)-binding proteins that interact with components of degradosomes or impede RNA decay mediated by polynucleotide phosphorylase and RNase E
    • Feng Y, Huang H, Liao J, Cohen SN (2001) Escherichia coli poly(A)-binding proteins that interact with components of degradosomes or impede RNA decay mediated by polynucleotide phosphorylase and RNase E. J Biol Chem 276: 31651-31656.
    • (2001) J Biol Chem , vol.276 , pp. 31651-31656
    • Feng, Y.1    Huang, H.2    Liao, J.3    Cohen, S.N.4
  • 38
    • 0029121223 scopus 로고
    • Identification of GroEL as a constituent of a messenger RNA-protection complex in Escherichia coli
    • Georgellis D, Sohlberg B, Hartl FU, von Gabain A (1995) Identification of GroEL as a constituent of a messenger RNA-protection complex in Escherichia coli. Mol Microbiol 16: 1259-1268.
    • (1995) Mol Microbiol , vol.16 , pp. 1259-1268
    • Georgellis, D.1    Sohlberg, B.2    Hartl, F.U.3    von Gabain, A.4
  • 39
    • 2942588534 scopus 로고    scopus 로고
    • An actin-like gene can determine the cell polarity in bacteria
    • Gitai Z, Dye N, Shapiro L (2004) An actin-like gene can determine the cell polarity in bacteria. Proc Natl Acad Sci 101: 8643-8648.
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 8643-8648
    • Gitai, Z.1    Dye, N.2    Shapiro, L.3
  • 41
    • 0033368475 scopus 로고    scopus 로고
    • Messenger RNA stability and its role in control of gene expression in bacteria and phages
    • Grunberg-Manago M (1999) Messenger RNA stability and its role in control of gene expression in bacteria and phages. Annual Rev Gen 33: 193-227.
    • (1999) Annual Rev Gen , vol.33 , pp. 193-227
    • Grunberg-Manago, M.1
  • 42
    • 0001486263 scopus 로고
    • Enzymatic synthesis of nucleic acid like polynucleotides
    • Grunberg-Manago M, Oritz PJ, Ochoa S (1955) Enzymatic synthesis of nucleic acid like polynucleotides. Science 122: 907-910.
    • (1955) Science , vol.122 , pp. 907-910
    • Grunberg-Manago, M.1    Oritz, P.J.2    Ochoa, S.3
  • 43
    • 0017108817 scopus 로고
    • Study on the structure-function relationship of polynucleotide phosphorylase: model of a proteolytic degraded polynucleotide phosphorylase
    • Guissani A, Portier C (1976) Study on the structure-function relationship of polynucleotide phosphorylase: model of a proteolytic degraded polynucleotide phosphorylase. Nucleic Acids Res 3: 3015-3024.
    • (1976) Nucleic Acids Res , vol.3 , pp. 3015-3024
    • Guissani, A.1    Portier, C.2
  • 45
    • 78651067735 scopus 로고    scopus 로고
    • Hfq binding at RhlB-recognition region of RNase E is crucial for the rapid degradation of target mRNAs mediated by sRNAs in Escherichia coli
    • Ikeda Y, Yagi M, Morita T, Alba H (2011) Hfq binding at RhlB-recognition region of RNase E is crucial for the rapid degradation of target mRNAs mediated by sRNAs in Escherichia coli. Mol Microbiol 79: 419-432.
    • (2011) Mol Microbiol , vol.79 , pp. 419-432
    • Ikeda, Y.1    Yagi, M.2    Morita, T.3    Alba, H.4
  • 46
    • 0018422771 scopus 로고
    • Isolation and characterization of a temperature-sensitive dnaK mutant of Escherichia coli
    • Itikawah H, Ryu J-I (1979) Isolation and characterization of a temperature-sensitive dnaK mutant of Escherichia coli. J Bacteriol 138: 339-344.
    • (1979) J Bacteriol , vol.138 , pp. 339-344
    • Itikawah, H.1    Ryu, J.-I.2
  • 48
    • 0029438136 scopus 로고
    • Autoregulation of RNase E synthesis in Escherichia coli
    • Jain C, Belasco JG (1995) Autoregulation of RNase E synthesis in Escherichia coli. Nucleic Acids Symp Ser 33: 85-88.
