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Volumn 2, Issue 1, 2011, Pages

Specific inhibition of bacterial RNase T2 by helix 41 of 16S ribosomal RNA

Author keywords

[No Author keywords available]

Indexed keywords

RIBONUCLEASE; RIBONUCLEASE T2; RNA 16S; UNCLASSIFIED DRUG; RIBONUCLEASE T(2);

EID: 82555196600     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms1553     Document Type: Article
Times cited : (24)

References (39)
  • 1
    • 0001654554 scopus 로고
    • Studies on ribonucleases in takadiastase
    • Sato, K. & Egami, F. Studies on ribonucleases in takadiastase. J. Biochem. 44, 753-767 (1957).
    • (1957) J. Biochem. , vol.44 , pp. 753-767
    • Sato, K.1    Egami, F.2
  • 2
    • 77952585622 scopus 로고    scopus 로고
    • T2 family ribonucleases: Ancient enzymes with diverse roles
    • Luhtala, N. & Parker, R. T2 family ribonucleases: ancient enzymes with diverse roles. Trends Biochem. Sci. 35, 253-259 (2010).
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 253-259
    • Luhtala, N.1    Parker, R.2
  • 3
    • 0000326707 scopus 로고
    • Phosphate-regulated induction of intracellular ribonucleases in cultured tomato (Lycopersicon esculentum) cells
    • Loffler, A., Abel, S., Jost, W., Beintema, J. J. & Glund, K. Phosphate-regulated induction of intracellular ribonucleases in cultured tomato (Lycopersicon esculentum) cells. Plant Physiol. 98, 1472-1478 (1992).
    • (1992) Plant Physiol. , vol.98 , pp. 1472-1478
    • Loffler, A.1    Abel, S.2    Jost, W.3    Beintema, J.J.4    Glund, K.5
  • 4
    • 0001491584 scopus 로고
    • Induction of an extracellular ribonuclease in cultured tomato cells upon phosphate starvation
    • Nurnberger, T., Abel, S., Jost, W. & Glund, K. Induction of an extracellular ribonuclease in cultured tomato cells upon phosphate starvation. Plant Physiol. 92, 970-976 (1990). (Pubitemid 120029786)
    • (1990) Plant Physiology , vol.92 , Issue.4 , pp. 970-976
    • Nurnberger, T.1    Abel, S.2    Jost, W.3    Glund, K.4
  • 5
    • 35748977936 scopus 로고    scopus 로고
    • Identification and biochemical characterization of unique secretory nucleases of the human enteric pathogen, Entamoeba histolytica
    • DOI 10.1074/jbc.M705975200
    • McGugan, G. C. Jr., Joshi, M. B. & Dwyer, D. M. Identification and biochemical characterization of unique secretory nucleases of the human enteric pathogen, Entamoeba histolytica. J. Biol. Chem. 282, 31789-31802 (2007). (Pubitemid 350044888)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.43 , pp. 31789-31802
    • McGugan Jr., G.C.1    Joshi, M.B.2    Dwyer, D.M.3
  • 6
    • 65249152479 scopus 로고    scopus 로고
    • The RNase Rny1p cleaves tRNAs and promotes cell death during oxidative stress in Saccharomyces cerevisiae
    • Thompson, D. M. & Parker, R. The RNase Rny1p cleaves tRNAs and promotes cell death during oxidative stress in Saccharomyces cerevisiae. J. Cell Biol. 185, 43-50 (2009).
    • (2009) J. Cell Biol. , vol.185 , pp. 43-50
    • Thompson, D.M.1    Parker, R.2
  • 7
    • 52949145277 scopus 로고    scopus 로고
    • TRNA cleavage is a conserved response to oxidative stress in eukaryotes
    • Thompson, D. M., Lu, C., Green, P. J. & Parker, R. tRNA cleavage is a conserved response to oxidative stress in eukaryotes. RNA 14, 2095-2103 (2008).
    • (2008) RNA , vol.14 , pp. 2095-2103
    • Thompson, D.M.1    Lu, C.2    Green, P.J.3    Parker, R.4
  • 8
    • 0037085304 scopus 로고    scopus 로고
    • rns and ribotoxin L3 loop
    • DOI 10.1074/jbc.M104147200
    • Langedijk, J. P. Translocation activity of C-terminal domain of pestivirus Erns and ribotoxin L3 loop. J. Biol. Chem. 277, 5308-5314 (2002). (Pubitemid 34968575)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.7 , pp. 5308-5314
