메뉴 건너뛰기




Volumn 84, Issue C, 2009, Pages 1-41

Chapter 1 A Phylogenetic View of Bacterial Ribonucleases

Author keywords

[No Author keywords available]

Indexed keywords


EID: 59649127625     PISSN: 00796603     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Review
Times cited : (5)

References (197)
  • 1
    • 59649109125 scopus 로고
    • The order of induction and deinduction of the enzymes of the lactose operon in E. coli
    • Alpers D.H., and Tomkins G.M. The order of induction and deinduction of the enzymes of the lactose operon in E. coli. Proc Natl Acad Sci USA 53 (1965) 797-802
    • (1965) Proc Natl Acad Sci USA , vol.53 , pp. 797-802
    • Alpers, D.H.1    Tomkins, G.M.2
  • 2
    • 76549154030 scopus 로고
    • Biology, molecular and organismic
    • Dobzhansky T. Biology, molecular and organismic. Am Zool 4 (1964) 443-452
    • (1964) Am Zool , vol.4 , pp. 443-452
    • Dobzhansky, T.1
  • 3
    • 0037115876 scopus 로고    scopus 로고
    • The phylogenetic distribution of bacterial ribonucleases
    • Condon C., and Putzer H. The phylogenetic distribution of bacterial ribonucleases. Nucleic Acids Res 30 (2002) 5339-5346
    • (2002) Nucleic Acids Res , vol.30 , pp. 5339-5346
    • Condon, C.1    Putzer, H.2
  • 4
    • 0020530065 scopus 로고
    • Acquisitive evolution of ribitol dehydrogenase in Klebsiella pneumoniae
    • Thompson L.W., and Krawiec S. Acquisitive evolution of ribitol dehydrogenase in Klebsiella pneumoniae. J Bacteriol 154 (1983) 1027-1031
    • (1983) J Bacteriol , vol.154 , pp. 1027-1031
    • Thompson, L.W.1    Krawiec, S.2
  • 5
    • 20444419762 scopus 로고    scopus 로고
    • Was photosynthetic RuBisCO recruited by acquisitive evolution from RuBisCO-like proteins involved in sulfur metabolism?
    • Ashida H., Danchin A., and Yokota A. Was photosynthetic RuBisCO recruited by acquisitive evolution from RuBisCO-like proteins involved in sulfur metabolism?. Res Microbiol 156 (2005) 611-618
    • (2005) Res Microbiol , vol.156 , pp. 611-618
    • Ashida, H.1    Danchin, A.2    Yokota, A.3
  • 6
    • 0041595218 scopus 로고    scopus 로고
    • Allen C., Bekoff M., and Lauder G. (Eds), MIT Press, Cambridge, MA
    • In: Allen C., Bekoff M., and Lauder G. (Eds). Nature's Purposes (1998), MIT Press, Cambridge, MA
    • (1998) Nature's Purposes
  • 8
    • 0001415430 scopus 로고
    • Speculations on the origin and evolution of photosynthesis
    • Granick S. Speculations on the origin and evolution of photosynthesis. Annals New York Acad Sci 69 (1957) 292-308
    • (1957) Annals New York Acad Sci , vol.69 , pp. 292-308
    • Granick, S.1
  • 10
    • 0024254814 scopus 로고
    • Before enzymes and templates: Theory of surface metabolism
    • Wachtershauser G. Before enzymes and templates: Theory of surface metabolism. Microbiol. Rev. 52 (1988) 452-484
    • (1988) Microbiol. Rev. , vol.52 , pp. 452-484
    • Wachtershauser, G.1
  • 11
    • 0024893581 scopus 로고
    • Homeotopic transformation and the origin of translation
    • Danchin A. Homeotopic transformation and the origin of translation. Prog Biophys Mol Biol 54 (1989) 81-86
    • (1989) Prog Biophys Mol Biol , vol.54 , pp. 81-86
    • Danchin, A.1
  • 12
    • 26444558214 scopus 로고    scopus 로고
    • How essential are nonessential genes?
    • Fang G., Rocha E., and Danchin A. How essential are nonessential genes?. Mol Biol Evol 22 (2005) 2147-2156
    • (2005) Mol Biol Evol , vol.22 , pp. 2147-2156
    • Fang, G.1    Rocha, E.2    Danchin, A.3
  • 13
    • 33947725697 scopus 로고    scopus 로고
    • The extant core bacterial proteome is an archive of the origin of life
    • Danchin A., Fang G., and Noria S. The extant core bacterial proteome is an archive of the origin of life. Proteomics 7 (2007) 875-889
    • (2007) Proteomics , vol.7 , pp. 875-889
    • Danchin, A.1    Fang, G.2    Noria, S.3
  • 14
    • 0029847554 scopus 로고    scopus 로고
    • Selfish operons: Horizontal transfer may drive the evolution of gene clusters
    • Lawrence J.G., and Roth J.R. Selfish operons: Horizontal transfer may drive the evolution of gene clusters. Genetics 143 (1996) 1843-1860
    • (1996) Genetics , vol.143 , pp. 1843-1860
    • Lawrence, J.G.1    Roth, J.R.2
  • 15
    • 39549098697 scopus 로고    scopus 로고
    • Persistence drives gene clustering in bacterial genomes
    • Fang G., Rocha E.P., and Danchin A. Persistence drives gene clustering in bacterial genomes. BMC Genomics 9 (2008) 4
    • (2008) BMC Genomics , vol.9 , pp. 4
    • Fang, G.1    Rocha, E.P.2    Danchin, A.3
  • 16
    • 34249672905 scopus 로고    scopus 로고
    • Ribozyme catalysis of metabolism in the RNA world
    • Chen X., Li N., and Ellington A.D. Ribozyme catalysis of metabolism in the RNA world. Chem Biodivers 4 (2007) 633-655
    • (2007) Chem Biodivers , vol.4 , pp. 633-655
    • Chen, X.1    Li, N.2    Ellington, A.D.3
  • 18
    • 34249931851 scopus 로고    scopus 로고
    • OLE RNA, an RNA motif that is highly conserved in several extremophilic bacteria, is a substrate for and can be regulated by RNase P RNA
    • Ko J.H., and Altman S. OLE RNA, an RNA motif that is highly conserved in several extremophilic bacteria, is a substrate for and can be regulated by RNase P RNA. Proc Natl Acad Sci USA 104 (2007) 7815-7820
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 7815-7820
    • Ko, J.H.1    Altman, S.2
  • 19
    • 0024529973 scopus 로고
    • Ribonuclease P: An enzyme with a catalytic RNA subunit
    • Altman S. Ribonuclease P: An enzyme with a catalytic RNA subunit. Adv Enzymol Relat Areas Mol Biol 62 (1989) 1-36
    • (1989) Adv Enzymol Relat Areas Mol Biol , vol.62 , pp. 1-36
    • Altman, S.1
  • 21
    • 17144365857 scopus 로고    scopus 로고
    • Experimental RNomics in Aquifex aeolicus: Identification of small non-coding RNAs and the putative 6S RNA homolog
    • Willkomm D.K., Minnerup J., Huttenhofer A., and Hartmann R.K. Experimental RNomics in Aquifex aeolicus: Identification of small non-coding RNAs and the putative 6S RNA homolog. Nucleic Acids Res 33 (2005) 1949-1960
    • (2005) Nucleic Acids Res , vol.33 , pp. 1949-1960
    • Willkomm, D.K.1    Minnerup, J.2    Huttenhofer, A.3    Hartmann, R.K.4
  • 22
    • 43049088477 scopus 로고    scopus 로고
    • Life without RNase P
    • Randau L., Schroder I., and Soll D. Life without RNase P. Nature 453 (2008) 120-123
    • (2008) Nature , vol.453 , pp. 120-123
    • Randau, L.1    Schroder, I.2    Soll, D.3
  • 23
    • 44649177016 scopus 로고    scopus 로고
    • 5′-End maturation of tRNA in Aquifex aeolicus
    • Marszalkowski M., Willkomm D.K., and Hartmann R.K. 5′-End maturation of tRNA in Aquifex aeolicus. Biol Chem 389 (2008) 395-403
    • (2008) Biol Chem , vol.389 , pp. 395-403
    • Marszalkowski, M.1    Willkomm, D.K.2    Hartmann, R.K.3
  • 24
    • 0031711821 scopus 로고    scopus 로고
    • Ribonuclease P: Unity and diversity in a tRNA processing ribozyme
    • Frank D.N., and 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
  • 25
    • 0024851604 scopus 로고
    • Specific interactions in RNA enzyme-substrate complexes
    • Guerrier-Takada C., Lumelsky N., and Altman S. Specific interactions in RNA enzyme-substrate complexes. Science 246 (1989) 1578-1584
    • (1989) Science , vol.246 , pp. 1578-1584
    • Guerrier-Takada, C.1    Lumelsky, N.2    Altman, S.3
  • 26
    • 0029295957 scopus 로고
    • Processing of the precursor to the catalytic RNA subunit of RNase P from Escherichia coli
    • Lundberg U., and Altman S. Processing of the precursor to the catalytic RNA subunit of RNase P from Escherichia coli. RNA 1 (1995) 327-334
    • (1995) RNA , vol.1 , pp. 327-334
    • Lundberg, U.1    Altman, S.2
  • 27
    • 33749334411 scopus 로고    scopus 로고
    • Analysis of RNase P protein (RnpA) expression in Bacillus subtilis utilizing strains with suppressible rnpA expression
    • Gossringer M., Kretschmer-Kazemi Far R., and Hartmann R.K. Analysis of RNase P protein (RnpA) expression in Bacillus subtilis utilizing strains with suppressible rnpA expression. J Bacteriol 188 (2006) 6816-6823
    • (2006) J Bacteriol , vol.188 , pp. 6816-6823
    • Gossringer, M.1    Kretschmer-Kazemi Far, R.2    Hartmann, R.K.3
  • 28
    • 0025166185 scopus 로고
    • Complementation of an RNase P RNA (rnpB) gene deletion in Escherichia coli by homologous genes from distantly related eubacteria
    • Waugh D.S., and Pace N.R. Complementation of an RNase P RNA (rnpB) gene deletion in Escherichia coli by homologous genes from distantly related eubacteria. J Bacteriol 172 (1990) 6316-6322
    • (1990) J Bacteriol , vol.172 , pp. 6316-6322
    • Waugh, D.S.1    Pace, N.R.2
  • 29
    • 0032546728 scopus 로고    scopus 로고
    • Derivation of the three-dimensional architecture of bacterial ribonuclease P RNAs from comparative sequence analysis
    • Massire C., Jaeger L., and Westhof E. Derivation of the three-dimensional architecture of bacterial ribonuclease P RNAs from comparative sequence analysis. J Mol Biol 279 (1998) 773-793
    • (1998) J Mol Biol , vol.279 , pp. 773-793