    • (1995) Nucleic Acids Symp Ser , vol.33 , pp. 85-88
    • Jain, C.1    Belasco, J.G.2
  • 49
    • 0036231777 scopus 로고    scopus 로고
    • Consequences of RNase E scarcity in Escherichia coli
    • Jain C, Deana A, Belasco JG (2002) Consequences of RNase E scarcity in Escherichia coli. Mol Microbiol 43: 1053-1064.
    • (2002) Mol Microbiol , vol.43 , pp. 1053-1064
    • Jain, C.1    Deana, A.2    Belasco, J.G.3
  • 50
    • 0036382938 scopus 로고    scopus 로고
    • Mutational analysis of polynucleotide phosphorylase from Escherichia coli
    • Jarrige AC, Brechemier-Baey D, Mathy N, Duche O, Portier C (2002) Mutational analysis of polynucleotide phosphorylase from Escherichia coli. J Mol Biol 321: 397-409.
    • (2002) J Mol Biol , vol.321 , pp. 397-409
    • Jarrige, A.C.1    Brechemier-Baey, D.2    Mathy, N.3    Duche, O.4    Portier, C.5
  • 51
    • 0033048066 scopus 로고    scopus 로고
    • Moonlighting proteins
    • Jeffery CJ (1999) Moonlighting proteins. Trends Biochem Sci 24: 8-11.
    • (1999) Trends Biochem Sci , vol.24 , pp. 8-11
    • Jeffery, C.J.1
  • 52
    • 85011939098 scopus 로고    scopus 로고
    • Unraveling new roles for minor components of the E. coli RNA degradosome
    • Kaberdin VR, Lin-Chao S (2009) Unraveling new roles for minor components of the E. coli RNA degradosome. RNA Biol 6: 402-405.
    • (2009) RNA Biol , vol.6 , pp. 402-405
    • Kaberdin, V.R.1    Lin-Chao, S.2
  • 53
    • 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 VR, Miczak A, Jakobsen JS, Lin-Chao S, McDowall KJ, von Gabain A (1998) 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 95: 11637-11642.
    • (1998) Proc Natl Acad Sci , 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
  • 54
    • 0015968053 scopus 로고
    • The involvement of ribonuclease I, ribonuclease II, and polynucleotide phosphorylase in the degradation of stable ribonucleic acid during carbon starvation in Escherichia coli
    • Kaplan R, Apirion D (1974) The involvement of ribonuclease I, ribonuclease II, and polynucleotide phosphorylase in the degradation of stable ribonucleic acid during carbon starvation in Escherichia coli. J Biol Chem 249: 149-151.
    • (1974) J Biol Chem , vol.249 , pp. 149-151
    • Kaplan, R.1    Apirion, D.2
  • 55
    • 0016861437 scopus 로고
    • Decay of ribosomal ribonucleic acid in Escherichia coli cells starved for various nutrients
    • Kaplan R, Apirion D (1975) Decay of ribosomal ribonucleic acid in Escherichia coli cells starved for various nutrients. J Biol Chem 250: 3174-3178.
    • (1975) J Biol Chem , vol.250 , pp. 3174-3178
    • Kaplan, R.1    Apirion, D.2
  • 56
    • 54249138245 scopus 로고    scopus 로고
    • The RNase E of Escherichia coli is a membrane-binding protein
    • Khemici V, Poljak L, Luisi BF, Carpousis AJ (2008) The RNase E of Escherichia coli is a membrane-binding protein. Mol Biol 70: 799-813.
    • (2008) Mol Biol , vol.70 , pp. 799-813
    • Khemici, V.1    Poljak, L.2    Luisi, B.F.3    Carpousis, A.J.4
  • 57
    • 77951539769 scopus 로고    scopus 로고
    • Rapid cleavage of RNA by RNase E in the absence of 5′ monophosphate stimulation
    • doi: 10. 1111/j. 1365-2958. 2009. 06935x
    • Kime L, Jourdan SS, Stead JA, Hidalgo-Sastre A, McDowall KJ (2009) Rapid cleavage of RNA by RNase E in the absence of 5′ monophosphate stimulation. Mol Microbiol. doi: 10. 1111/j. 1365-2958. 2009. 06935x.
