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Volumn 96, Issue 3, 2015, Pages 633-650

Hfq binds directly to the ribosome-binding site of IS10 transposase mRNA to inhibit translation

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; COMPLEMENTARY RNA; IS10 TRANSPOSASE; MESSENGER RNA; RNA BINDING PROTEIN; RNA BINDING PROTEIN HFQ; TN10 TRANSPOSASE; TRANSPOSASE; UNCLASSIFIED DRUG; ESCHERICHIA COLI PROTEIN; HFQ PROTEIN, E COLI; HOST FACTOR 1; PROTEIN BINDING;

EID: 84928433960     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12961     Document Type: Article
Times cited : (50)

References (66)
  • 1
    • 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
  • 2
    • 62849101179 scopus 로고    scopus 로고
    • Global systems-level analysis of Hfq and SmpB deletion mutants in Salmonella: implications for virulence and global protein translation
    • Ansong, C., Yoon, H., Porwollik, S., Mottaz-Brewer, H., Petritis, B.O., Jaitly, N., etal. (2009) Global systems-level analysis of Hfq and SmpB deletion mutants in Salmonella: implications for virulence and global protein translation. PLoS ONE 4: e4809.
    • (2009) PLoS ONE , vol.4 , pp. e4809
    • Ansong, C.1    Yoon, H.2    Porwollik, S.3    Mottaz-Brewer, H.4    Petritis, B.O.5    Jaitly, N.6
  • 3
    • 84858692356 scopus 로고    scopus 로고
    • RelA protein stimulates the activity of RyhB small RNA by acting on RNA-binding protein Hfq
    • Argaman, L., Elgrably-Weiss, M., Hershko, T., Vogel, J., and Altuvia, S. (2012) RelA protein stimulates the activity of RyhB small RNA by acting on RNA-binding protein Hfq. Proc Natl Acad Sci USA 109: 4621-4626.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 4621-4626
    • Argaman, L.1    Elgrably-Weiss, M.2    Hershko, T.3    Vogel, J.4    Altuvia, S.5
  • 4
    • 0032731196 scopus 로고    scopus 로고
    • Twelve species of the nucleoid-associated protein from Escherichia coli
    • Azam, T.A., and Ishihama, A. (1999) Twelve species of the nucleoid-associated protein from Escherichia coli. J Biol Chem 274: 33105-33113.
    • (1999) J Biol Chem , vol.274 , pp. 33105-33113
    • Azam, T.A.1    Ishihama, A.2
  • 5
    • 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
  • 6
    • 84906350474 scopus 로고    scopus 로고
    • Revisiting the coding potential of the E. coli genome through Hfq co-immunoprecipitation
    • Bilusic, I., Popitsch, N., Rescheneder, P., Schroeder, R., and Lybecker, M. (2014) Revisiting the coding potential of the E. coli genome through Hfq co-immunoprecipitation. RNA Biol 11: 641-654.
    • (2014) RNA Biol , vol.11 , pp. 641-654
    • Bilusic, I.1    Popitsch, N.2    Rescheneder, P.3    Schroeder, R.4    Lybecker, M.5
  • 7
    • 0031015418 scopus 로고    scopus 로고
    • Mutations that increase expression of the rpoS gene and decrease its dependence on hfq function in Salmonella Typhimurium
    • Brown, L., and Elliott, T. (1997) Mutations that increase expression of the rpoS gene and decrease its dependence on hfq function in Salmonella Typhimurium. J Bacteriol 179: 656-662.
    • (1997) J Bacteriol , vol.179 , pp. 656-662
    • Brown, L.1    Elliott, T.2
  • 8
    • 0024213092 scopus 로고
    • Analysis of the promoters and transcripts involved in IS10 anti-sense RNA control
    • Case, C.C., Roels, S.M., Gonzalez, J.E., Simons, E.L., and Simons, R.W. (1988) Analysis of the promoters and transcripts involved in IS10 anti-sense RNA control. Gene 72: 219-236.
    • (1988) Gene , vol.72 , pp. 219-236
    • Case, C.C.1    Roels, S.M.2    Gonzalez, J.E.3    Simons, E.L.4    Simons, R.W.5
  • 9
    • 0024802862 scopus 로고
    • The unusual stability of the IS10 anti-sense RNA is critical for its function and is determined by the structure of its stem-domain
    • Case, C.C., Roels, S.M., Jensen, P.D., Lee, J., Kleckner, N., and Simons, R.W. (1989) The unusual stability of the IS10 anti-sense RNA is critical for its function and is determined by the structure of its stem-domain. EMBO J 8: 4297-4305.