    • Massire, C.1    Jaeger, L.2    Westhof, E.3
  • 30
    • 33645512683 scopus 로고    scopus 로고
    • Type A and B RNase P RNAs are interchangeable in vivo despite substantial biophysical differences
    • Wegscheid B., Condon C., and Hartmann R.K. Type A and B RNase P RNAs are interchangeable in vivo despite substantial biophysical differences. EMBO Rep 7 (2006) 411-417
    • (2006) EMBO Rep , vol.7 , pp. 411-417
    • Wegscheid, B.1    Condon, C.2    Hartmann, R.K.3
  • 31
    • 0029949699 scopus 로고    scopus 로고
    • Domain structure of the ribozyme from eubacterial ribonuclease P
    • Loria A., and Pan T. Domain structure of the ribozyme from eubacterial ribonuclease P. RNA 2 (1996) 551-563
    • (1996) RNA , vol.2 , pp. 551-563
    • Loria, A.1    Pan, T.2
  • 32
    • 33748863131 scopus 로고    scopus 로고
    • Bacterial RNase P: A new view of an ancient enzyme
    • Kazantsev A.V., and Pace N.R. Bacterial RNase P: A new view of an ancient enzyme. Nat Rev Microbiol 4 (2006) 729-740
    • (2006) Nat Rev Microbiol , vol.4 , pp. 729-740
    • Kazantsev, A.V.1    Pace, N.R.2
  • 33
    • 0035339722 scopus 로고    scopus 로고
    • Modular construction for function of a ribonucleoprotein enzyme: The catalytic domain of Bacillus subtilis RNase P complexed with B. subtilis RNase P protein
    • Loria A., and Pan T. Modular construction for function of a ribonucleoprotein enzyme: The catalytic domain of Bacillus subtilis RNase P complexed with B. subtilis RNase P protein. Nucleic Acids Res 29 (2001) 1892-1897
    • (2001) Nucleic Acids Res , vol.29 , pp. 1892-1897
    • Loria, A.1    Pan, T.2
  • 34
    • 0032530462 scopus 로고    scopus 로고
    • Evolutionary variation in bacterial RNase P RNAs
    • Haas E.S., and Brown J.W. Evolutionary variation in bacterial RNase P RNAs. Nucleic Acids Res 26 (1998) 4093-4099
    • (1998) Nucleic Acids Res , vol.26 , pp. 4093-4099
    • Haas, E.S.1    Brown, J.W.2
  • 35
    • 34548740836 scopus 로고    scopus 로고
    • In vitro detection of the enzymatic activity of folate-dependent tRNA (Uracil-54,-C5)-methyltransferase: evolutionary implications
    • Urbonavicius J., Brochier-Armanet C., Skouloubris S., Myllykallio H., and Grosjean H. In vitro detection of the enzymatic activity of folate-dependent tRNA (Uracil-54,-C5)-methyltransferase: evolutionary implications. Methods Enzymol 425 (2007) 103-119
    • (2007) Methods Enzymol , vol.425 , pp. 103-119
    • Urbonavicius, J.1    Brochier-Armanet, C.2    Skouloubris, S.3    Myllykallio, H.4    Grosjean, H.5
  • 36
    • 20244389141 scopus 로고    scopus 로고
    • Investigation of the phylogenetic relationships within the genus Bartonella based on comparative sequence analysis of the rnpB gene, 16S rDNA and 23S rDNA
    • Pitulle C., Strehse C., Brown J.W., and Breitschwerdt E.B. Investigation of the phylogenetic relationships within the genus Bartonella based on comparative sequence analysis of the rnpB gene, 16S rDNA and 23S rDNA. Int J Syst Evol Microbiol 52 (2002) 2075-2080
    • (2002) Int J Syst Evol Microbiol , vol.52 , pp. 2075-2080
    • Pitulle, C.1    Strehse, C.2    Brown, J.W.3    Breitschwerdt, E.B.4
  • 37
    • 0032999983 scopus 로고    scopus 로고
    • Detection of seven major evolutionary lineages in cyanobacteria based on the 16S rRNA gene sequence analysis with new sequences of five marine Synechococcus strains
    • Honda D., Yokota A., and Sugiyama J. Detection of seven major evolutionary lineages in cyanobacteria based on the 16S rRNA gene sequence analysis with new sequences of five marine Synechococcus strains. J Mol Evol 48 (1999) 723-739
    • (1999) J Mol Evol , vol.48 , pp. 723-739
    • Honda, D.1    Yokota, A.2    Sugiyama, J.3
  • 39
    • 2542452389 scopus 로고    scopus 로고
    • Signature sequences in diverse proteins provide evidence for the late divergence of the Order Aquificales
    • Griffiths E., and Gupta R.S. Signature sequences in diverse proteins provide evidence for the late divergence of the Order Aquificales. Int Microbiol 7 (2004) 41-52
    • (2004) Int Microbiol , vol.7 , pp. 41-52
    • Griffiths, E.1    Gupta, R.S.2
  • 40
    • 33751119816 scopus 로고    scopus 로고
    • Thermostable RNase P RNAs lacking P18 identified in the Aquificales
    • Marszalkowski M., Teune J.H., Steger G., Hartmann R.K., and Willkomm D.K. Thermostable RNase P RNAs lacking P18 identified in the Aquificales. RNA 12 (2006) 1915-1921
    • (2006) RNA , vol.12 , pp. 1915-1921
    • Marszalkowski, M.1    Teune, J.H.2    Steger, G.3    Hartmann, R.K.4    Willkomm, D.K.5
  • 41
    • 0029149054 scopus 로고
    • The planctomycetes: Emerging models for microbial ecology, evolution and cell biology
    • Fuerst J.A. The planctomycetes: Emerging models for microbial ecology, evolution and cell biology. Microbiology 141 Pt 7 (1995) 1493-1506
    • (1995) Microbiology , vol.141 , Issue.PART 7 , pp. 1493-1506
    • Fuerst, J.A.1
  • 42
    • 4344673663 scopus 로고    scopus 로고
    • Comparative analysis of ribonuclease P RNA of the planctomycetes
    • Butler M.K., and Fuerst J.A. Comparative analysis of ribonuclease P RNA of the planctomycetes. Int J Syst Evol Microbiol 54 (2004) 1333-1344
    • (2004) Int J Syst Evol Microbiol , vol.54 , pp. 1333-1344
    • Butler, M.K.1    Fuerst, J.A.2
  • 43
    • 0030024243 scopus 로고    scopus 로고
    • Sequence heterogeneities among 16S ribosomal RNA sequences, and their effect on phylogenetic analyses at the species level
    • Cilia V., Lafay B., and Christen R. Sequence heterogeneities among 16S ribosomal RNA sequences, and their effect on phylogenetic analyses at the species level. Mol Biol Evol 13 (1996) 451-461
    • (1996) Mol Biol Evol , vol.13 , pp. 451-461
    • Cilia, V.1    Lafay, B.2    Christen, R.3
  • 44
    • 1942443733 scopus 로고    scopus 로고
    • Divergence and redundancy of 16S rRNA sequences in genomes with multiple rrn operons
    • Acinas S.G., Marcelino L.A., Klepac-Ceraj V., and Polz M.F. Divergence and redundancy of 16S rRNA sequences in genomes with multiple rrn operons. J Bacteriol 186 (2004) 2629-2635
    • (2004) J Bacteriol , vol.186 , pp. 2629-2635
    • Acinas, S.G.1    Marcelino, L.A.2    Klepac-Ceraj, V.3    Polz, M.F.4
  • 45
    • 0035369055 scopus 로고    scopus 로고
    • Identification of a putative chromosomal replication origin from Helicobacter pylori and its interaction with the initiator protein DnaA
    • Zawilak A., Cebrat S., Mackiewicz P., Krol-Hulewicz A., Jakimowicz D., Messer W., et al. Identification of a putative chromosomal replication origin from Helicobacter pylori and its interaction with the initiator protein DnaA. Nucleic Acids Res 29 (2001) 2251-2259
    • (2001) Nucleic Acids Res , vol.29 , pp. 2251-2259
    • Zawilak, A.1    Cebrat, S.2    Mackiewicz, P.3    Krol-Hulewicz, A.4    Jakimowicz, D.5    Messer, W.6
  • 46
    • 0034814681 scopus 로고    scopus 로고
    • The ribonuclease P family
    • Hall T.A., and Brown J.W. The ribonuclease P family. Methods Enzymol 341 (2001) 56-77
    • (2001) Methods Enzymol , vol.341 , pp. 56-77
    • Hall, T.A.1    Brown, J.W.2
  • 48
    • 33947716757 scopus 로고    scopus 로고
    • Probing the architecture of the B. subtilis RNase P holoenzyme active site by cross-linking and affinity cleavage
    • Niranjanakumari S., Day-Storms J.J., Ahmed M., Hsieh J., Zahler N.H., Venters R.A., et al. Probing the architecture of the B. subtilis RNase P holoenzyme active site by cross-linking and affinity cleavage. RNA 13 (2007) 521-535
    • (2007) RNA , vol.13 , pp. 521-535
    • Niranjanakumari, S.1    Day-Storms, J.J.2    Ahmed, M.3    Hsieh, J.4    Zahler, N.H.5    Venters, R.A.6
  • 49
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: The Keio collection
    • 2006.0008
    • Baba T., Ara T., Hasegawa M., Takai Y., Okumura Y., Baba M., et al. Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: The Keio collection. Mol Syst Biol 2 (2006) 2006.0008
    • (2006) Mol Syst Biol , vol.2
    • Baba, T.1    Ara, T.2    Hasegawa, M.3    Takai, Y.4    Okumura, Y.5    Baba, M.6
  • 51
    • 0016087667 scopus 로고
    • On some principles governing molecular evolution
    • Kimura M., and Ota T. On some principles governing molecular evolution. Proc Natl Acad Sci USA 71 (1974) 2848-2852
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 2848-2852
    • Kimura, M.1    Ota, T.2
  • 52
    • 33748094844 scopus 로고    scopus 로고
    • Reducing intrinsic biochemical noise in cells and its thermodynamic limit
    • Qian H. Reducing intrinsic biochemical noise in cells and its thermodynamic limit. J Mol Biol 362 (2006) 387-392
    • (2006) J Mol Biol , vol.362 , pp. 387-392
    • Qian, H.1
  • 53
    • 35548995356 scopus 로고    scopus 로고
    • The RNA degradosome of Escherichia coli: An mRNA-degrading machine assembled on RNase E
    • Carpousis A.J. The RNA degradosome of Escherichia coli: An mRNA-degrading machine assembled on RNase E. Annu Rev Microbiol 61 (2007) 71-87
    • (2007) Annu Rev Microbiol , vol.61 , pp. 71-87
    • Carpousis, A.J.1
  • 55
    • 0032939521 scopus 로고    scopus 로고