    • (2009) Mol Microbiol
    • Kime, L.1    Jourdan, S.S.2    Stead, J.A.3    Hidalgo-Sastre, A.4    McDowall, K.J.5
  • 58
    • 0016754161 scopus 로고
    • Polynucleotide phosphorylase can participate in decay of mRNA in Escherichia coli in the absence of ribonuclease II
    • Kinscherf TG, Apirion D (1975) Polynucleotide phosphorylase can participate in decay of mRNA in Escherichia coli in the absence of ribonuclease II. Mol Gen Genet 139: 357-362.
    • (1975) Mol Gen Genet , vol.139 , pp. 357-362
    • Kinscherf, T.G.1    Apirion, D.2
  • 59
    • 0000190747 scopus 로고
    • Adenosine triphoshpate synthesis from polyphosphate by an enzyme from Escherichia coli
    • Kornberg SR (1957) Adenosine triphoshpate synthesis from polyphosphate by an enzyme from Escherichia coli. Biochem Biophys Acta 26: 294-300.
    • (1957) Biochem Biophys Acta , vol.26 , pp. 294-300
    • Kornberg, S.R.1
  • 61
    • 0035955548 scopus 로고    scopus 로고
    • Crystal Structure of the Escherichia coli RNA degradosome component enolase
    • Kuhnel K, Luisi BF (2001) Crystal Structure of the Escherichia coli RNA degradosome component enolase. J Mol Biol 313: 583-592.
    • (2001) J Mol Biol , vol.313 , pp. 583-592
    • Kuhnel, K.1    Luisi, B.F.2
  • 62
    • 0036719292 scopus 로고    scopus 로고
    • mRNA decay in Escherochia coli comes of age
    • Kushner SR (2002) mRNA decay in Escherochia coli comes of age. J Bacteriol 184: 4658-4665.
    • (2002) J Bacteriol , vol.184 , pp. 4658-4665
    • Kushner, S.R.1
  • 63
    • 0043224223 scopus 로고    scopus 로고
    • RraA. A protein inhibitor of RNase E activity that globally modulates RNA abundance in E. coli
    • Lee K, Zhan X, Gao J, Qiu J, Feng Y, Meganathan R, Cohen SN, Georgiou G (2003) RraA. A protein inhibitor of RNase E activity that globally modulates RNA abundance in E. coli. Cell 114: 623-634.
    • (2003) Cell , vol.114 , pp. 623-634
    • Lee, K.1    Zhan, X.2    Gao, J.3    Qiu, J.4    Feng, Y.5    Meganathan, R.6    Cohen, S.N.7    Georgiou, G.8
  • 64
    • 0029146185 scopus 로고
    • Hsc66, an Hsp70 homolog in Escherichia coli, is induced by cold shock but not by heat shock
    • Lelivelt MJ, Kawula TH (1995) Hsc66, an Hsp70 homolog in Escherichia coli, is induced by cold shock but not by heat shock. J Bacteriol 177: 4900-4907.
    • (1995) J Bacteriol , vol.177 , pp. 4900-4907
    • Lelivelt, M.J.1    Kawula, T.H.2
  • 65
    • 0030802287 scopus 로고    scopus 로고
    • Molecular chaperones and the cytoskeleton
    • Liang P, MacRae TH (1997) Molecular chaperones and the cytoskeleton. J Cell Sci 110: 1431-1440.
    • (1997) J Cell Sci , vol.110 , pp. 1431-1440
    • Liang, P.1    Macrae, T.H.2
  • 66
    • 28044439868 scopus 로고    scopus 로고
    • RhlB helicase rather than enolase is the β-subunit of the Escherichia coli polynucleotide phosphorylase (PNPase)-exoribonucleolytic complex
    • Lin P-H, Lin-Chao S (2005) RhlB helicase rather than enolase is the β-subunit of the Escherichia coli polynucleotide phosphorylase (PNPase)-exoribonucleolytic complex. Proc Natl Acad Sci 102: 16590-16595.