    • Langedijk, J.P.M.1
  • 9
    • 0027238125 scopus 로고
    • Processing of the envelope glycoproteins of pestiviruses
    • Rumenapf, T., Unger, G., Strauss, J. H. & Thiel, H. J. Processing of the envelope glycoproteins of pestiviruses. J. Virol. 67, 3288-3294 (1993). (Pubitemid 23143701)
    • (1993) Journal of Virology , vol.67 , Issue.6 , pp. 3288-3294
    • Rumenapf, T.1    Unger, G.2    Strauss, J.H.3    Thiel, H.-J.4
  • 10
    • 77953238904 scopus 로고    scopus 로고
    • Protein interactions and subcellular localization in S-RNase-based self-incompatibility
    • Sims, T. L., Patel, A. & Shrestha, P. Protein interactions and subcellular localization in S-RNase-based self-incompatibility. Biochem. Soc. Trans. 38, 622-626 (2010).
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 622-626
    • Sims, T.L.1    Patel, A.2    Shrestha, P.3
  • 11
    • 0242496945 scopus 로고    scopus 로고
    • Degradation of stable RNA in Bacteria
    • DOI 10.1074/jbc.R300031200
    • Deutscher, M. P. Degradation of stable RNA in bacteria. J. Biol. Chem. 278, 45041-45044 (2003). (Pubitemid 37432634)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.46 , pp. 45041-45044
    • Deutscher, M.P.1
  • 12
    • 0032932638 scopus 로고    scopus 로고
    • Function, mechanism and regulation of bacterial ribonucleases
    • DOI 10.1016/S0168-6445(99)00013-3, PII S0168644599000133
    • Nicholson, A. W. Function, mechanism and regulation of bacterial ribonucleases. FEMS Microbiol. Rev. 23, 371-390 (1999). (Pubitemid 29236184)
    • (1999) FEMS Microbiology Reviews , vol.23 , Issue.3 , pp. 371-390
    • Nicholson, A.W.1
  • 13
    • 0025294939 scopus 로고
    • Escherichia coli rna gene encoding RNase I: Cloning overexpression, subcellular distribution of the enzyme, and use of an rna deletion to identify additional RNases
    • Zhu, L. Q., Gangopadhyay, T., Padmanabha, K. P. & Deutscher, M. P. Escherichia coli rna gene encoding RNase I: cloning, overexpression, subcellular distribution of the enzyme, and use of an rna deletion to identify additional RNases. J. Bacteriol. 172, 3146-3151 (1990). (Pubitemid 20179767)
    • (1990) Journal of Bacteriology , vol.172 , Issue.6 , pp. 3146-3151
    • Zhu, L.1    Gangopadhyay, T.2    Padmanabha, K.P.3    Deutscher, M.P.4
  • 14
    • 0021160119 scopus 로고
    • A multiple mutant of Escherichia coli lacking the exoribonucleases RNase II, RNase D, and RNase BN
    • Zaniewski, R., Petkaitis, E. & Deutscher, M. P. A multiple mutant of Escherichia coli lacking the exoribonucleases RNase II, RNase D, and RNase BN. J. Biol. Chem. 259, 11651-11653 (1984). (Pubitemid 14022076)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.19 , pp. 11651-11653
    • Zaniewski, R.1    Petkaitis, E.2    Deutscher, M.P.3
  • 15
    • 49749188739 scopus 로고
    • Latent ribonuclease activity in a ribonucleoprotein
    • Elson, D. Latent ribonuclease activity in a ribonucleoprotein. Biochim. Biophys. Acta 27, 216-217 (1958).
    • (1958) Biochim. Biophys. Acta , vol.27 , pp. 216-217
    • Elson, D.1
  • 16
    • 0000600593 scopus 로고
    • Purification and mechanism of action of ribonuclease from Escherichia coli ribosomes
    • Spahr, P. F. & Hollingworth, B. R. Purification and mechanism of action of ribonuclease from Escherichia coli ribosomes. J. Biol. Chem. 236, 823-831 (1961).
    • (1961) J. Biol. Chem. , vol.236 , pp. 823-831
    • Spahr, P.F.1    Hollingworth, B.R.2
  • 17
    • 0001618142 scopus 로고
    • Some observations on the latent ribonuclease of Escherichia coli
