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Volumn 42, Issue 4, 2014, Pages 2736-2749

Mapping Hfq-RNA interaction surfaces using tryptophan fluorescence quenching

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL RNA; MESSENGER RNA; PROTEIN HFQ; RNA BINDING PROTEIN; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 84895789299     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkt1171     Document Type: Article
Times cited : (65)

References (65)
  • 1
    • 0036714801 scopus 로고    scopus 로고
    • Predicted structure and phyletic distribution of the RNA-binding protein Hfq
    • Sun, X., Zhulin, I. and Wartell, R.M. (2002) Predicted structure and phyletic distribution of the RNA-binding protein Hfq. Nucleic Acids Res., 30, 3662-3671.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3662-3671
    • Sun, X.1    Zhulin, I.2    Wartell, R.M.3
  • 2
    • 1642565815 scopus 로고    scopus 로고
    • The bacterial Sm-like protein Hfq: A key player in RNA transactions
    • Valentin-Hansen, P., Eriksen, M. and Udesen, C. (2004) The bacterial Sm-like protein Hfq: a key player in RNA transactions. Mol. Microbiol., 51, 1525-1533.
    • (2004) Mol. Microbiol. , vol.51 , pp. 1525-1533
    • Valentin-Hansen, P.1    Eriksen, M.2    Udesen, C.3
  • 3
    • 0028243445 scopus 로고
    • Characterization of broadly pleiotropic phenotypes caused by an hfq insertion mutation in Escherichia coli K-12
    • Tsui, H.C., Leung, H.C. and Winkler, M.E. (1994) Characterization of broadly pleiotropic phenotypes caused by an hfq insertion mutation in Escherichia coli K-12. Mol. Microbiol., 13, 35-49.
    • (1994) Mol. Microbiol. , vol.13 , pp. 35-49
    • Tsui, H.C.1    Leung, H.C.2    Winkler, M.E.3
  • 4
    • 84875457350 scopus 로고    scopus 로고
    • Bacterial small RNA-based negative regulation: Hfq and its accomplices
    • De Lay, N., Schu, D.J. and Gottesman, S. (2013) Bacterial small RNA-based negative regulation: Hfq and its accomplices. J. Biol. Chem., 288, 7996-8003.
    • (2013) J. Biol. Chem. , vol.288 , pp. 7996-8003
    • De Lay, N.1    Schu, D.J.2    Gottesman, S.3
  • 5
    • 84879027709 scopus 로고    scopus 로고
    • Archaeal and eukaryotic homologs of Hfq: A structural and evolutionary perspective on Sm function
    • Mura, C., Randolph, P.S., Patterson, J. and Cozen, A.E. (2013) Archaeal and eukaryotic homologs of Hfq: a structural and evolutionary perspective on Sm function. RNA Biol., 10, 636-651.
    • (2013) RNA Biol. , vol.10 , pp. 636-651
    • Mura, C.1    Randolph, P.S.2    Patterson, J.3    Cozen, A.E.4
  • 6
    • 0014409656 scopus 로고
    • Factor fraction required for the synthesis of bacteriophage Qbeta-RNA
    • Franze de Fernandez, M.T., Eoyang, L. and August, J.T. (1968) Factor fraction required for the synthesis of bacteriophage Qbeta-RNA. Nature, 219, 588-590.
    • (1968) Nature , vol.219 , pp. 588-590
    • Franze De Fernandez, M.T.1    Eoyang, L.2    August, J.T.3
  • 7
    • 0015500282 scopus 로고
    • Bacterial proteins required for replication of phage Q ribonucleic acid. Pruification and properties of host factor i a ribonucleic acid-binding protein
    • Franze de Fernandez, M.T., Hayward, W.S. and August, J.T. (1972) Bacterial proteins required for replication of phage Q ribonucleic acid. Pruification and properties of host factor I, a ribonucleic acid-binding protein. J. Biol. Chem., 247, 824-831.
    • (1972) J. Biol. Chem. , vol.247 , pp. 824-831
    • Franze De Fernandez, M.T.1    Hayward, W.S.2    August, J.T.3
  • 8
    • 0035395606 scopus 로고    scopus 로고
    • Identification of novel small RNAs using comparative genomics and microarrays
    • Wassarman, K.M., Repoila, F., Rosenow, C., Storz, G. and Gottesman, S. (2001) Identification of novel small RNAs using comparative genomics and microarrays. Genes Dev., 15, 1637-1651.