    • (2005) Proc Natl Acad Sci , vol.102 , pp. 16590-16595
    • Lin, P.-H.1    Lin-Chao, S.2
  • 67
    • 34447306927 scopus 로고    scopus 로고
    • The PNPase, exosome and RNA helicases as the building components of evolutionarily conserved RNA degradation machines
    • Lin-Chao S, Chiou N-T, Schuster G (2007) The PNPase, exosome and RNA helicases as the building components of evolutionarily conserved RNA degradation machines. J Biomed Sci 14: 523-532.
    • (2007) J Biomed Sci , vol.14 , pp. 523-532
    • Lin-Chao, S.1    Chiou, N.-T.2    Schuster, G.3
  • 68
    • 0035793043 scopus 로고    scopus 로고
    • RNA Degradosome exist in vivo in Escherichia coli as multicomponent complexes associated with the cytoplasmic membrane via the N-terminal region of ribonuclease E
    • Liou GG, Jane WN, Cohen SN, Lin NS, Lin-Chao S (2001) RNA Degradosome exist in vivo in Escherichia coli as multicomponent complexes associated with the cytoplasmic membrane via the N-terminal region of ribonuclease E. Proc Natl Acad Sci 98: 63-68.
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 63-68
    • Liou, G.G.1    Jane, W.N.2    Cohen, S.N.3    Lin, N.S.4    Lin-Chao, S.5
  • 69
    • 0037174922 scopus 로고    scopus 로고
    • DEAD box RhlB RNA helicase physically associates with exoribonuclease PNPase to degrade double-stranded RNA independent of the degradosome-assembling region of RNase E
    • Liou GG, Chang HY, Lin CS, Lin-Chao S (2002) DEAD box RhlB RNA helicase physically associates with exoribonuclease PNPase to degrade double-stranded RNA independent of the degradosome-assembling region of RNase E. J Biol Chem 277: 41157-41162.
    • (2002) J Biol Chem , vol.277 , pp. 41157-41162
    • Liou, G.G.1    Chang, H.Y.2    Lin, C.S.3    Lin-Chao, S.4
  • 71
    • 33947614717 scopus 로고    scopus 로고
    • The KH and S1 domains of Escherichia coli polynucleotide phosphorylase are necessary for autoregulation and growth at low temperature
    • Matus-Ortega ME, Regonesi ME, Pina-Escobedo A, Tortora P, Deho G, Garcia-Mena J (2007) The KH and S1 domains of Escherichia coli polynucleotide phosphorylase are necessary for autoregulation and growth at low temperature. Biochim Biophys Acta 1769: 194-203.
    • (2007) Biochim Biophys Acta , vol.1769 , pp. 194-203
    • Matus-Ortega, M.E.1    Regonesi, M.E.2    Pina-Escobedo, A.3    Tortora, P.4    Deho, G.5    Garcia-Mena, J.6
  • 72
    • 75049084936 scopus 로고    scopus 로고
    • Bacterial motility complexes require the actin-like protein, MreB and the Ras homologue, MglA
    • Mauriello EMF, Mouhamar F, Nan B, Ducret A, Dai D, Zusman DR, Mignot T (2010) Bacterial motility complexes require the actin-like protein, MreB and the Ras homologue, MglA. EMBO J 29: 315-326.
    • (2010) EMBO J , vol.29 , pp. 315-326
    • Mauriello, E.M.F.1    Mouhamar, F.2    Nan, B.3    Ducret, A.4    Dai, D.5    Zusman, D.R.6    Mignot, T.7
  • 73
    • 0027954650 scopus 로고
    • DnaK mutants defective in ATPase activity are defective in negative regulation of the heat shock response: expression of mutant DnaK proteins results in filamentation
    • McCarty JS, Walker GC (1994) DnaK mutants defective in ATPase activity are defective in negative regulation of the heat shock response: expression of mutant DnaK proteins results in filamentation. J Bacteriol 176: 764-780.
    • (1994) J Bacteriol , vol.176 , pp. 764-780
    • McCarty, J.S.1    Walker, G.C.2
  • 74
    • 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
    • McDowall KJ, Cohen SN (1996) 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: 349-355.