    • Neu, H. C. & Heppel, L. A. Some observations on the latent ribonuclease of Escherichia coli. Proc. Natl Acad. Sci. USA 51, 1267-1274 (1964).
    • (1964) Proc. Natl Acad. Sci. USA , vol.51 , pp. 1267-1274
    • Neu, H.C.1    Heppel, L.A.2
  • 18
    • 0015502048 scopus 로고
    • Association of ribonuclease i with ribosomes and their subunits
    • Datta, A. K. & Burma, D. P. Association of ribonuclease I with ribosomes and their subunits. J. Biol. Chem. 247, 6795-6801 (1972).
    • (1972) J. Biol. Chem. , vol.247 , pp. 6795-6801
    • Datta, A.K.1    Burma, D.P.2
  • 19
    • 0018633240 scopus 로고
    • Site of action of RNase I on the 50 S ribosome of Escherichia coli and the association of the enzyme with the partially degraded subunit
    • Raziuddin, Chatterji, D., Ghosh, S. & Burma, D. P. Site of action of RNase I on the 50 S ribosome of Escherichia coli and the association of the enzyme with the partially degraded subunit. J. Biol. Chem. 254, 10575-10578 (1979). (Pubitemid 10159351)
    • (1979) Journal of Biological Chemistry , vol.254 , Issue.21 , pp. 10575-10578
    • Raziuddin1    Chatterji, D.2    Ghosh, S.3    Burma, D.P.4
  • 20
    • 0014528911 scopus 로고
    • Induction by mercuric ion of extensive degradation of cellular ribonucleic acid in Escherichia coli
    • Beppu, T. & Arima, K. Induction by mercuric ion of extensive degradation of cellular ribonucleic acid in Escherichia coli. J. Bacteriol. 98, 888-897 (1969).
    • (1969) J. Bacteriol. , vol.98 , pp. 888-897
    • Beppu, T.1    Arima, K.2
  • 21
    • 0025171946 scopus 로고
    • Purification and characterization of Escherichia coli RNase I. Comparisons with RNase M
    • Meador, J. 3rd., Cannon, B., Cannistraro, V. J. & Kennell, D. Purification and characterization of Escherichia coli RNase I. Comparisons with RNase M. Eur. J. Biochem. 187, 549-553 (1990). (Pubitemid 20074917)
    • (1990) European Journal of Biochemistry , vol.187 , Issue.3 , pp. 549-553
    • Meador III, J.1    Cannon, B.2    Cannistraro, V.J.3    Kennell, D.4
  • 22
    • 67449128217 scopus 로고    scopus 로고
    • The ordered transcription of RNA domains is not essential for ribosome biogenesis in Escherichia coli
    • Kitahara, K. & Suzuki, T. The ordered transcription of RNA domains is not essential for ribosome biogenesis in Escherichia coli. Mol. Cell 34, 760-766 (2009).
    • (2009) Mol. Cell , vol.34 , pp. 760-766
    • Kitahara, K.1    Suzuki, T.2
  • 23
    • 23044445236 scopus 로고    scopus 로고
    • Features of ribosome-peptidyl-tRNA interactions essential for tryptophan induction of tna operon expression
    • DOI 10.1016/j.molcel.2005.06.013, PII S1097276505013924
    • Cruz-Vera, L. R., Rajagopal, S., Squires, C. & Yanofsky, C. Features of ribosome-peptidyl-tRNA interactions essential for tryptophan induction of tna operon expression. Mol. Cell 19, 333-343 (2005). (Pubitemid 41074889)
    • (2005) Molecular Cell , vol.19 , Issue.3 , pp. 333-343
    • Cruz-Vera, L.R.1    Rajagopal, S.2    Squires, C.3    Yanofsky, C.4
  • 24
    • 78651153358 scopus 로고
    • The release of ribonuclease into the medium when Escherichia coli cells are converted to speroplasts
    • Neu, H. C. & Heppel, L. A. The release of ribonuclease into the medium when Escherichia coli cells are converted to speroplasts. J. Biol. Chem. 239, 3893-3900 (1964).
    • (1964) J. Biol. Chem. , vol.239 , pp. 3893-3900
    • Neu, H.C.1    Heppel, L.A.2
  • 25
    • 0017761812 scopus 로고
    • Genetic mapping of the F plasmid gene that promotes degradation of stable ribonucleic acid in Escherichia coli