    • (2001) Genes Dev. , vol.15 , pp. 1637-1651
    • Wassarman, K.M.1    Repoila, F.2    Rosenow, C.3    Storz, G.4    Gottesman, S.5
  • 11
    • 0016189410 scopus 로고
    • Nucleotide sequence specific interaction of host factor i with bacteriophage Q beta RNA
    • Hori, K. and Yanazaki, Y. (1974) Nucleotide sequence specific interaction of host factor I with bacteriophage Q beta RNA. FEBS Lett., 43, 20-22.
    • (1974) FEBS Lett. , vol.43 , pp. 20-22
    • Hori, K.1    Yanazaki, Y.2
  • 12
    • 0017227834 scopus 로고
    • Site-specific interaction of Qbeta host factor and ribosomal protein S1 with Qbeta and R17 bacteriophage RNAs
    • Senear, A.W. and Steitz, J.A. (1976) Site-specific interaction of Qbeta host factor and ribosomal protein S1 with Qbeta and R17 bacteriophage RNAs. J. Biol. Chem., 251, 1902-1912.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1902-1912
    • Senear, A.W.1    Steitz, J.A.2
  • 13
    • 0019254853 scopus 로고
    • Interaction of Escherichia coli host factor protein with oligoriboadenylates
    • de Haseth, P.L. and Uhlenbeck, O.C. (1980) Interaction of Escherichia coli host factor protein with oligoriboadenylates. Biochemistry, 19, 6138-6146.
    • (1980) Biochemistry , vol.19 , pp. 6138-6146
    • De Haseth, P.L.1    Uhlenbeck, O.C.2
  • 14
    • 0019256070 scopus 로고
    • Interaction of Escherichia coli host factor protein with Q beta ribonucleic acid
    • de Haseth, P.L. and Uhlenbeck, O.C. (1980) Interaction of Escherichia coli host factor protein with Q beta ribonucleic acid. Biochemistry, 19, 6146-6151.
    • (1980) Biochemistry , vol.19 , pp. 6146-6151
    • De Haseth, P.L.1    Uhlenbeck, O.C.2
  • 15
    • 0032531904 scopus 로고    scopus 로고
    • The OxyS regulatory RNA represses rpoS translation and binds the Hfq (HF-I) protein
    • Zhang, A., Altuvia, S., Tiwari, A., Argaman, L., Hengge-Aronis, R. and Storz, G. (1998) The OxyS regulatory RNA represses rpoS translation and binds the Hfq (HF-I) protein. EMBO J., 17, 6061-6068.
    • (1998) EMBO J. , vol.17 , pp. 6061-6068
    • Zhang, A.1    Altuvia, S.2    Tiwari, A.3    Argaman, L.4    Hengge-Aronis, R.5    Storz, G.6
  • 16
    • 84859915108 scopus 로고    scopus 로고
    • Multiple factors dictate target selection by Hfq-binding small RNAs
    • Beisel, C.L., Updegrove, T.B., Janson, B.J. and Storz, G. (2012) Multiple factors dictate target selection by Hfq-binding small RNAs. EMBO J., 31, 1961-1974.
    • (2012) EMBO J. , vol.31 , pp. 1961-1974
    • Beisel, C.L.1    Updegrove, T.B.2    Janson, B.J.3    Storz, G.4
  • 17
    • 79960433506 scopus 로고    scopus 로고
    • Hfq and its constellation of RNA
    • Vogel, J. and Luisi, B.F. (2011) Hfq and its constellation of RNA. Nat. Rev. Microbiol., 9, 578-589.
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 578-589
    • Vogel, J.1    Luisi, B.F.2
  • 18
    • 3142564584 scopus 로고    scopus 로고
    • The small RNA chaperone Hfq and multiple small RNAs control quorum sensing in Vibrio harveyi and Vibrio cholerae
    • Lenz, D.H., Mok, K.C., Lilley, B.N., Kulkarni, R.V., Wingreen, N.S. and Bassler, B.L. (2004) The small RNA chaperone Hfq and multiple small RNAs control quorum sensing in Vibrio harveyi and Vibrio cholerae. Cell, 118, 69-82.