    • (1996) J Mol Biol , vol.255 , pp. 349-355
    • McDowall, K.J.1    Cohen, S.N.2
  • 75
    • 0027273009 scopus 로고
    • The ams-I and rne-3071 temperature-sensitive mutations in the ams gene are in close proximity to each other and cause substitutions within a domain that resembles a product of the Escherichia coli mre locus
    • McDowall KJ, Hernandez RG, Lin-Chao S, Cohen SN (1993) The ams-I and rne-3071 temperature-sensitive mutations in the ams gene are in close proximity to each other and cause substitutions within a domain that resembles a product of the Escherichia coli mre locus. J Bacteriol 175: 4245-4249.
    • (1993) J Bacteriol , vol.175 , pp. 4245-4249
    • McDowall, K.J.1    Hernandez, R.G.2    Lin-Chao, S.3    Cohen, S.N.4
  • 76
    • 0029976430 scopus 로고    scopus 로고
    • Proteins associated with RNase E in a multicomponent ribonucleolytic complex
    • Miczak A, Kaberdin VR, Wei CL, Lin-Chao S (1996) Proteins associated with RNase E in a multicomponent ribonucleolytic complex. Proc Natl Acad Sci USA 93: 3865-3869.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 3865-3869
    • Miczak, A.1    Kaberdin, V.R.2    Wei, C.L.3    Lin-Chao, S.4
  • 77
    • 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 (1997) The exosome: a conserved eukaryotic RNA processing complex containing multiple 3″-> 5″ exoribonucleases. Cell 91: 457-466.
    • (1997) Cell , vol.91 , pp. 457-466
    • Mitchell, P.1    Petfalski, E.2    Shevchenko, A.3    Mann, M.4    Tollervey, D.5
  • 79
    • 0034710943 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase functions both as a 3′-5′ exonuclease and a poly(A) polymerase in Escherichia coli
    • Mohanty BK, Kushner SR (2000) Polynucleotide phosphorylase functions both as a 3′-5′ exonuclease and a poly(A) polymerase in Escherichia coli. Proc Natl Acad Sci 97: 11966-11971.
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 11966-11971
    • Mohanty, B.K.1    Kushner, S.R.2
  • 80
    • 0346980557 scopus 로고    scopus 로고
    • Bacterial mitosis: ParM of plasmid R1 moves plasmid DNA by an actin-like insertional polymerization mechanism
    • Møller-Jensen J, Borch J, Dam M, Jense RB, Roepstorff P, Gerdes K (2003) Bacterial mitosis: ParM of plasmid R1 moves plasmid DNA by an actin-like insertional polymerization mechanism. Mol Cell 12: 1477-1487.
    • (2003) Mol Cell , vol.12 , pp. 1477-1487
    • Møller-Jensen, J.1    Borch, J.2    Dam, M.3    Jense, R.B.4    Roepstorff, P.5    Gerdes, K.6
  • 81
    • 8544261105 scopus 로고    scopus 로고
    • Enolase in the RNA degradosome plays a crucial role in the rapid decay of glucose transporter mRNA in the response to phosphosugar stress in Escherichia coli
    • Morita T, Kawamoto H, Mizota T, Inada T, Aiba H (2004) Enolase in the RNA degradosome plays a crucial role in the rapid decay of glucose transporter mRNA in the response to phosphosugar stress in Escherichia coli. Mol Microbiol 54: 1063-1075.
    • (2004) Mol Microbiol , vol.54 , pp. 1063-1075
    • Morita, T.1    Kawamoto, H.2    Mizota, T.3    Inada, T.4    Aiba, H.5
  • 82
    • 24944507588 scopus 로고    scopus 로고
    • RNase E-based ribonucleoprotein complexes: mechanical basis of mRNA destabilization mediated by bacterial noncoding RNAs
    • Morita T, Maki K, Aiba H (2005) RNase E-based ribonucleoprotein complexes: mechanical basis of mRNA destabilization mediated by bacterial noncoding RNAs. Genes Dev 19: 2176-2186.