    • mRNA degradation in bacteria
    • Rauhut R., and Klug G. mRNA degradation in bacteria. FEMS Microbiol Rev 23 (1999) 353-370
    • (1999) FEMS Microbiol Rev , vol.23 , pp. 353-370
    • Rauhut, R.1    Klug, G.2
  • 56
    • 33748414894 scopus 로고    scopus 로고
    • Unravelling the dynamics of RNA degradation by ribonuclease II and its RNA-bound complex
    • Frazao C., McVey C.E., Amblar M., Barbas A., Vonrhein C., Arraiano C.M., et al. Unravelling the dynamics of RNA degradation by ribonuclease II and its RNA-bound complex. Nature 443 (2006) 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
  • 57
    • 0344936574 scopus 로고    scopus 로고
    • Global analysis of genomic texts: The distribution of AGCT tetranucleotides in the Escherichia coli and Bacillus subtilis genomes predicts translational frameshifting and ribosomal hopping in several genes
    • Henaut A., Lisacek F., Nitschke P., Moszer I., and Danchin A. Global analysis of genomic texts: The distribution of AGCT tetranucleotides in the Escherichia coli and Bacillus subtilis genomes predicts translational frameshifting and ribosomal hopping in several genes. Electrophoresis 19 (1998) 515-527
    • (1998) Electrophoresis , vol.19 , pp. 515-527
    • Henaut, A.1    Lisacek, F.2    Nitschke, P.3    Moszer, I.4    Danchin, A.5
  • 58
    • 0026693656 scopus 로고
    • Enolase is present at the centrosome of HeLa cells
    • Johnstone S.A., Waisman D.M., and Rattner J.B. Enolase is present at the centrosome of HeLa cells. Exp Cell Res 202 (1992) 458-463
    • (1992) Exp Cell Res , vol.202 , pp. 458-463
    • Johnstone, S.A.1    Waisman, D.M.2    Rattner, J.B.3
  • 59
    • 33744475377 scopus 로고    scopus 로고
    • Alpha-crystallin expression affects microtubule assembly and prevents their aggregation
    • Xi J.H., Bai F., McGaha R., and Andley U.P. Alpha-crystallin expression affects microtubule assembly and prevents their aggregation. Faseb J 20 (2006) 846-857
    • (2006) Faseb J , vol.20 , pp. 846-857
    • Xi, J.H.1    Bai, F.2    McGaha, R.3    Andley, U.P.4
  • 62
    • 0030779484 scopus 로고    scopus 로고
    • Polyphosphate kinase is a component of the Escherichia coli RNA degradosome
    • Blum E., Py B., Carpousis A.J., and Higgins C.F. Polyphosphate kinase is a component of the Escherichia coli RNA degradosome. Mol Microbiol 26 (1997) 387-398
    • (1997) Mol Microbiol , vol.26 , pp. 387-398
    • Blum, E.1    Py, B.2    Carpousis, A.J.3    Higgins, C.F.4
  • 63
    • 14644415964 scopus 로고    scopus 로고
    • Localization of Escherichia coli poly(A) polymerase I in cellular membrane
    • Jasiecki J., and Wegrzyn G. Localization of Escherichia coli poly(A) polymerase I in cellular membrane. Biochem Biophys Res Commun 329 (2005) 598-602
    • (2005) Biochem Biophys Res Commun , vol.329 , pp. 598-602
    • Jasiecki, J.1    Wegrzyn, G.2
  • 64
    • 0031588599 scopus 로고    scopus 로고
    • Comparison between the Escherichia coli and Bacillus subtilis genomes suggests that a major function of polynucleotide phosphorylase is to synthesize CDP
    • Danchin A. Comparison between the Escherichia coli and Bacillus subtilis genomes suggests that a major function of polynucleotide phosphorylase is to synthesize CDP. DNA Res 4 (1997) 9-18
    • (1997) DNA Res , vol.4 , pp. 9-18
    • Danchin, A.1
  • 65
    • 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., and Cohen S.N. 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 (2001) 31651-31656
    • (2001) J Biol Chem , vol.276 , pp. 31651-31656
    • Feng, Y.1    Huang, H.2    Liao, J.3    Cohen, S.N.4
  • 68
    • 0002720053 scopus 로고    scopus 로고
    • Metabolic generation and utilization of phosphate bond energy
    • Nord F.F., and Werkman C.H. (Eds), Fordham University, New York, NY
    • Lipmann F. Metabolic generation and utilization of phosphate bond energy. In: Nord F.F., and Werkman C.H. (Eds). Advances in enzymology and related areas of molecular biology 1 (2006), Fordham University, New York, NY 99-162
    • (2006) Advances in enzymology and related areas of molecular biology , vol.1 , pp. 99-162
    • Lipmann, F.1
  • 69
    • 67649654098 scopus 로고    scopus 로고
    • Natural selection and immortality
    • Aug 22 [Epub ahead of Print]
    • Danchin A. Natural selection and immortality. Biogerontology (2008) Aug 22 [Epub ahead of Print]
    • (2008) Biogerontology
    • Danchin, A.1
  • 71
    • 0029918138 scopus 로고    scopus 로고
    • The anaerobic Escherichia coli ribonucleotide reductase. Subunit structure and iron sulfur center
    • Ollagnier S., Mulliez E., Gaillard J., Eliasson R., Fontecave M., and Reichard P. The anaerobic Escherichia coli ribonucleotide reductase. Subunit structure and iron sulfur center. J Biol Chem 271 (1996) 9410-9416
    • (1996) J Biol Chem , vol.271 , pp. 9410-9416
    • Ollagnier, S.1    Mulliez, E.2    Gaillard, J.3    Eliasson, R.4    Fontecave, M.5    Reichard, P.6
  • 72
    • 57549096867 scopus 로고
    • A hypothesis on a possible competitive relation between DNA synthesis and protein synthesis
    • Cohen S.S. A hypothesis on a possible competitive relation between DNA synthesis and protein synthesis. Cancer Res 20 (1960) 698-699
    • (1960) Cancer Res , vol.20 , pp. 698-699
    • Cohen, S.S.1
  • 73
    • 0036606915 scopus 로고    scopus 로고
    • Base composition bias might result from competition for metabolic resources
    • Rocha E.P., and Danchin A. Base composition bias might result from competition for metabolic resources. Trends Genet 18 (2002) 291-294
    • (2002) Trends Genet , vol.18 , pp. 291-294
    • Rocha, E.P.1    Danchin, A.2
  • 74
    • 0034435974 scopus 로고    scopus 로고
    • A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation
    • Symmons M.F., Jones G.H., and Luisi B.F. A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation. Structure 8 (2000) 1215-1226
    • (2000) Structure , vol.8 , pp. 1215-1226
    • Symmons, M.F.1    Jones, G.H.2    Luisi, B.F.3
  • 75
    • 0141453035 scopus 로고    scopus 로고
    • Domain analysis of the chloroplast polynucleotide phosphorylase reveals discrete functions in RNA degradation, polyadenylation, and sequence homology with exosome proteins
    • Yehudai-Resheff S., Portnoy V., Yogev S., Adir N., and Schuster G. Domain analysis of the chloroplast polynucleotide phosphorylase reveals discrete functions in RNA degradation, polyadenylation, and sequence homology with exosome proteins. Plant Cell 15 (2003) 2003-2019
    • (2003) Plant Cell , vol.15 , pp. 2003-2019
    • Yehudai-Resheff, S.1    Portnoy, V.2    Yogev, S.3    Adir, N.4    Schuster, G.5
  • 76
    • 0038687705 scopus 로고    scopus 로고
    • A Streptomyces coelicolor functional orthologue of Escherichia coli RNase E shows shuffling of catalytic and PNPase-binding domains
    • Lee K., and Cohen S.N. A Streptomyces coelicolor functional orthologue of Escherichia coli RNase E shows shuffling of catalytic and PNPase-binding domains. Mol Microbiol 48 (2003) 349-360
    • (2003) Mol Microbiol , vol.48 , pp. 349-360
    • Lee, K.1    Cohen, S.N.2
  • 78
    • 40549098736 scopus 로고    scopus 로고
    • UniProtKB/Swiss-Prot: the manually annotated section of the UniProt KnowledgeBase
    • Boutet E., Lieberherr D., Tognolli M., Schneider M., and Bairoch A. UniProtKB/Swiss-Prot: the manually annotated section of the UniProt KnowledgeBase. Methods Mol Biol 406 (2007) 89-112
    • (2007) Methods Mol Biol , vol.406 , pp. 89-112
    • Boutet, E.1    Lieberherr, D.2    Tognolli, M.3    Schneider, M.4    Bairoch, A.5
  • 79
    • 0026806544 scopus 로고
    • Characterization of Escherichia coli RNase PH
    • Kelly K.O., and Deutscher M.P. Characterization of Escherichia coli RNase PH. J Biol Chem 267 (1992) 17153-17158
    • (1992) J Biol Chem , vol.267 , pp. 17153-17158
    • Kelly, K.O.1    Deutscher, M.P.2
  • 80
    • 0030576503 scopus 로고    scopus 로고
    • Maturation pathways for E. coli tRNA precursors: A random multienzyme process in vivo
    • Li Z., and 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, Z.1    Deutscher, M.P.2
  • 81
    • 0042858117 scopus 로고    scopus 로고
    • Crystal structure of the tRNA processing enzyme RNase PH from Aquifex aeolicus
    • Ishii R., Nureki O., and Yokoyama S. Crystal structure of the tRNA processing enzyme RNase PH from Aquifex aeolicus. J Biol Chem 278 (2003) 32397-32404
    • (2003) J Biol Chem , vol.278 , pp. 32397-32404
    • Ishii, R.1    Nureki, O.2    Yokoyama, S.3
  • 82
    • 1342331853 scopus 로고    scopus 로고
    • Crystal structure of the phosphorolytic exoribonuclease RNase PH from Bacillus subtilis and implications for its quaternary structure and tRNA binding
    • Harlow L.S., Kadziola A., Jensen K.F., and Larsen S. Crystal structure of the phosphorolytic exoribonuclease RNase PH from Bacillus subtilis and implications for its quaternary structure and tRNA binding. Protein Sci 13 (2004) 668-677
    • (2004) Protein Sci , vol.13 , pp. 668-677
    • Harlow, L.S.1    Kadziola, A.2    Jensen, K.F.3    Larsen, S.4
  • 83