    • (2004) Cell , vol.118 , pp. 69-82
    • Lenz, D.H.1    Mok, K.C.2    Lilley, B.N.3    Kulkarni, R.V.4    Wingreen, N.S.5    Bassler, B.L.6
  • 20
    • 33845713571 scopus 로고    scopus 로고
    • The RNA chaperone Hfq is essential for the virulence of Salmonella typhimurium
    • Sittka, A., Pfeiffer, V., Tedin, K. and Vogel, J. (2007) The RNA chaperone Hfq is essential for the virulence of Salmonella typhimurium. Mol. Microbiol., 63, 193-217.
    • (2007) Mol. Microbiol. , vol.63 , pp. 193-217
    • Sittka, A.1    Pfeiffer, V.2    Tedin, K.3    Vogel, J.4
  • 21
    • 75249100904 scopus 로고    scopus 로고
    • The role of Hfq in bacterial pathogens
    • Chao, Y. and Vogel, J. (2010) The role of Hfq in bacterial pathogens. Curr. Opin. Microbiol., 13, 24-33.
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 24-33
    • Chao, Y.1    Vogel, J.2
  • 22
    • 0029889596 scopus 로고    scopus 로고
    • Efficient translation of the RpoS sigma factor in Salmonella typhimurium requires host factor I, an RNA-binding protein encoded by the hfq gene
    • Brown, L. and Elliott, T. (1996) Efficient translation of the RpoS sigma factor in Salmonella typhimurium requires host factor I, an RNA-binding protein encoded by the hfq gene. J. Bacteriol., 178, 3763-3770.
    • (1996) J. Bacteriol. , vol.178 , pp. 3763-3770
    • Brown, L.1    Elliott, T.2
  • 24
    • 46449132381 scopus 로고    scopus 로고
    • Impact of the RNA chaperone Hfq on the fitness and virulence potential of uropathogenic Escherichia coli
    • Kulesus, R.R., Diaz-Perez, K., Slechta, E.S., Eto, D.S. and Mulvey, M.A. (2008) Impact of the RNA chaperone Hfq on the fitness and virulence potential of uropathogenic Escherichia coli. Infect. Immun., 76, 3019-3026.
    • (2008) Infect. Immun. , vol.76 , pp. 3019-3026
    • Kulesus, R.R.1    Diaz-Perez, K.2    Slechta, E.S.3    Eto, D.S.4    Mulvey, M.A.5
  • 25
    • 3142550776 scopus 로고    scopus 로고
    • Hfq is essential for Vibrio cholerae virulence and downregulates sigma expression
    • Ding, Y., Davis, B.M. and Waldor, M.K. (2004) Hfq is essential for Vibrio cholerae virulence and downregulates sigma expression. Mol. Microbiol., 53, 345-354.
    • (2004) Mol. Microbiol. , vol.53 , pp. 345-354
    • Ding, Y.1    Davis, B.M.2    Waldor, M.K.3
  • 27
    • 84875800892 scopus 로고    scopus 로고
    • Impact of Hfq on the intrinsic drug resistance of Salmonella enterica serovar typhimurium
    • Hayashi-Nishino, M., Fukushima, A. and Nishino, K. (2012) Impact of Hfq on the intrinsic drug resistance of Salmonella enterica serovar typhimurium. Front. Microbiol., 3, 205.
    • (2012) Front. Microbiol. , vol.3 , pp. 205
    • Hayashi-Nishino, M.1    Fukushima, A.2    Nishino, K.3
  • 28
    • 0030711638 scopus 로고    scopus 로고
    • Negative regulation of mutS and mutH repair gene expression by the Hfq and RpoS global regulators of Escherichia coli K-12
    • Tsui, H.C., Feng, G. and Winkler, M.E. (1997) Negative regulation of mutS and mutH repair gene expression by the Hfq and RpoS global regulators of Escherichia coli K-12, J. Bacteriol., 179, 7476-7487.