    • Ohnishi, Y., Iguma, H., Ono, T., Nagaishi, H. & Clark, A. J. Genetic mapping of the F plasmid gene that promotes degradation of stable ribonucleic acid in Escherichia coli. J. Bacteriol. 132, 784-789 (1977). (Pubitemid 8241646)
    • (1977) Journal of Bacteriology , vol.132 , Issue.3 , pp. 784-789
    • Ohnishi, Y.1    Iguma, H.2    Ono, T.3
  • 26
    • 0016439430 scopus 로고
    • Factor promotes turnover of stable RNA in Escherichia coli
    • Onishi, Y. F. factor promotes turnover of stable RNA in Escherichia coli. Science 187, 257-258 (1975).
    • (1975) Science , vol.187 , pp. 257-258
    • Onishi . Y, F.1
  • 28
    • 0034699518 scopus 로고    scopus 로고
    • Structure of the 30S ribosomal subunit
    • Wimberly, B. T. et al. Structure of the 30S ribosomal subunit. Nature 407, 327-339 (2000).
    • (2000) Nature , vol.407 , pp. 327-339
    • Wimberly, B.T.1
  • 30
    • 0013834728 scopus 로고
    • The inhibition of ribosomal ribonuclease by bacterial ribosomes
    • Wade, H. E. & Robinson, H. K. The inhibition of ribosomal ribonuclease by bacterial ribosomes. Biochem. J. 97, 747-753 (1965).
    • (1965) Biochem. J. , vol.97 , pp. 747-753
    • Wade, H.E.1    Robinson, H.K.2
  • 32
    • 34547619912 scopus 로고    scopus 로고
    • Functional genetic selection of Helix 66 in Escherichia coli 23S rRNA identified the eukaryotic-binding sequence for ribosomal protein L2
    • DOI 10.1093/nar/gkm356
    • Kitahara, K., Kajiura, A., Sato, N. S. & Suzuki, T. Functional genetic selection of Helix 66 in Escherichia coli 23S rRNA identified the eukaryotic-binding sequence for ribosomal protein L2. Nucleic Acids Res. 35, 4018-4029 (2007). (Pubitemid 47244623)
    • (2007) Nucleic Acids Research , vol.35 , Issue.12 , pp. 4018-4029
    • Kitahara, K.1    Kajiura, A.2    Sato, N.S.3    Suzuki, T.4
  • 33
    • 58849150431 scopus 로고    scopus 로고
    • The phage abortive infection system, ToxIN, functions as a protein-RNA toxin-antitoxin pair
    • Fineran, P. C. et al. The phage abortive infection system, ToxIN, functions as a protein-RNA toxin-antitoxin pair. Proc. Natl Acad. Sci. USA 106, 894-899 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 894-899
    • Fineran, P.C.1
  • 34
    • 0034814890 scopus 로고    scopus 로고
    • Cytoplasmic ribonuclease inhibitor
    • DOI 10.1016/S0076-6879(01)41180-3
    • Shapiro, R. Cytoplasmic ribonuclease inhibitor. Methods Enzymol. 341, 611-628 (2001). (Pubitemid 32928553)
    • (2001) Methods in Enzymology , vol.341 , pp. 611-628
    • Shapiro, R.1
  • 36
    • 2942571539 scopus 로고    scopus 로고
    • The comparative RNA web (CRW) site: An online database of comparative sequence and structure information for ribosomal, Intron, and other RNAs
    • Cannone, J. J. et al. The comparative RNA web (CRW) site: an online database of comparative sequence and structure information for ribosomal, Intron, and other RNAs. BMC Bioinformatics 3, 2 (2002).
    • (2002) BMC Bioinformatics , vol.3 , pp. 2
    • Cannone, J.J.1
  • 37
    • 58149200948 scopus 로고    scopus 로고
    • The Ribosomal Database Project: Improved alignments and new tools for rRNA analysis
    • Cole, J. R. et al. The Ribosomal Database Project: improved alignments and new tools for rRNA analysis. Nucleic Acids Res. 37, D141-D145 (2009).
    • (2009) Nucleic Acids Res. , vol.37
    • Cole, J.R.1
  • 38
  • 39
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • DOI 10.1006/abio.1987.9999
    • Chomczynski, P. & Sacchi, N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156-159 (1987). (Pubitemid 17064313)
    • (1987) Analytical Biochemistry , vol.162 , Issue.1 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2


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