    • 21244498581 scopus 로고    scopus 로고
    • Ribonuclease PH plays a major role in the exonucleolytic maturation of CCA-containing tRNA precursors in Bacillus subtilis
    • Wen T., Oussenko I.A., Pellegrini O., Bechhofer D.H., and Condon C. Ribonuclease PH plays a major role in the exonucleolytic maturation of CCA-containing tRNA precursors in Bacillus subtilis. Nucleic Acids Res 33 (2005) 3636-3643
    • (2005) Nucleic Acids Res , vol.33 , pp. 3636-3643
    • Wen, T.1    Oussenko, I.A.2    Pellegrini, O.3    Bechhofer, D.H.4    Condon, C.5
  • 84
    • 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., and 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
  • 85
    • 42649116726 scopus 로고    scopus 로고
    • A comparative analysis of CCA-adding enzymes from human and E. coli: Differences in CCA addition and tRNA 3′-end repair
    • Lizano E., Scheibe M., Rammelt C., Betat H., and Morl M. A comparative analysis of CCA-adding enzymes from human and E. coli: Differences in CCA addition and tRNA 3′-end repair. Biochimie 90 5 (2008) 762-772
    • (2008) Biochimie , vol.90 , Issue.5 , pp. 762-772
    • Lizano, E.1    Scheibe, M.2    Rammelt, C.3    Betat, H.4    Morl, M.5
  • 86
    • 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., and Schuster G. The PNPase, exosome and RNA helicases as the building components of evolutionarily-conserved RNA degradation machines. J Biomed Sci 14 (2007) 523-532
    • (2007) J Biomed Sci , vol.14 , pp. 523-532
    • Lin-Chao, S.1    Chiou, N.T.2    Schuster, G.3
  • 87
    • 0029974966 scopus 로고    scopus 로고
    • Guanosine pentaphosphate synthetase from Streptomyces antibioticus is also a polynucleotide phosphorylase
    • Jones G.H., and Bibb M.J. Guanosine pentaphosphate synthetase from Streptomyces antibioticus is also a polynucleotide phosphorylase. J Bacteriol 178 (1996) 4281-4288
    • (1996) J Bacteriol , vol.178 , pp. 4281-4288
    • Jones, G.H.1    Bibb, M.J.2
  • 88
    • 0030771435 scopus 로고    scopus 로고
    • Guanosine tetra- and pentaphosphate promote accumulation of inorganic polyphosphate in Escherichia coli
    • Kuroda A., Murphy H., Cashel M., and Kornberg A. Guanosine tetra- and pentaphosphate promote accumulation of inorganic polyphosphate in Escherichia coli. J Biol Chem 272 (1997) 21240-21243
    • (1997) J Biol Chem , vol.272 , pp. 21240-21243
    • Kuroda, A.1    Murphy, H.2    Cashel, M.3    Kornberg, A.4
  • 89
    • 0035834062 scopus 로고    scopus 로고
    • Visualization of protein S1 within the 30S ribosomal subunit and its interaction with messenger RNA
    • Sengupta J., Agrawal R.K., and Frank J. Visualization of protein S1 within the 30S ribosomal subunit and its interaction with messenger RNA. Proc Natl Acad Sci USA 98 (2001) 11991-11996
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11991-11996
    • Sengupta, J.1    Agrawal, R.K.2    Frank, J.3
  • 91
    • 0036703022 scopus 로고    scopus 로고
    • Ribosomal protein S1 induces a conformational change of tmRNA; more than one protein S1 per molecule of tmRNA
    • Bordeau V., and Felden B. Ribosomal protein S1 induces a conformational change of tmRNA; more than one protein S1 per molecule of tmRNA. Biochimie 84 (2002) 723-729
    • (2002) Biochimie , vol.84 , pp. 723-729
    • Bordeau, V.1    Felden, B.2
  • 93
    • 33745951483 scopus 로고    scopus 로고
    • Characterization of the functional domains of Escherichia coli RNase II
    • Amblar M., Barbas A., Fialho A.M., and Arraiano C.M. Characterization of the functional domains of Escherichia coli RNase II. J Mol Biol 360 (2006) 921-933
    • (2006) J Mol Biol , vol.360 , pp. 921-933
    • Amblar, M.1    Barbas, A.2    Fialho, A.M.3    Arraiano, C.M.4
  • 94
    • 4143138726 scopus 로고    scopus 로고
    • Structural characterization of the RNase E S1 domain and identification of its oligonucleotide-binding and dimerization interfaces
    • Schubert M., Edge R.E., Lario P., Cook M.A., Strynadka N.C., Mackie G.A., et al. Structural characterization of the RNase E S1 domain and identification of its oligonucleotide-binding and dimerization interfaces. J Mol Biol 341 (2004) 37-54
    • (2004) J Mol Biol , vol.341 , pp. 37-54
    • Schubert, M.1    Edge, R.E.2    Lario, P.3    Cook, M.A.4    Strynadka, N.C.5    Mackie, G.A.6
  • 95
    • 33845887686 scopus 로고    scopus 로고
    • Activation of RegB endoribonuclease by S1 ribosomal protein requires an 11 nt conserved sequence
    • Durand S., Richard G., Bisaglia M., Laalami S., Bontems F., and Uzan M. Activation of RegB endoribonuclease by S1 ribosomal protein requires an 11 nt conserved sequence. Nucleic Acids Res 34 (2006) 6549-6560
    • (2006) Nucleic Acids Res , vol.34 , pp. 6549-6560
    • Durand, S.1    Richard, G.2    Bisaglia, M.3    Laalami, S.4    Bontems, F.5    Uzan, M.6
  • 96
    • 33847304137 scopus 로고    scopus 로고
    • Structural and functional studies of RegB, a new member of a family of sequence-specific ribonucleases involved in mRNA inactivation on the ribosome
    • Odaert B., Saida F., Aliprandi P., Durand S., Crechet J.B., Guerois R., et al. Structural and functional studies of RegB, a new member of a family of sequence-specific ribonucleases involved in mRNA inactivation on the ribosome. J Biol Chem 282 (2007) 2019-2028
    • (2007) J Biol Chem , vol.282 , pp. 2019-2028
    • Odaert, B.1    Saida, F.2    Aliprandi, P.3    Durand, S.4    Crechet, J.B.5    Guerois, R.6
  • 98
    • 0035253621 scopus 로고    scopus 로고
    • KH domain: One motif, two folds
    • Grishin N.V. KH domain: One motif, two folds. Nucleic Acids Res 29 (2001) 638-643
    • (2001) Nucleic Acids Res , vol.29 , pp. 638-643
    • Grishin, N.V.1
  • 99
    • 33745757322 scopus 로고    scopus 로고
    • Era and RbfA have overlapping function in ribosome biogenesis in Escherichia coli
    • Inoue K., Chen J., Tan Q., and Inouye M. Era and RbfA have overlapping function in ribosome biogenesis in Escherichia coli. J Mol Microbiol Biotechnol 11 (2006) 41-52
    • (2006) J Mol Microbiol Biotechnol , vol.11 , pp. 41-52
    • Inoue, K.1    Chen, J.2    Tan, Q.3    Inouye, M.4
  • 100
    • 29444446682 scopus 로고    scopus 로고
    • Functional analysis of the post-transcriptional regulator RsmA reveals a novel RNA-binding site
    • Heeb S., Kuehne S.A., Bycroft M., Crivii S., Allen M.D., Haas D., et al. Functional analysis of the post-transcriptional regulator RsmA reveals a novel RNA-binding site. J Mol Biol 355 (2006) 1026-1036
    • (2006) J Mol Biol , vol.355 , pp. 1026-1036
    • Heeb, S.1    Kuehne, S.A.2    Bycroft, M.3    Crivii, S.4    Allen, M.D.5    Haas, D.6
  • 101
    • 27144485749 scopus 로고    scopus 로고
    • Function of the conserved S1 and KH domains in polynucleotide phosphorylase
    • Stickney L.M., Hankins J.S., Miao X., and Mackie G.A. Function of the conserved S1 and KH domains in polynucleotide phosphorylase. J Bacteriol 187 (2005) 7214-7221
    • (2005) J Bacteriol , vol.187 , pp. 7214-7221
    • Stickney, L.M.1    Hankins, J.S.2    Miao, X.3    Mackie, G.A.4
  • 102
    • 40449098228 scopus 로고    scopus 로고
    • PNPase is a key player in the regulation of small RNAs that control the expression of outer membrane proteins
    • Andrade J.M., and Arraiano C.M. PNPase is a key player in the regulation of small RNAs that control the expression of outer membrane proteins. RNA 14 (2008) 543-551
    • (2008) RNA , vol.14 , pp. 543-551
    • Andrade, J.M.1    Arraiano, C.M.2
  • 103
    • 28044439868 scopus 로고    scopus 로고
    • RhlB helicase rather than enolase is the beta-subunit of the Escherichia coli polynucleotide phosphorylase (PNPase)-exoribonucleolytic complex
    • Lin P.H., and Lin-Chao S. RhlB helicase rather than enolase is the beta-subunit of the Escherichia coli polynucleotide phosphorylase (PNPase)-exoribonucleolytic complex. Proc Natl Acad Sci USA 102 (2005) 16590-16595
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 16590-16595
    • Lin, P.H.1    Lin-Chao, S.2
  • 104
    • 9644277144 scopus 로고    scopus 로고
    • The RNase E of Escherichia coli has at least two binding sites for DEAD-box RNA helicases: Functional replacement of RhlB by RhlE
    • Khemici V., Toesca I., Poljak L., Vanzo N.F., and Carpousis A.J. The RNase E of Escherichia coli has at least two binding sites for DEAD-box RNA helicases: Functional replacement of RhlB by RhlE. Mol Microbiol 54 (2004) 1422-1430
    • (2004) Mol Microbiol , vol.54 , pp. 1422-1430
    • Khemici, V.1    Toesca, I.2    Poljak, L.3    Vanzo, N.F.4    Carpousis, A.J.5
  • 105
    • 0033375911 scopus 로고    scopus 로고
    • Mechanisms of mRNA surveillance in eukaryotes
    • Hilleren P., and Parker R. Mechanisms of mRNA surveillance in eukaryotes. Annu Rev Genet 33 (1999) 229-260
    • (1999) Annu Rev Genet , vol.33 , pp. 229-260
    • Hilleren, P.1    Parker, R.2
  • 106
    • 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 G.G., Chang H.Y., Lin C.S., and Lin-Chao S. 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 (2002) 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
  • 107