    • (1997) J. Bacteriol. , vol.179 , pp. 7476-7487
    • Tsui, H.C.1    Feng, G.2    Winkler, M.E.3
  • 29
    • 21844476794 scopus 로고    scopus 로고
    • Translational autocontrol of the Escherichia coli hfq RNA chaperone gene
    • Vecerek, B., Moll, I. and Blasi, U. (2005) Translational autocontrol of the Escherichia coli hfq RNA chaperone gene. RNA, 11, 976-984.
    • (2005) RNA , vol.11 , pp. 976-984
    • Vecerek, B.1    Moll, I.2    Blasi, U.3
  • 30
    • 80054716344 scopus 로고    scopus 로고
    • Evidences of autoregulation of Hfq expression in Sinorhizobium meliloti strain 2011
    • Sobrero, P. and Valverde, C. (2011) Evidences of autoregulation of Hfq expression in Sinorhizobium meliloti strain 2011. Arch. Microbiol., 193, 629-639.
    • (2011) Arch. Microbiol. , vol.193 , pp. 629-639
    • Sobrero, P.1    Valverde, C.2
  • 33
    • 0242380623 scopus 로고    scopus 로고
    • Sm-like proteins in Eubacteria: The crystal structure of the Hfq protein from Escherichia coli
    • Sauter, C., Basquin, J. and Suck, D. (2003) Sm-like proteins in Eubacteria: the crystal structure of the Hfq protein from Escherichia coli. Nucleic Acids Res., 31, 4091-4098.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 4091-4098
    • Sauter, C.1    Basquin, J.2    Suck, D.3
  • 35
    • 0036645689 scopus 로고    scopus 로고
    • Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: A bacterial Sm-like protein
    • Schumacher, M.A., Pearson, R.F., Moller, T., Valentin-Hansen, P. and Brennan, R.G. (2002) Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: a bacterial Sm-like protein. EMBO J., 21, 3546-3556.
    • (2002) EMBO J. , vol.21 , pp. 3546-3556
    • Schumacher, M.A.1    Pearson, R.F.2    Moller, T.3    Valentin-Hansen, P.4    Brennan, R.G.5
  • 36
    • 80053643342 scopus 로고    scopus 로고
    • Cooperation of Escherichia coli Hfq hexamers in DsrA binding
    • Wang, W., Wang, L., Zou, Y., Zhang, J., Gong, Q., Wu, J. and Shi, Y. (2011) Cooperation of Escherichia coli Hfq hexamers in DsrA binding. Genes Dev., 25, 2106-2117.
    • (2011) Genes Dev. , vol.25 , pp. 2106-2117
    • Wang, W.1    Wang, L.2    Zou, Y.3    Zhang, J.4    Gong, Q.5    Wu, J.6    Shi, Y.7
  • 37
    • 84878819251 scopus 로고    scopus 로고
    • Hfq-bridged ternary complex is important for translation activation of rpoS by DsrA
    • Wang, W., Wang, L., Wu, J., Gong, Q. and Shi, Y. (2013) Hfq-bridged ternary complex is important for translation activation of rpoS by DsrA. Nucleic Acids Res., 41, 5938-5948.
    • (2013) Nucleic Acids Res. , vol.41 , pp. 5938-5948
    • Wang, W.1    Wang, L.2    Wu, J.3    Gong, Q.4    Shi, Y.5
  • 38
    • 80051962605 scopus 로고    scopus 로고
    • Structural basis for RNA 3-end recognition by Hfq
    • Sauer, E. and Weichenrieder, O. (2011) Structural basis for RNA 3-end recognition by Hfq. Proc. Natl Acad. Sci. USA, 108, 13065-13070.