    • (1989) EMBO J , vol.8 , pp. 4297-4305
    • Case, C.C.1    Roels, S.M.2    Jensen, P.D.3    Lee, J.4    Kleckner, N.5    Simons, R.W.6
  • 10
    • 0025278320 scopus 로고
    • The IS10 transposase mRNA is destabilized during antisense RNA control
    • Case, C.C., Simons, E.L., and Simons, R.W. (1990) The IS10 transposase mRNA is destabilized during antisense RNA control. EMBO J 9: 1259-1266.
    • (1990) EMBO J , vol.9 , pp. 1259-1266
    • Case, C.C.1    Simons, E.L.2    Simons, R.W.3
  • 12
    • 84867577054 scopus 로고    scopus 로고
    • An atlas of Hfq-bound transcripts reveals 3′ UTRs as a genomic reservoir of regulatory small RNAs.
    • Chao, Y., Papenfort, K., Reinhardt, R., Sharma, C.M., and Vogel, J., (2012) An atlas of Hfq-bound transcripts reveals 3′ UTRs as a genomic reservoir of regulatory small RNAs, p. 4005-4019.
    • (2012) , pp. 4005-4019
    • Chao, Y.1    Papenfort, K.2    Reinhardt, R.3    Sharma, C.M.4    Vogel, J.5
  • 13
    • 84859365433 scopus 로고    scopus 로고
    • Noncanonical repression of translation initiation through small RNA recruitment of the RNA chaperone Hfq
    • Desnoyers, G., and Massé, E. (2012) Noncanonical repression of translation initiation through small RNA recruitment of the RNA chaperone Hfq. Genes Dev 26: 726-739.
    • (2012) Genes Dev , vol.26 , pp. 726-739
    • Desnoyers, G.1    Massé, E.2
  • 14
    • 65649150695 scopus 로고    scopus 로고
    • Ribosomal initiation complexes probed by toeprinting and effect of trans-acting translational regulators in bacteria
    • Fechter, P., Chevalier, C., Yusupova, G., Yusupov, M., Romby, P., and Marzi, S. (2009) Ribosomal initiation complexes probed by toeprinting and effect of trans-acting translational regulators in bacteria. Methods Mol Biol 540: 247-263.
    • (2009) Methods Mol Biol , vol.540 , pp. 247-263
    • Fechter, P.1    Chevalier, C.2    Yusupova, G.3    Yusupov, M.4    Romby, P.5    Marzi, S.6
  • 16
    • 69749123311 scopus 로고    scopus 로고
    • Caught at its own game: regulatory small RNA inactivated by an inducible transcript mimicking its target
    • Figueroa-Bossi, N., Valentini, M., Malleret, L., and Bossi, L. (2009) Caught at its own game: regulatory small RNA inactivated by an inducible transcript mimicking its target. Genes Dev 23: 2004-2015.
    • (2009) Genes Dev , vol.23 , pp. 2004-2015
    • Figueroa-Bossi, N.1    Valentini, M.2    Malleret, L.3    Bossi, L.4
  • 18
    • 1542320707 scopus 로고    scopus 로고
    • Hfq, a new chaperoning role: binding to messenger RNA determines access for small RNA regulator
    • Geissmann, T.A., and Touati, D. (2004) Hfq, a new chaperoning role: binding to messenger RNA determines access for small RNA regulator. EMBO J 23: 396-405.
    • (2004) EMBO J , vol.23 , pp. 396-405
    • Geissmann, T.A.1    Touati, D.2
  • 19
    • 33947361601 scopus 로고    scopus 로고
    • Hfq modulates the σE-mediated envelope stress response and the σ32-mediated cytoplasmic stress response in escherichia coli
    • Guisbert, E., V., Rhodius, A., Ahuja, N., Witkin, E., and Gross, C.A. (2007) Hfq modulates the σE-mediated envelope stress response and the σ32-mediated cytoplasmic stress response in escherichia coli. J Bacteriol 189: 1963-1973.
    • (2007) J Bacteriol , vol.189 , pp. 1963-1973
    • Guisbert, V.E.1    Rhodius, A.2    Ahuja, N.3    Witkin, E.4    Gross, C.A.5
  • 20
    • 84904362234 scopus 로고    scopus 로고
    • MicL, a new σE-dependent sRNA, combats envelope stress by repressing synthesis of Lpp, the major outer membrane lipoprotein
    • Guo, M.S., Updegrove, T.B., Gogol, E.B., Shabalina, S.A., Gross, C.A., and Storz, G. (2014) MicL, a new σE-dependent sRNA, combats envelope stress by repressing synthesis of Lpp, the major outer membrane lipoprotein. Genes Dev 28: 1620-1634.