    • 3042691769 scopus 로고    scopus 로고
    • HrpA, a DEAH-box RNA helicase, is involved in mRNA processing of a fimbrial operon in Escherichia coli
    • Koo J.T., Choe J., and Moseley S.L. HrpA, a DEAH-box RNA helicase, is involved in mRNA processing of a fimbrial operon in Escherichia coli. Mol Microbiol 52 (2004) 1813-1826
    • (2004) Mol Microbiol , vol.52 , pp. 1813-1826
    • Koo, J.T.1    Choe, J.2    Moseley, S.L.3
  • 108
    • 0027361712 scopus 로고
    • Beat the clock: Paradigms for NTPases in the maintenance of biological fidelity
    • Burgess S.M., and Guthrie C. Beat the clock: Paradigms for NTPases in the maintenance of biological fidelity. Trends Biochem Sci 18 (1993) 381-384
    • (1993) Trends Biochem Sci , vol.18 , pp. 381-384
    • Burgess, S.M.1    Guthrie, C.2
  • 109
    • 41949105648 scopus 로고    scopus 로고
    • Allosteric activation of the ATPase activity of the Escherichia coli RhlB RNA helicase
    • Worrall J.A., Howe F.S., McKay A.R., Robinson C.V., and Luisi B.F. Allosteric activation of the ATPase activity of the Escherichia coli RhlB RNA helicase. J Biol Chem 283 9 (2008) 5567-5576
    • (2008) J Biol Chem , vol.283 , Issue.9 , pp. 5567-5576
    • Worrall, J.A.1    Howe, F.S.2    McKay, A.R.3    Robinson, C.V.4    Luisi, B.F.5
  • 110
    • 38449108345 scopus 로고    scopus 로고
    • RNA misfolding and the action of chaperones
    • Russell R. RNA misfolding and the action of chaperones. Front Biosci 13 (2008) 1-20
    • (2008) Front Biosci , vol.13 , pp. 1-20
    • Russell, R.1
  • 111
    • 25844462537 scopus 로고    scopus 로고
    • Coping with cold: The genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125
    • Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N., et al. Coping with cold: The genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125. Genome Res 15 (2005) 1325-1335
    • (2005) Genome Res , vol.15 , pp. 1325-1335
    • Medigue, C.1    Krin, E.2    Pascal, G.3    Barbe, V.4    Bernsel, A.5    Bertin, P.N.6
  • 112
    • 9244221616 scopus 로고    scopus 로고
    • Inorganic polyphosphate in the origin and survival of species
    • Brown M.R., and Kornberg A. Inorganic polyphosphate in the origin and survival of species. Proc Natl Acad Sci USA 101 (2004) 16085-16087
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 16085-16087
    • Brown, M.R.1    Kornberg, A.2
  • 113
    • 33847685201 scopus 로고    scopus 로고
    • A polyphosphate kinase 1 (ppk1) mutant of Pseudomonas aeruginosa exhibits multiple ultrastructural and functional defects
    • Fraley C.D., Rashid M.H., Lee S.S., Gottschalk R., Harrison J., Wood P.J., et al. A polyphosphate kinase 1 (ppk1) mutant of Pseudomonas aeruginosa exhibits multiple ultrastructural and functional defects. Proc Natl Acad Sci USA 104 (2007) 3526-3531
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 3526-3531
    • Fraley, C.D.1    Rashid, M.H.2    Lee, S.S.3    Gottschalk, R.4    Harrison, J.5    Wood, P.J.6
  • 115
    • 0037168609 scopus 로고    scopus 로고
    • A polyphosphate kinase (PPK2) widely conserved in bacteria
    • Zhang H., Ishige K., and Kornberg A. A polyphosphate kinase (PPK2) widely conserved in bacteria. Proc Natl Acad Sci USA 99 (2002) 16678-16683
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16678-16683
    • Zhang, H.1    Ishige, K.2    Kornberg, A.3
  • 116
    • 2942563978 scopus 로고    scopus 로고
    • Characterization of Mycobacterium tuberculosis NAD kinase: Functional analysis of the full-length enzyme by site-directed mutagenesis
    • Raffaelli N., Finaurini L., Mazzola F., Pucci L., Sorci L., Amici A., et al. Characterization of Mycobacterium tuberculosis NAD kinase: Functional analysis of the full-length enzyme by site-directed mutagenesis. Biochemistry 43 (2004) 7610-7617
    • (2004) Biochemistry , vol.43 , pp. 7610-7617
    • Raffaelli, N.1    Finaurini, L.2    Mazzola, F.3    Pucci, L.4    Sorci, L.5    Amici, A.6
  • 117
    • 33846818898 scopus 로고    scopus 로고
    • RNaseE and the other constituents of the RNA degradosome are components of the bacterial cytoskeleton
    • Taghbalout A., and Rothfield L. RNaseE and the other constituents of the RNA degradosome are components of the bacterial cytoskeleton. Proc Natl Acad Sci USA 104 (2007) 1667-1672
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 1667-1672
    • Taghbalout, A.1    Rothfield, L.2
  • 118
    • 84923400776 scopus 로고    scopus 로고
    • Uehara memorial foundation symposium genome science: Towards a new paradigm?
    • Tokyo
    • Noria S., and Danchin A. Uehara memorial foundation symposium genome science: Towards a new paradigm?. International Congress Series 1246 (2002) 3-13 Tokyo
    • (2002) International Congress Series , vol.1246 , pp. 3-13
    • Noria, S.1    Danchin, A.2
  • 119
    • 0031835534 scopus 로고    scopus 로고
    • Nucleoside diphosphate kinase: Role in bacterial growth, virulence, cell signalling and polysaccharide synthesis
    • Chakrabarty A.M. Nucleoside diphosphate kinase: Role in bacterial growth, virulence, cell signalling and polysaccharide synthesis. Mol Microbiol 28 (1998) 875-882
    • (1998) Mol Microbiol , vol.28 , pp. 875-882
    • Chakrabarty, A.M.1
  • 120
    • 2942562280 scopus 로고    scopus 로고
    • Evolutionary relatedness between glycolytic enzymes most frequently occurring in genomes
    • Oslancova A., and Janecek S. Evolutionary relatedness between glycolytic enzymes most frequently occurring in genomes. Folia Microbiol (Praha) 49 (2004) 247-258
    • (2004) Folia Microbiol (Praha) , vol.49 , pp. 247-258
    • Oslancova, A.1    Janecek, S.2
  • 122
    • 15244343863 scopus 로고    scopus 로고
    • mRNA decay in prokaryotes and eukaryotes: Different approaches to a similar problem
    • Kushner S.R. mRNA decay in prokaryotes and eukaryotes: Different approaches to a similar problem. IUBMB Life 56 (2004) 585-594
    • (2004) IUBMB Life , vol.56 , pp. 585-594
    • Kushner, S.R.1
  • 123
    • 21844443073 scopus 로고    scopus 로고
    • Addition of poly(A) and heteropolymeric 3′ ends in Bacillus subtilis wild-type and polynucleotide phosphorylase-deficient strains
    • Campos-Guillen J., Bralley P., Jones G.H., Bechhofer D.H., and Olmedo-Alvarez G. Addition of poly(A) and heteropolymeric 3′ ends in Bacillus subtilis wild-type and polynucleotide phosphorylase-deficient strains. J Bacteriol 187 (2005) 4698-4706
    • (2005) J Bacteriol , vol.187 , pp. 4698-4706
    • Campos-Guillen, J.1    Bralley, P.2    Jones, G.H.3    Bechhofer, D.H.4    Olmedo-Alvarez, G.5
  • 124
    • 36849032886 scopus 로고    scopus 로고
    • Sensing of 5′ monophosphate by Escherichia coli RNase G can significantly enhance association with RNA and stimulate the decay of functional mRNA transcripts in vivo
    • Jourdan S.S., and McDowall K.J. Sensing of 5′ monophosphate by Escherichia coli RNase G can significantly enhance association with RNA and stimulate the decay of functional mRNA transcripts in vivo. Mol Microbiol 67 (2008) 102-115
    • (2008) Mol Microbiol , vol.67 , pp. 102-115
    • Jourdan, S.S.1    McDowall, K.J.2
  • 125
    • 0042497078 scopus 로고    scopus 로고
    • RNase G-dependent degradation of the eno mRNA encoding a glycolysis enzyme enolase in Escherichia coli
    • Kaga N., Umitsuki G., Nagai K., and Wachi M. RNase G-dependent degradation of the eno mRNA encoding a glycolysis enzyme enolase in Escherichia coli. Biosci Biotechnol Biochem 66 (2002) 2216-2220
    • (2002) Biosci Biotechnol Biochem , vol.66 , pp. 2216-2220
    • Kaga, N.1    Umitsuki, G.2    Nagai, K.3    Wachi, M.4
  • 126
    • 0027955358 scopus 로고
    • Cytoplasmic axial filaments in Escherichia coli cells: Possible function in the mechanism of chromosome segregation and cell division
    • Okada Y., Wachi M., Hirata A., Suzuki K., Nagai K., and Matsuhashi M. Cytoplasmic axial filaments in Escherichia coli cells: Possible function in the mechanism of chromosome segregation and cell division. J Bacteriol 176 (1994) 917-922
    • (1994) J Bacteriol , vol.176 , pp. 917-922
    • Okada, Y.1    Wachi, M.2    Hirata, A.3    Suzuki, K.4    Nagai, K.5    Matsuhashi, M.6
  • 127
    • 0033532514 scopus 로고    scopus 로고
    • Escherichia coli cafA gene encodes a novel RNase, designated as RNase G, involved in processing of the 5′ end of 16S rRNA
    • Wachi M., Umitsuki G., Shimizu M., Takada A., and Nagai K. Escherichia coli cafA gene encodes a novel RNase, designated as RNase G, involved in processing of the 5′ end of 16S rRNA. Biochem Biophys Res Commun 259 (1999) 483-488
    • (1999) Biochem Biophys Res Commun , vol.259 , pp. 483-488
    • Wachi, M.1    Umitsuki, G.2    Shimizu, M.3    Takada, A.4    Nagai, K.5
  • 128
    • 11144297942 scopus 로고    scopus 로고
    • Characterization of Aquifex aeolicus RNase E/G
    • Kaberdin V.R., and Bizebard T. Characterization of Aquifex aeolicus RNase E/G. Biochem Biophys Res Commun 327 (2005) 382-392
    • (2005) Biochem Biophys Res Commun , vol.327 , pp. 382-392
    • Kaberdin, V.R.1    Bizebard, T.2
  • 129
    • 1442325396 scopus 로고    scopus 로고