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 13065-13070
    • Sauer, E.1    Weichenrieder, O.2
  • 39
    • 72049095718 scopus 로고    scopus 로고
    • Structure of Escherichia coli Hfq bound to polyriboadenylate RNA
    • Link, T.M., Valentin-Hansen, P. and Brennan, R.G. (2009) Structure of Escherichia coli Hfq bound to polyriboadenylate RNA. Proc. Natl Acad. Sci. USA, 106, 19292-19297.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 19292-19297
    • Link, T.M.1    Valentin-Hansen, P.2    Brennan, R.G.3
  • 40
    • 84857839806 scopus 로고    scopus 로고
    • Crystal structure of Hfq from Bacillus subtilis in complex with SELEX-derived RNA aptamer: Insight into RNA-binding properties of bacterial Hfq
    • Someya, T., Baba, S., Fujimoto, M., Kawai, G., Kumasaka, T. and Nakamura, K. (2012) Crystal structure of Hfq from Bacillus subtilis in complex with SELEX-derived RNA aptamer: insight into RNA-binding properties of bacterial Hfq. Nucleic Acids Res., 40, 1856-1867.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 1856-1867
    • Someya, T.1    Baba, S.2    Fujimoto, M.3    Kawai, G.4    Kumasaka, T.5    Nakamura, K.6
  • 42
    • 77958563236 scopus 로고    scopus 로고
    • An upstream Hfq binding site in the fhlA mRNA leader region facilitates the OxyS-fhlA interaction
    • Salim, N.N. and Feig, A.L. (2010) An upstream Hfq binding site in the fhlA mRNA leader region facilitates the OxyS-fhlA interaction. PLoS One, 5, e13028.
    • (2010) PLoS One , vol.5
    • Salim, N.N.1    Feig, A.L.2
  • 43
    • 84870503889 scopus 로고    scopus 로고
    • Requirement of upstream Hfq-binding (ARN)x elements in glmS and the Hfq C-terminal region for GlmS upregulation by sRNAs GlmZ and GlmY
    • Salim, N.N., Faner, M.A., Philip, J.A. and Feig, A.L. (2012) Requirement of upstream Hfq-binding (ARN)x elements in glmS and the Hfq C-terminal region for GlmS upregulation by sRNAs GlmZ and GlmY. Nucleic Acids Res., 40, 8021-8032.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 8021-8032
    • Salim, N.N.1    Faner, M.A.2    Philip, J.A.3    Feig, A.L.4
  • 44
    • 50649097486 scopus 로고    scopus 로고
    • The rpoS mRNA leader recruits Hfq to facilitate annealing with DsrA sRNA
    • Soper, T.J. and Woodson, S.A. (2008) The rpoS mRNA leader recruits Hfq to facilitate annealing with DsrA sRNA. RNA, 14, 1907-1917.
    • (2008) RNA , vol.14 , pp. 1907-1917
    • Soper, T.J.1    Woodson, S.A.2
  • 46
    • 54849408366 scopus 로고    scopus 로고
    • Effect of Hfq on RprA-RpoS mRNA pairing: Hfq-RNA binding and the influence of the 5 RpoS mRNA leader region
    • Updegrove, T., Wilf, N., Sun, X. and Wartell, R.M. (2008) Effect of Hfq on RprA-RpoS mRNA pairing: Hfq-RNA binding and the influence of the 5 RpoS mRNA leader region. Biochemistry, 47, 11184-11195.
    • (2008) Biochemistry , vol.47 , pp. 11184-11195
    • Updegrove, T.1    Wilf, N.2    Sun, X.3    Wartell, R.M.4
  • 47
    • 77951995663 scopus 로고    scopus 로고
    • Expression, crystallization and preliminary crystallographic analysis of RNA-binding protein Hfq (YmaH) from Bacillus subtilis in complex with an RNA aptamer, Acta Crystallogr
    • Baba, S., Someya, T., Kawai, G., Nakamura, K. and Kumasaka, T. (2010) Expression, crystallization and preliminary crystallographic analysis of RNA-binding protein Hfq (YmaH) from Bacillus subtilis in complex with an RNA aptamer, Acta Crystallogr. Sect F. Struct. Biol. Cryst. Commun., 66, 563-566.
    • (2010) Sect F. Struct. Biol. Cryst. Commun. , vol.66 , pp. 563-566
    • Baba, S.1    Someya, T.2    Kawai, G.3    Nakamura, K.4    Kumasaka, T.5
  • 48
    • 79958095433 scopus 로고    scopus 로고
    • Despite similar binding to the Hfq protein regulatory RNAs widely differ in their competition performance
    • Olejniczak, M. (2011) Despite similar binding to the Hfq protein regulatory RNAs widely differ in their competition performance. Biochemistry, 50, 4427-4440.
    • (2011) Biochemistry , vol.50 , pp. 4427-4440
    • Olejniczak, M.1
  • 51
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Macromolecular Crystallography, Pt A, 276, 307-326.