    • (2005) Genes Dev , vol.19 , pp. 2176-2186
    • Morita, T.1    Maki, K.2    Aiba, H.3
  • 83
    • 33645508496 scopus 로고    scopus 로고
    • Translational repression is sufficient for gene silencing by bacterial small noncoding RNAs in the absence of mRNA destruction
    • Morita T, Mochizuki Y, Aiba H (2006) Translational repression is sufficient for gene silencing by bacterial small noncoding RNAs in the absence of mRNA destruction. Proc Natl Acad Sci USA 103: 4858-4863.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 4858-4863
    • Morita, T.1    Mochizuki, Y.2    Aiba, H.3
  • 84
    • 0027250040 scopus 로고
    • Escherichia coli endoribonuclease RNase E: autoregulation of expression and site-specific cleavage of mRNA
    • Mudd EA, Higgins CF (1993) Escherichia coli endoribonuclease RNase E: autoregulation of expression and site-specific cleavage of mRNA. Mol Microbiol 9: 557-568.
    • (1993) Mol Microbiol , vol.9 , pp. 557-568
    • Mudd, E.A.1    Higgins, C.F.2
  • 85
    • 0032932638 scopus 로고    scopus 로고
    • Function, mechanism and regulation of bacterial ribonucleases
    • Nicholson AW (1999) Function, mechanism and regulation of bacterial ribonucleases. FEMS Microbiol Rev 23: 371-390.
    • (1999) FEMS Microbiol Rev , vol.23 , pp. 371-390
    • Nicholson, A.W.1
  • 86
    • 67349257830 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli polynucleotide phosphorylase core bound to RNase E, RNA and manganese: implications for catalytic mechanism and RNA degradosome assembly
    • Nurmohamed S, Vaidialingam B, Callaghan AJ, Luisi BF (2009) Crystal structure of Escherichia coli polynucleotide phosphorylase core bound to RNase E, RNA and manganese: implications for catalytic mechanism and RNA degradosome assembly. J Mol Biol 389: 17-33.
    • (2009) J Mol Biol , vol.389 , pp. 17-33
    • Nurmohamed, S.1    Vaidialingam, B.2    Callaghan, A.J.3    Luisi, B.F.4
  • 89
    • 0033995502 scopus 로고    scopus 로고
    • The yvaJ gene of Bacillus subtilis enocides a 3′-to-5′ exoribonuclease and is not essential in a strain lacking polynucleotide phosphorylase
    • Oussenko IA, Bechhofer DH (2002) The yvaJ gene of Bacillus subtilis enocides a 3′-to-5′ exoribonuclease and is not essential in a strain lacking polynucleotide phosphorylase. J Bacteriol 182: 2639-2642.
    • (2002) J Bacteriol , vol.182 , pp. 2639-2642
    • Oussenko, I.A.1    Bechhofer, D.H.2
  • 90
    • 34247547010 scopus 로고    scopus 로고
    • Sub-cellular localization of post-translational modifications of the Plasmodium yoelii enolase suggest moonlighting functions
    • Pal-Bowmick I, Vora HV, Jarori GK (2007) Sub-cellular localization of post-translational modifications of the Plasmodium yoelii enolase suggest moonlighting functions. Malaria J 6: 45-51.
    • (2007) Malaria J , vol.6 , pp. 45-51
    • Pal-Bowmick, I.1    Vora, H.V.2    Jarori, G.K.3
  • 91
    • 0016438636 scopus 로고
    • Quaternary structure of Escherichia coli polynucleotide phosphorylase: new evidence for a trimeric structure
    • Portier C (1975) Quaternary structure of Escherichia coli polynucleotide phosphorylase: new evidence for a trimeric structure. FEBS Letters 50: 79-81.
    • (1975) FEBS Letters , vol.50 , pp. 79-81
    • Portier, C.1
  • 92
    • 0029922992 scopus 로고    scopus 로고
    • A DEAD-box RNA helicase in the Escherichia coli RNA degradosome
    • Py B, Higgens CF, Krisch HM, Carpousis AJ (1996) A DEAD-box RNA helicase in the Escherichia coli RNA degradosome. Nature 381: 169-172.
    • (1996) Nature , vol.381 , pp. 169-172
    • Py, B.1    Higgens, C.F.2    Krisch, H.M.3    Carpousis, A.J.4
  • 93
    • 4344573414 scopus 로고    scopus 로고
    • The exosome, a molecular machine for controlled RNA degradation in both nucleus and cytoplasm
    • Raijmakers R, Schilders G, Pruijn GJM (2004) The exosome, a molecular machine for controlled RNA degradation in both nucleus and cytoplasm. Eur J Cell Biol 83: 175-183.