    • The function of RNase G in Escherichia coli is constrained by its amino and carboxyl termini
    • Deana A., and Belasco J.G. The function of RNase G in Escherichia coli is constrained by its amino and carboxyl termini. Mol Microbiol 51 (2004) 1205-1217
    • (2004) Mol Microbiol , vol.51 , pp. 1205-1217
    • Deana, A.1    Belasco, J.G.2
  • 130
    • 34147145981 scopus 로고    scopus 로고
    • Quaternary structure and biochemical properties of mycobacterial RNase E/G
    • Zeller M.E., Csanadi A., Miczak A., Rose T., Bizebard T., and Kaberdin V.R. Quaternary structure and biochemical properties of mycobacterial RNase E/G. Biochem J 403 (2007) 207-215
    • (2007) Biochem J , vol.403 , pp. 207-215
    • Zeller, M.E.1    Csanadi, A.2    Miczak, A.3    Rose, T.4    Bizebard, T.5    Kaberdin, V.R.6
  • 131
    • 33845719997 scopus 로고    scopus 로고
    • Maturation of the 5′ end of Bacillus subtilis 16S rRNA by the essential ribonuclease YkqC/RNase J1
    • Britton R.A., Wen T., Schaefer L., Pellegrini O., Uicker W.C., Mathy N., et al. Maturation of the 5′ end of Bacillus subtilis 16S rRNA by the essential ribonuclease YkqC/RNase J1. Mol Microbiol 63 (2007) 127-138
    • (2007) Mol Microbiol , vol.63 , pp. 127-138
    • Britton, R.A.1    Wen, T.2    Schaefer, L.3    Pellegrini, O.4    Uicker, W.C.5    Mathy, N.6
  • 132
    • 33748705968 scopus 로고    scopus 로고
    • Identification of a novel regulatory protein (CsrD) that targets the global regulatory RNAs CsrB and CsrC for degradation by RNase E
    • Suzuki K., Babitzke P., Kushner S.R., and Romeo T. Identification of a novel regulatory protein (CsrD) that targets the global regulatory RNAs CsrB and CsrC for degradation by RNase E. Genes Dev 20 (2006) 2605-2617
    • (2006) Genes Dev , vol.20 , pp. 2605-2617
    • Suzuki, K.1    Babitzke, P.2    Kushner, S.R.3    Romeo, T.4
  • 133
    • 34347402424 scopus 로고    scopus 로고
    • Complexes of tRNA and maturation enzymes: Shaping up for translation
    • Li H. Complexes of tRNA and maturation enzymes: Shaping up for translation. Curr Opin Struct Biol 17 (2007) 293-301
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 293-301
    • Li, H.1
  • 134
    • 27144495430 scopus 로고    scopus 로고
    • Structure of Escherichia coli RNase E catalytic domain and implications for RNA turnover
    • Callaghan A.J., Marcaida M.J., Stead J.A., McDowall K.J., Scott W.G., and Luisi B.F. Structure of Escherichia coli RNase E catalytic domain and implications for RNA turnover. Nature 437 (2005) 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
  • 135
    • 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., and 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
  • 136
    • 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., et al. RraA. a protein inhibitor of RNase E activity that globally modulates RNA abundance in E. coli. Cell 114 (2003) 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
  • 137
    • 33748506522 scopus 로고    scopus 로고
    • Differential modulation of E. coli mRNA abundance by inhibitory proteins that alter the composition of the degradosome
    • Gao J., Lee K., Zhao M., Qiu J., Zhan X., Saxena A., et al. Differential modulation of E. coli mRNA abundance by inhibitory proteins that alter the composition of the degradosome. Mol Microbiol 61 (2006) 394-406
    • (2006) Mol Microbiol , vol.61 , pp. 394-406
    • Gao, J.1    Lee, K.2    Zhao, M.3    Qiu, J.4    Zhan, X.5    Saxena, A.6
  • 138
    • 34948859355 scopus 로고    scopus 로고
    • Metallo-beta-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily
    • Bebrone C. Metallo-beta-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily. Biochem Pharmacol 74 (2007) 1686-1701
    • (2007) Biochem Pharmacol , vol.74 , pp. 1686-1701
    • Bebrone, C.1
  • 139
    • 34247157802 scopus 로고    scopus 로고
    • Nucleases of the metallo-beta-lactamase family and their role in DNA and RNA metabolism
    • Dominski Z. Nucleases of the metallo-beta-lactamase family and their role in DNA and RNA metabolism. Crit Rev Biochem Mol Biol 42 (2007) 67-93
    • (2007) Crit Rev Biochem Mol Biol , vol.42 , pp. 67-93
    • Dominski, Z.1
  • 140
    • 33947360611 scopus 로고    scopus 로고
    • When all's zed and done: The structure and function of RNase Z in prokaryotes
    • Redko Y., Li de Lasierra-Gallay I., and Condon C. When all's zed and done: The structure and function of RNase Z in prokaryotes. Nat Rev Microbiol 5 (2007) 278-286
    • (2007) Nat Rev Microbiol , vol.5 , pp. 278-286
    • Redko, Y.1    Li de Lasierra-Gallay, I.2    Condon, C.3
  • 141
    • 0043239333 scopus 로고    scopus 로고
    • Endonucleolytic processing of CCA-less tRNA precursors by RNase Z in Bacillus subtilis
    • Pellegrini O., Nezzar J., Marchfelder A., Putzer H., and Condon C. Endonucleolytic processing of CCA-less tRNA precursors by RNase Z in Bacillus subtilis. EMBO J 22 (2003) 4534-4543
    • (2003) EMBO J , vol.22 , pp. 4534-4543
    • Pellegrini, O.1    Nezzar, J.2    Marchfelder, A.3    Putzer, H.4    Condon, C.5
  • 142
    • 20444465226 scopus 로고    scopus 로고
    • The RNase Z homologue encoded by Escherichia coli elaC gene is RNase BN
    • Ezraty B., Dahlgren B., and Deutscher M.P. The RNase Z homologue encoded by Escherichia coli elaC gene is RNase BN. J Biol Chem 280 (2005) 16542-16545
    • (2005) J Biol Chem , vol.280 , pp. 16542-16545
    • Ezraty, B.1    Dahlgren, B.2    Deutscher, M.P.3
  • 143
    • 33645826534 scopus 로고    scopus 로고
    • RNase Z in Escherichia coli plays a significant role in mRNA decay
    • Perwez T., and Kushner S.R. RNase Z in Escherichia coli plays a significant role in mRNA decay. Mol Microbiol 60 (2006) 723-737
    • (2006) Mol Microbiol , vol.60 , pp. 723-737
    • Perwez, T.1    Kushner, S.R.2
  • 144
    • 29044449835 scopus 로고    scopus 로고
    • The tRNase Z family of proteins: Physiological functions, substrate specificity and structural properties
    • Vogel A., Schilling O., Spath B., and Marchfelder A. The tRNase Z family of proteins: Physiological functions, substrate specificity and structural properties. Biol Chem 386 (2005) 1253-1264
    • (2005) Biol Chem , vol.386 , pp. 1253-1264
    • Vogel, A.1    Schilling, O.2    Spath, B.3    Marchfelder, A.4
  • 145
    • 17844361922 scopus 로고    scopus 로고
    • Ribonucleases J1 and J2: Two novel endoribonucleases in B. subtilis with functional homology to E. coli RNase E
    • Even S., Pellegrini O., Zig L., Labas V., Vinh J., Brechemmier-Baey D., et al. Ribonucleases J1 and J2: Two novel endoribonucleases in B. subtilis with functional homology to E. coli RNase E. Nucleic Acids Res 33 (2005) 2141-2152
    • (2005) Nucleic Acids Res , vol.33 , pp. 2141-2152
    • Even, S.1    Pellegrini, O.2    Zig, L.3    Labas, V.4    Vinh, J.5    Brechemmier-Baey, D.6
  • 146
    • 34249101864 scopus 로고    scopus 로고
    • 5′-to-3′ exoribonuclease activity in bacteria: Role of RNase J1 in rRNA maturation and 5′ stability of mRNA
    • Mathy N., Benard L., Pellegrini O., Daou R., Wen T., and Condon C. 5′-to-3′ exoribonuclease activity in bacteria: Role of RNase J1 in rRNA maturation and 5′ stability of mRNA. Cell 129 (2007) 681-692
    • (2007) Cell , vol.129 , pp. 681-692
    • Mathy, N.1    Benard, L.2    Pellegrini, O.3    Daou, R.4    Wen, T.5    Condon, C.6
  • 148
    • 0033901449 scopus 로고    scopus 로고
    • RNase III processing of intervening sequences found in helix 9 of 23S rRNA in the alpha subclass of Proteobacteria
    • Evguenieva-Hackenberg E., and Klug G. RNase III processing of intervening sequences found in helix 9 of 23S rRNA in the alpha subclass of Proteobacteria. J Bacteriol 182 (2000) 4719-4729
    • (2000) J Bacteriol , vol.182 , pp. 4719-4729
    • Evguenieva-Hackenberg, E.1    Klug, G.2
  • 150
    • 0037377346 scopus 로고    scopus 로고
    • SsrA-mediated trans-translation plays a role in mRNA quality control by facilitating degradation of truncated mRNAs
    • Yamamoto Y., Sunohara T., Jojima K., Inada T., and Aiba H. SsrA-mediated trans-translation plays a role in mRNA quality control by facilitating degradation of truncated mRNAs. RNA 9 (2003) 408-418
    • (2003) RNA , vol.9 , pp. 408-418
    • Yamamoto, Y.1    Sunohara, T.2    Jojima, K.3    Inada, T.4    Aiba, H.5
  • 151
    • 34247519181 scopus 로고    scopus 로고
    • Trans-translation: The tmRNA-mediated surveillance mechanism for ribosome rescue, directed protein degradation, and nonstop mRNA decay
    • Dulebohn D., Choy J., Sundermeier T., Okan N., and Karzai A.W. Trans-translation: The tmRNA-mediated surveillance mechanism for ribosome rescue, directed protein degradation, and nonstop mRNA decay. Biochemistry 46 (2007) 4681-4693
    • (2007) Biochemistry , vol.46 , pp. 4681-4693
    • Dulebohn, D.1    Choy, J.2    Sundermeier, T.3    Okan, N.4    Karzai, A.W.5
  • 152
    • 33751358590 scopus 로고    scopus 로고
    • RNase R degrades non-stop mRNAs selectively in an SmpB-tmRNA-dependent manner
    • Richards J., Mehta P., and Karzai A.W. RNase R degrades non-stop mRNAs selectively in an SmpB-tmRNA-dependent manner. Mol Microbiol 62 (2006) 1700-1712