    • (1997) Macromolecular Crystallography, Pt A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 55
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel, E. and Henrick, K. (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D. Biol. Crystallogr., 60, 2256-2268.
    • (2004) Acta Crystallogr. D. Biol. Crystallogr. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 56
    • 0029887308 scopus 로고    scopus 로고
    • Fluorescence polarization analysis of protein-DNA and protein-protein interactions
    • Lundblad, J.R., Laurance, M. and Goodman, R.H. (1996) Fluorescence polarization analysis of protein-DNA and protein-protein interactions. Mol. Endocrinol., 10, 607-612.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 607-612
    • Lundblad, J.R.1    Laurance, M.2    Goodman, R.H.3
  • 57
    • 84883809477 scopus 로고    scopus 로고
    • Mutations in interaction surfaces differentially impact E. Coli Hfq association with small RNAs and their mRNA targets
    • Zhang, A., Schu, D.J., Tjaden, B.C., Storz, G. and Gottesman, S. (2013) Mutations in interaction surfaces differentially impact E. coli Hfq association with small RNAs and their mRNA targets. J. Mol. Biol., 425, 3678-3697.
    • (2013) J. Mol. Biol. , vol.425 , pp. 3678-3697
    • Zhang, A.1    Schu, D.J.2    Tjaden, B.C.3    Storz, G.4    Gottesman, S.5
  • 59
    • 84862232515 scopus 로고    scopus 로고
    • Small RNA binding to the lateral surface of Hfq hexamers and structural rearrangements upon mRNA target recognition
    • Sauer, E., Schmidt, S. and Weichenrieder, O. (2012) Small RNA binding to the lateral surface of Hfq hexamers and structural rearrangements upon mRNA target recognition. Proc. Natl Acad. Sci. USA, 109, 9396-9401.
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 9396-9401
    • Sauer, E.1    Schmidt, S.2    Weichenrieder, O.3
  • 60
    • 84883478358 scopus 로고    scopus 로고
    • Conserved arginines on the rim of Hfq catalyze base pair formation and exchange
    • Panja, S., Schu, D.J. and Woodson, S.A. (2013) Conserved arginines on the rim of Hfq catalyze base pair formation and exchange. Nucleic Acids Res., 41, 7536-7546.
    • (2013) Nucleic Acids Res. , vol.41 , pp. 7536-7546
    • Panja, S.1    Schu, D.J.2    Woodson, S.A.3
  • 63
    • 0032716841 scopus 로고    scopus 로고
    • Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid
    • Ali Azam, T., Iwata, A., Nishimura, A., Ueda, S. and Ishihama, A. (1999) Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid. J. Bacteriol., 181, 6361-6370.
    • (1999) J. Bacteriol. , vol.181 , pp. 6361-6370
    • Ali Azam, T.1    Iwata, A.2    Nishimura, A.3    Ueda, S.4    Ishihama, A.5
  • 64
    • 84860000113 scopus 로고    scopus 로고
    • The functional Hfq-binding module of bacterial sRNAs consists of a double or single hairpin preceded by a U-rich sequence and followed by a 3 poly(U) tail
    • Ishikawa, H., Otaka, H., Maki, K., Morita, T. and Aiba, H. (2012) The functional Hfq-binding module of bacterial sRNAs consists of a double or single hairpin preceded by a U-rich sequence and followed by a 3 poly(U) tail. RNA, 18, 1062-1074.
    • (2012) RNA , vol.18 , pp. 1062-1074
    • Ishikawa, H.1    Otaka, H.2    Maki, K.3    Morita, T.4    Aiba, H.5
  • 65
    • 2442645227 scopus 로고    scopus 로고
    • The RNA-binding protein Hfq of Listeria monocytogenes: Role in stress tolerance and virulence
    • Christiansen, J.K., Larsen, M.H., Ingmer, H., Sogaard-Andersen, L. and Kallipolitis, B.H. (2004) The RNA-binding protein Hfq of Listeria monocytogenes: role in stress tolerance and virulence. J. Bacteriol., 186, 3355-3362.
    • (2004) J. Bacteriol. , vol.186 , pp. 3355-3362
    • Christiansen, J.K.1    Larsen, M.H.2    Ingmer, H.3    Sogaard-Andersen, L.4    Kallipolitis, B.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.