    • (2004) Eur J Cell Biol , vol.83 , pp. 175-183
    • Raijmakers, R.1    Schilders, G.2    Pruijn, G.J.M.3
  • 94
    • 0032970686 scopus 로고    scopus 로고
    • Poly(A) polymerase of Escherichia coli: characterization of the catalytic domain, an RNA binding site and regions for the interaction with proteins involved in mRNA degradation
    • Raynal LC, Carpousis AJ (1999) Poly(A) polymerase of Escherichia coli: characterization of the catalytic domain, an RNA binding site and regions for the interaction with proteins involved in mRNA degradation. Mol Microbiol 32: 765-775.
    • (1999) Mol Microbiol , vol.32 , pp. 765-775
    • Raynal, L.C.1    Carpousis, A.J.2
  • 96
    • 30544445654 scopus 로고    scopus 로고
    • Spatial control of bacterial division-site pacement
    • Rothfield L, Taghbalout A, Shih Y-L (2005) Spatial control of bacterial division-site pacement. Nat Rev Microbiol 31: 959-968.
    • (2005) Nat Rev Microbiol , vol.31 , pp. 959-968
    • Rothfield, L.1    Taghbalout, A.2    Shih, Y.-L.3
  • 98
    • 0037315564 scopus 로고    scopus 로고
    • Global RNA half-life analysis in Escherichia coli reveals positional patterns of transcript degradation
    • Selinger DW, Saxena RM, Cheung KJ, Church GM, Rosenow C (2003) Global RNA half-life analysis in Escherichia coli reveals positional patterns of transcript degradation. Genome Res 13: 216-223.
    • (2003) Genome Res , vol.13 , pp. 216-223
    • Selinger, D.W.1    Saxena, R.M.2    Cheung, K.J.3    Church, G.M.4    Rosenow, C.5
  • 100
    • 0037699937 scopus 로고    scopus 로고
    • Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two coiled cell poles
    • Shih Y-L, Le T, Rothfield L (2003) Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two coiled cell poles. Proc Natl Acad Sci 100: 7865-7870.
    • (2003) Proc Natl Acad Sci , vol.100 , pp. 7865-7870
    • Shih, Y.-L.1    Le, T.2    Rothfield, L.3
  • 102
    • 0027389009 scopus 로고
    • Functional interaction of heat shock protein GroEL with an RNase E-like activity in Escherichia coli
    • Sohlberg B, Lundberg U, Hartl F-U, Von Gabain A (1993) Functional interaction of heat shock protein GroEL with an RNase E-like activity in Escherichia coli. Proc Natl Acad Sci 90: 277-281.
    • (1993) Proc Natl Acad Sci , vol.90 , pp. 277-281
    • Sohlberg, B.1    Lundberg, U.2    Hartl, F.-U.3    von Gabain, A.4
  • 104
    • 33846818898 scopus 로고    scopus 로고
    • RNase E and the other constituents of the RNA degradosome are the components of the bacterial cytoskeleton
    • Taghbalout A, Rothfield L (2007) RNase E and the other constituents of the RNA degradosome are the components of the bacterial cytoskeleton. Proc Natl Acad Sci 104: 1667-1672.
    • (2007) Proc Natl Acad Sci , vol.104 , pp. 1667-1672
    • Taghbalout, A.1    Rothfield, L.2
  • 105
    • 54249144032 scopus 로고    scopus 로고
    • New insights into the cellular organization of the RNA processing and degradation machinery of Escherichia coli
    • Taghbalout A, Rothfield L (2008a) New insights into the cellular organization of the RNA processing and degradation machinery of Escherichia coli. Mol Microbiol 70: 780-782.
    • (2008) Mol Microbiol , vol.70 , pp. 780-782
    • Taghbalout, A.1    Rothfield, L.2
  • 106
    • 46649086171 scopus 로고    scopus 로고
    • RNase E and RNA helicase B play central roles in the cytoskeletal organization of the RNA degradosome
    • Taghbalout A, Rothfield L (2008b) RNase E and RNA helicase B play central roles in the cytoskeletal organization of the RNA degradosome. Biol Chem 283: 13850-13855.