    • (2006) Mol Microbiol , vol.62 , pp. 1700-1712
    • Richards, J.1    Mehta, P.2    Karzai, A.W.3
  • 153
    • 41049097536 scopus 로고    scopus 로고
    • Cleavage of mRNAs and role of tmRNA system under amino acid starvation in Escherichia coli
    • Li X., Yagi M., Morita T., and Aiba H. Cleavage of mRNAs and role of tmRNA system under amino acid starvation in Escherichia coli. Mol Microbiol 68 2 (2008) 462-473
    • (2008) Mol Microbiol , vol.68 , Issue.2 , pp. 462-473
    • Li, X.1    Yagi, M.2    Morita, T.3    Aiba, H.4
  • 154
    • 43449118061 scopus 로고    scopus 로고
    • Mini-III, an unusual member of the RNase III family of enzymes, catalyzes 23S ribosomal RNA maturation in B. subtilis
    • Redko Y., Bechhofer D.H., and Condon C. Mini-III, an unusual member of the RNase III family of enzymes, catalyzes 23S ribosomal RNA maturation in B. subtilis. Mol Microbiol 68 (2008) 1096-1106
    • (2008) Mol Microbiol , vol.68 , pp. 1096-1106
    • Redko, Y.1    Bechhofer, D.H.2    Condon, C.3
  • 155
    • 0033575262 scopus 로고    scopus 로고
    • Ribonuclease activity of rat liver perchloric acid-soluble protein, a potent inhibitor of protein synthesis
    • Morishita R., Kawagoshi A., Sawasaki T., Madin K., Ogasawara T., Oka T., et al. Ribonuclease activity of rat liver perchloric acid-soluble protein, a potent inhibitor of protein synthesis. J Biol Chem 274 (1999) 20688-20692
    • (1999) J Biol Chem , vol.274 , pp. 20688-20692
    • Morishita, R.1    Kawagoshi, A.2    Sawasaki, T.3    Madin, K.4    Ogasawara, T.5    Oka, T.6
  • 156
    • 33749645818 scopus 로고    scopus 로고
    • Functional analysis of 11 putative essential genes in Bacillus subtilis
    • Hunt A., Rawlins J.P., Thomaides H.B., and Errington J. Functional analysis of 11 putative essential genes in Bacillus subtilis. Microbiology 152 (2006) 2895-2907
    • (2006) Microbiology , vol.152 , pp. 2895-2907
    • Hunt, A.1    Rawlins, J.P.2    Thomaides, H.B.3    Errington, J.4
  • 157
    • 0037977118 scopus 로고    scopus 로고
    • RNA processing and degradation in Bacillus subtilis
    • Condon C. RNA processing and degradation in Bacillus subtilis. Microbiol Mol Biol Rev 67 (2003) 157-174
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 157-174
    • Condon, C.1
  • 159
    • 0030447708 scopus 로고    scopus 로고
    • Identification and characterization of the Escherichia coli rbn gene encoding the tRNA processing enzyme RNase BN
    • Callahan C., and 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
  • 160
    • 19544363942 scopus 로고    scopus 로고
    • Universal biases in protein composition of model prokaryotes
    • Pascal G., Medigue C., and Danchin A. Universal biases in protein composition of model prokaryotes. Proteins 60 (2005) 27-35
    • (2005) Proteins , vol.60 , pp. 27-35
    • Pascal, G.1    Medigue, C.2    Danchin, A.3
  • 161
    • 34548089729 scopus 로고    scopus 로고
    • Evolution of ribonuclease H genes in prokaryotes to avoid inheritance of redundant genes
    • Kochiwa H., Tomita M., and Kanai A. Evolution of ribonuclease H genes in prokaryotes to avoid inheritance of redundant genes. BMC Evol Biol 7 (2007) 128
    • (2007) BMC Evol Biol , vol.7 , pp. 128
    • Kochiwa, H.1    Tomita, M.2    Kanai, A.3
  • 162
    • 4344595870 scopus 로고    scopus 로고
    • Identification of the first archaeal Type 1 RNase H gene from Halobacterium sp. NRC-1: Archaeal RNase HI can cleave an RNA-DNA junction
    • Ohtani N., Yanagawa H., Tomita M., and Itaya M. Identification of the first archaeal Type 1 RNase H gene from Halobacterium sp. NRC-1: Archaeal RNase HI can cleave an RNA-DNA junction. Biochem J 381 (2004) 795-802
    • (2004) Biochem J , vol.381 , pp. 795-802
    • Ohtani, N.1    Yanagawa, H.2    Tomita, M.3    Itaya, M.4
  • 163
    • 25644450448 scopus 로고    scopus 로고
    • Bacillus subtilis YkuK protein is distantly related to RNase H
    • Knizewski L., and Ginalski K. Bacillus subtilis YkuK protein is distantly related to RNase H. FEMS Microbiol Lett 251 (2005) 341-346
    • (2005) FEMS Microbiol Lett , vol.251 , pp. 341-346
    • Knizewski, L.1    Ginalski, K.2
  • 164
    • 33749578566 scopus 로고    scopus 로고
    • Substrate recognition and catalysis by the exoribonuclease RNase R
    • Vincent H.A., and Deutscher M.P. Substrate recognition and catalysis by the exoribonuclease RNase R. J Biol Chem 281 (2006) 29769-29775
    • (2006) J Biol Chem , vol.281 , pp. 29769-29775
    • Vincent, H.A.1    Deutscher, M.P.2
  • 165
    • 0037077311 scopus 로고    scopus 로고
    • Purification and characterization of the Escherichia coli exoribonuclease RNase R. Comparison with RNase II
    • Cheng Z.F., and Deutscher M.P. Purification and characterization of the Escherichia coli exoribonuclease RNase R. Comparison with RNase II. J Biol Chem 277 (2002) 21624-21629
    • (2002) J Biol Chem , vol.277 , pp. 21624-21629
    • Cheng, Z.F.1    Deutscher, M.P.2
  • 166
    • 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., Klein F., Sulthana S., Jager S., Jagannadham M.V., Evguenieva-Hackenberg E., et al. Exoribonuclease R interacts with endoribonuclease E and an RNA helicase in the psychrotrophic bacterium Pseudomonas syringae Lz4W. J Biol Chem 280 (2005) 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
  • 167
    • 0035064787 scopus 로고    scopus 로고
    • RNase II levels change according to the growth conditions: Characterization of gmr, a new Escherichia coli gene involved in the modulation of RNase II
    • Cairrao F., Chora A., Zilhao R., Carpousis A.J., and Arraiano C.M. RNase II levels change according to the growth conditions: Characterization of gmr, a new Escherichia coli gene involved in the modulation of RNase II. Mol Microbiol 39 (2001) 1550-1561
    • (2001) Mol Microbiol , vol.39 , pp. 1550-1561
    • Cairrao, F.1    Chora, A.2    Zilhao, R.3    Carpousis, A.J.4    Arraiano, C.M.5
  • 168
    • 0018980250 scopus 로고
    • Apparent involvement of ribonuclease D in the 3′ processing of tRNA precursors
    • Cudny H., and Deutscher M.P. Apparent involvement of ribonuclease D in the 3′ processing of tRNA precursors. Proc Natl Acad Sci USA 77 (1980) 837-841
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 837-841
    • Cudny, H.1    Deutscher, M.P.2
  • 169
    • 0021169997 scopus 로고
    • Ribonuclease T: New exoribonuclease possibly involved in end-turnover of tRNA
    • Deutscher M.P., Marlor C.W., and Zaniewski R. Ribonuclease T: New exoribonuclease possibly involved in end-turnover of tRNA. Proc Natl Acad Sci USA 81 (1984) 4290-4293
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 4290-4293
    • Deutscher, M.P.1    Marlor, C.W.2    Zaniewski, R.3
  • 170
    • 36749062371 scopus 로고    scopus 로고
    • Reassessment of the in vivo functions of DNA polymerase I and RNase H in bacterial cell growth
    • Fukushima S., Itaya M., Kato H., Ogasawara N., and Yoshikawa H. Reassessment of the in vivo functions of DNA polymerase I and RNase H in bacterial cell growth. J Bacteriol 189 (2007) 8575-8583
    • (2007) J Bacteriol , vol.189 , pp. 8575-8583
    • Fukushima, S.1    Itaya, M.2    Kato, H.3    Ogasawara, N.4    Yoshikawa, H.5
  • 171
    • 38349117689 scopus 로고    scopus 로고
    • The bacterial enzyme RppH triggers messenger RNA degradation by 5′ pyrophosphate removal
    • Deana A., Celesnik H., and Belasco J.G. The bacterial enzyme RppH triggers messenger RNA degradation by 5′ pyrophosphate removal. Nature 451 (2008) 355-358
    • (2008) Nature , vol.451 , pp. 355-358
    • Deana, A.1    Celesnik, H.2    Belasco, J.G.3
  • 173
    • 0031801223 scopus 로고    scopus 로고
    • Aeromonas hydrophila adenylyl cyclase 2: A new class of adenylyl cyclases with thermophilic properties and sequence similarities to proteins from hyperthermophilic archaebacteria
    • Sismeiro O., Trotot P., Biville F., Vivares C., and Danchin A. Aeromonas hydrophila adenylyl cyclase 2: A new class of adenylyl cyclases with thermophilic properties and sequence similarities to proteins from hyperthermophilic archaebacteria. J Bacteriol 180 (1998) 3339-3344
    • (1998) J Bacteriol , vol.180 , pp. 3339-3344
    • Sismeiro, O.1    Trotot, P.2    Biville, F.3    Vivares, C.4    Danchin, A.5
  • 174
    • 33646739111 scopus 로고    scopus 로고
    • The NYN domains: Novel predicted RNAses with a PIN domain-like fold
    • Anantharaman V., and Aravind L. The NYN domains: Novel predicted RNAses with a PIN domain-like fold. RNA Biol 3 (2006) 18-27
    • (2006) RNA Biol , vol.3 , pp. 18-27
    • Anantharaman, V.1    Aravind, L.2
  • 175
    • 0034841160 scopus 로고    scopus 로고
    • Oligoribonucleotide-based gene-specific transcription inhibitors that target the open complex
    • Milne L., Perrin D.M., and Sigman D.S. Oligoribonucleotide-based gene-specific transcription inhibitors that target the open complex. Methods 23 (2001) 160-168
    • (2001) Methods , vol.23 , pp. 160-168
    • Milne, L.1    Perrin, D.M.2    Sigman, D.S.3
  • 176
    • 0016711596 scopus 로고
    • A novel oligoribonuclease of Escherichia coli. II. Mechanism of action
    • Datta A.K., and Niyogi K. A novel oligoribonuclease of Escherichia coli. II. Mechanism of action. J Biol Chem 250 (1975) 7313-7319
    • (1975) J Biol Chem , vol.250 , pp. 7313-7319
    • Datta, A.K.1    Niyogi, K.2
  • 177
    • 0033995794 scopus 로고    scopus 로고
    • Sulfur metabolism in Escherichia coli and related bacteria: Facts and fiction
    • Sekowska A., Kung H.F., and Danchin A. Sulfur metabolism in Escherichia coli and related bacteria: Facts and fiction. J Mol Microbiol Biotechnol 2 (2000) 145-177
    • (2000) J Mol Microbiol Biotechnol , vol.2 , pp. 145-177
    • Sekowska, A.1    Kung, H.F.2    Danchin, A.3
  • 178
    • 33646853530 scopus 로고    scopus 로고
    • Oligoribonuclease is a common downstream target of lithium-induced pAp accumulation in Escherichia coli and human cells
    • Mechold U., Ogryzko V., Ngo S., and Danchin A. Oligoribonuclease is a common downstream target of lithium-induced pAp accumulation in Escherichia coli and human cells. Nucleic Acids Res 34 (2006) 2364-2373
    • (2006) Nucleic Acids Res , vol.34 , pp. 2364-2373
    • Mechold, U.1    Ogryzko, V.2    Ngo, S.3    Danchin, A.4
  • 179
    • 4844220489 scopus 로고    scopus 로고
    • Functional and phylogenetic analysis of a plant-inducible oligoribonuclease (orn) gene from an indigenous Pseudomonas plasmid
    • Zhang X.X., Lilley A.K., Bailey M.J., and Rainey P.B. Functional and phylogenetic analysis of a plant-inducible oligoribonuclease (orn) gene from an indigenous Pseudomonas plasmid. Microbiology 150 (2004) 2889-2898
    • (2004) Microbiology , vol.150 , pp. 2889-2898
    • Zhang, X.X.1    Lilley, A.K.2    Bailey, M.J.3    Rainey, P.B.4
  • 180
    • 34547851775 scopus 로고    scopus 로고
    • YtqI from Bacillus subtilis has both oligoribonuclease and pAp-phosphatase activity
    • Mechold U., Fang G., Ngo S., Ogryzko V., and Danchin A. YtqI from Bacillus subtilis has both oligoribonuclease and pAp-phosphatase activity. Nucleic Acids Res 35 (2007) 4552-4561
    • (2007) Nucleic Acids Res , vol.35 , pp. 4552-4561
    • Mechold, U.1    Fang, G.2    Ngo, S.3    Ogryzko, V.4    Danchin, A.5
  • 181
    • 0036842854 scopus 로고    scopus 로고
    • Bacillus subtilis YhaM, a member of a new family of 3′-to-5′ exonucleases in gram-positive bacteria
    • Oussenko I.A., Sanchez R., and Bechhofer D.H. Bacillus subtilis YhaM, a member of a new family of 3′-to-5′ exonucleases in gram-positive bacteria. J Bacteriol 184 (2002) 6250-6259
    • (2002) J Bacteriol , vol.184 , pp. 6250-6259
    • Oussenko, I.A.1    Sanchez, R.2    Bechhofer, D.H.3
  • 182
    • 33645894689 scopus 로고    scopus 로고
    • Cyclic di-GMP as a second messenger
    • Romling U., and Amikam D. Cyclic di-GMP as a second messenger. Curr Opin Microbiol 9 (2006) 218-228
    • (2006) Curr Opin Microbiol , vol.9 , pp. 218-228
    • Romling, U.1    Amikam, D.2
  • 183
    • 24744457756 scopus 로고    scopus 로고
    • Identification and characterization of a cyclic di-GMP-specific phosphodiesterase and its allosteric control by GTP
    • Christen M., Christen B., Folcher M., Schauerte A., and Jenal U. Identification and characterization of a cyclic di-GMP-specific phosphodiesterase and its allosteric control by GTP. J Biol Chem 280 (2005) 30829-30837
    • (2005) J Biol Chem , vol.280 , pp. 30829-30837
    • Christen, M.1    Christen, B.2    Folcher, M.3    Schauerte, A.4    Jenal, U.5
  • 184
    • 0033935581 scopus 로고    scopus 로고
    • The natural evolutionary relationships among prokaryotes
    • Gupta R.S. The natural evolutionary relationships among prokaryotes. Crit Rev Microbiol 26 (2000) 111-131
    • (2000) Crit Rev Microbiol , vol.26 , pp. 111-131
    • Gupta, R.S.1
  • 185
    • 0037197889 scopus 로고    scopus 로고
    • The crystal structure of exonuclease RecJ bound to Mn2+ ion suggests how its characteristic motifs are involved in exonuclease activity
    • Yamagata A., Kakuta Y., Masui R., and Fukuyama K. The crystal structure of exonuclease RecJ bound to Mn2+ ion suggests how its characteristic motifs are involved in exonuclease activity. Proc Natl Acad Sci USA 99 (2002) 5908-5912
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5908-5912
    • Yamagata, A.1    Kakuta, Y.2    Masui, R.3    Fukuyama, K.4
  • 186
    • 0035370491 scopus 로고    scopus 로고
    • Overexpression, biophysical characterization, and crystallization of ribonuclease I from Escherichia coli, a broad-specificity enzyme in the RNase T2 family
    • Padmanabhan S., Zhou K., Chu C.Y., Lim R.W., and Lim L.W. Overexpression, biophysical characterization, and crystallization of ribonuclease I from Escherichia coli, a broad-specificity enzyme in the RNase T2 family. Arch Biochem Biophys 390 (2001) 42-50
    • (2001) Arch Biochem Biophys , vol.390 , pp. 42-50
    • Padmanabhan, S.1    Zhou, K.2    Chu, C.Y.3    Lim, R.W.4    Lim, L.W.5
  • 187
    • 33747855297 scopus 로고    scopus 로고
    • DomainSieve: a protein domain-based screen that led to the identification of dam-associated genes with potential link to DNA maintenance
    • Brezellec P., Hoebeke M., Hiet M.S., Pasek S., and Ferat J.L. DomainSieve: a protein domain-based screen that led to the identification of dam-associated genes with potential link to DNA maintenance. Bioinformatics 22 (2006) 1935-1941
    • (2006) Bioinformatics , vol.22 , pp. 1935-1941
    • Brezellec, P.1    Hoebeke, M.2    Hiet, M.S.3    Pasek, S.4    Ferat, J.L.5
  • 188
    • 3843123048 scopus 로고    scopus 로고
    • Bacillus subtilis YhcR, a high-molecular-weight, nonspecific endonuclease with a unique domain structure
    • Oussenko I.A., Sanchez R., and Bechhofer D.H. Bacillus subtilis YhcR, a high-molecular-weight, nonspecific endonuclease with a unique domain structure. J Bacteriol 186 (2004) 5376-5383
    • (2004) J Bacteriol , vol.186 , pp. 5376-5383
    • Oussenko, I.A.1    Sanchez, R.2    Bechhofer, D.H.3
  • 189
    • 33748309126 scopus 로고    scopus 로고
    • Shutdown decay of mRNA
    • Condon C. Shutdown decay of mRNA. Mol Microbiol 61 (2006) 573-583
    • (2006) Mol Microbiol , vol.61 , pp. 573-583
    • Condon, C.1
  • 190
    • 0027522090 scopus 로고
    • chpA and chpB, Escherichia coli chromosomal homologs of the pem locus responsible for stable maintenance of plasmid R100
    • Masuda Y., Miyakawa K., Nishimura Y., and Ohtsubo E. chpA and chpB, Escherichia coli chromosomal homologs of the pem locus responsible for stable maintenance of plasmid R100. J Bacteriol 175 (1993) 6850-6856
    • (1993) J Bacteriol , vol.175 , pp. 6850-6856
    • Masuda, Y.1    Miyakawa, K.2    Nishimura, Y.3    Ohtsubo, E.4
  • 192
    • 0027461096 scopus 로고
    • Autoregulation by cooperative binding of the PemI and PemK proteins to the promoter region of the pem operon
    • Tsuchimoto S., and Ohtsubo E. Autoregulation by cooperative binding of the PemI and PemK proteins to the promoter region of the pem operon. Mol Gen Genet 237 (1993) 81-88
    • (1993) Mol Gen Genet , vol.237 , pp. 81-88
    • Tsuchimoto, S.1    Ohtsubo, E.2
  • 193
    • 19944417284 scopus 로고    scopus 로고
    • The Bacillus subtilis ydcDE operon encodes an endoribonuclease of the MazF/PemK family and its inhibitor
    • Pellegrini O., Mathy N., Gogos A., Shapiro L., and Condon C. The Bacillus subtilis ydcDE operon encodes an endoribonuclease of the MazF/PemK family and its inhibitor. Mol Microbiol 56 (2005) 1139-1148
    • (2005) Mol Microbiol , vol.56 , pp. 1139-1148
    • Pellegrini, O.1    Mathy, N.2    Gogos, A.3    Shapiro, L.4    Condon, C.5
  • 194
    • 14244266086 scopus 로고    scopus 로고
    • Toxin-antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotes
    • Pandey D.P., and Gerdes K. Toxin-antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotes. Nucleic Acids Res 33 (2005) 966-976
    • (2005) Nucleic Acids Res , vol.33 , pp. 966-976
    • Pandey, D.P.1    Gerdes, K.2
  • 195
    • 13744261009 scopus 로고    scopus 로고
    • A novel endoribonuclease, RNase LS, in Escherichia coli
    • Otsuka Y., and Yonesaki T. A novel endoribonuclease, RNase LS, in Escherichia coli. Genetics 169 (2005) 13-20
    • (2005) Genetics , vol.169 , pp. 13-20
    • Otsuka, Y.1    Yonesaki, T.2
  • 196
    • 10644274361 scopus 로고    scopus 로고
    • Towards a comprehensive understanding of Bacillus subtilis cell physiology by physiological proteomics
    • Hecker M., and Volker U. Towards a comprehensive understanding of Bacillus subtilis cell physiology by physiological proteomics. Proteomics 4 (2004) 3727-3750
    • (2004) Proteomics , vol.4 , pp. 3727-3750
    • Hecker, M.1    Volker, U.2
  • 197
    • 57549088634 scopus 로고    scopus 로고
    • Archives or palimpsests? Bacterial genomes unveil a scenario for the origin of fife
    • Danchin A. Archives or palimpsests? Bacterial genomes unveil a scenario for the origin of fife. Biol Theory 2 (2007) 52-61
    • (2007) Biol Theory , vol.2 , pp. 52-61
    • Danchin, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.