    • (2008) Biol Chem , vol.283 , pp. 13850-13855
    • Taghbalout, A.1    Rothfield, L.2
  • 107
    • 77953985369 scopus 로고    scopus 로고
    • Self-assembly of the bacterial cytoskeleton-associated RNA helicase B protein into polymeric filamentous structures
    • Taghbalout A, Yang Q (2010) Self-assembly of the bacterial cytoskeleton-associated RNA helicase B protein into polymeric filamentous structures. Bacteriol 192: 3222-3226.
    • (2010) Bacteriol , vol.192 , pp. 3222-3226
    • Taghbalout, A.1    Yang, Q.2
  • 108
    • 21644439017 scopus 로고    scopus 로고
    • A decreased level of FtsZ is responsible for inviability of RNase E-deficient cells
    • Takada A, Nagai K, Wachi M (2005) A decreased level of FtsZ is responsible for inviability of RNase E-deficient cells. Cell Mol Biol 10: 733-741.
    • (2005) Cell Mol Biol , vol.10 , pp. 733-741
    • Takada, A.1    Nagai, K.2    Wachi, M.3
  • 109
    • 0034635423 scopus 로고    scopus 로고
    • The multiple activities of polyphosphate kinase of Escherichia coli and their subunit structure determined by radiation target analysis
    • Tzeng CM, Kornberg A (2000) The multiple activities of polyphosphate kinase of Escherichia coli and their subunit structure determined by radiation target analysis. J Biol Chem 275: 3977-3988.
    • (2000) J Biol Chem , vol.275 , pp. 3977-3988
    • Tzeng, C.M.1    Kornberg, A.2
  • 110
    • 0032727868 scopus 로고    scopus 로고
    • The exosome: a proteasome for RNA?
    • van Hoof A, Parker R (1999) The exosome: a proteasome for RNA? Cell 99: 347-350.
    • (1999) Cell , vol.99 , pp. 347-350
    • van Hoof, A.1    Parker, R.2
  • 113
    • 0023638691 scopus 로고
    • Mutant isolation and molecular cloning of mre genes, which determine cell shape, sensitivity to mecillinam, and amount of penicillin-binding proteins in Escherichia coli
    • Wachi M, Doi M, Tamaki S, Park W, Nakajima-Iijima S, Matsuhashi M (1987) Mutant isolation and molecular cloning of mre genes, which determine cell shape, sensitivity to mecillinam, and amount of penicillin-binding proteins in Escherichia coli. J Bacteriol 169: 4935-4940.
    • (1987) J Bacteriol , vol.169 , pp. 4935-4940
    • Wachi, M.1    Doi, M.2    Tamaki, S.3    Park, W.4    Nakajima-Iijima, S.5    Matsuhashi, M.6
  • 114
    • 21244498581 scopus 로고    scopus 로고
    • Ribonuclease PH plays a major role in the exonucleolytic maturation of CCA-containing tRNA precursors in Bacillus subtilis
    • doi: 10. 1093/nar/gki675
    • Wen T, Oussenko IA, Pellegrini O, Bechhofer DH, Condon C (2005) Ribonuclease PH plays a major role in the exonucleolytic maturation of CCA-containing tRNA precursors in Bacillus subtilis. Nucl Acids Res 33: doi: 10. 1093/nar/gki675.
    • (2005) Nucl Acids Res , vol.33
    • Wen, T.1    Oussenko, I.A.2    Pellegrini, O.3    Bechhofer, D.H.4    Condon, C.5
  • 115
    • 0027267498 scopus 로고
    • The Escherichia coli pcnB gene promotes adenylation of antisense RNAI of ColE1-type plasmids in vivo and degradation of RNAI decay intermediates
    • Xu F, Lin-Chao S, Cohen SN (1993) The Escherichia coli pcnB gene promotes adenylation of antisense RNAI of ColE1-type plasmids in vivo and degradation of RNAI decay intermediates. Proc Natl Acad Sci USA 90: 6756-6760.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 6756-6760
    • Xu, F.1    Lin-Chao, S.2    Cohen, S.N.3


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