    • (2014) Genes Dev , vol.28 , pp. 1620-1634
    • Guo, M.S.1    Updegrove, T.B.2    Gogol, E.B.3    Shabalina, S.A.4    Gross, C.A.5    Storz, G.6
  • 21
    • 0342576826 scopus 로고
    • DNA sequence organization of IS10-Right of TN10 and comparison with IS10-Left
    • Halling, S.M., Simons, R.W., Way, J.C., Walsh, R.B., and Kleckner, N. (1982) DNA sequence organization of IS10-Right of TN10 and comparison with IS10-Left. Proc Natl Acad Sci USA 79: 2608-2612.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 2608-2612
    • Halling, S.M.1    Simons, R.W.2    Way, J.C.3    Walsh, R.B.4    Kleckner, N.5
  • 22
    • 79958095005 scopus 로고    scopus 로고
    • Rapid binding and release of Hfq from ternary complexes during RNA annealing
    • Hopkins, J.F., Panja, S., and Woodson, S.A. (2011) Rapid binding and release of Hfq from ternary complexes during RNA annealing. Nucleic Acids Res 39: 5193-5202.
    • (2011) Nucleic Acids Res , vol.39 , pp. 5193-5202
    • Hopkins, J.F.1    Panja, S.2    Woodson, S.A.3
  • 23
    • 79551650983 scopus 로고    scopus 로고
    • Disruption of small RNA signaling caused by competition for Hfq
    • Hussein, R., and Lim, H.N. (2011) Disruption of small RNA signaling caused by competition for Hfq. PNAS 108: 1110-1115.
    • (2011) PNAS , vol.108 , pp. 1110-1115
    • Hussein, R.1    Lim, H.N.2
  • 24
    • 79958146262 scopus 로고    scopus 로고
    • Dynamic competition of DsrA and rpoS fragments for the proximal binding site of Hfq as a means for efficient annealing
    • Hwang, W., Arluison, V., and Hohng, S. (2011) Dynamic competition of DsrA and rpoS fragments for the proximal binding site of Hfq as a means for efficient annealing. Nucleic Acids Res 39: 5131-5139.
    • (2011) Nucleic Acids Res , vol.39 , pp. 5131-5139
    • Hwang, W.1    Arluison, V.2    Hohng, S.3
  • 25
    • 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
  • 26
    • 0028914927 scopus 로고
    • IS10 antisense control in vivo is affected by mutations throughout the region of complementarity between the interacting RNAs
    • Jain, C. (1995) IS10 antisense control in vivo is affected by mutations throughout the region of complementarity between the interacting RNAs. J Mol Biol 246: 585-594.
    • (1995) J Mol Biol , vol.246 , pp. 585-594
    • Jain, C.1
  • 27
    • 0027201842 scopus 로고
    • Preferential cis action of IS 10 transposase depends upon its mode of synthesis
    • Jain, C., and Kleckner, N. (1993) Preferential cis action of IS 10 transposase depends upon its mode of synthesis. Mol Microbiol 9: 249-260.
    • (1993) Mol Microbiol , vol.9 , pp. 249-260
    • Jain, C.1    Kleckner, N.2
  • 28
    • 0028107450 scopus 로고
    • Regulation of the Escherichia coli hfq gene encoding the host factor for phage Q beta
    • Kajitani, M., Kato, A., Wada, A., Inokuchi, Y., and Ishihama, A. (1994) Regulation of the Escherichia coli hfq gene encoding the host factor for phage Q beta. J Bacteriol 176: 531-534.
    • (1994) J Bacteriol , vol.176 , pp. 531-534
    • Kajitani, M.1    Kato, A.2    Wada, A.3    Inokuchi, Y.4    Ishihama, A.5
  • 29
    • 0025265019 scopus 로고
    • Regulating tn10 and is10 transposition
    • Kleckner, N. (1990) Regulating tn10 and is10 transposition. Genetics 124: 449-454.
    • (1990) Genetics , vol.124 , pp. 449-454
    • Kleckner, N.1
  • 30
    • 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
  • 31
    • 0025305877 scopus 로고
    • The IS10 antisense RNA blocks ribosome binding at the transposase translation initiation site
    • Ma, C., and Simons, R.W. (1990) The IS10 antisense RNA blocks ribosome binding at the transposase translation initiation site. EMBO J 9: 1267-1274.
    • (1990) EMBO J , vol.9 , pp. 1267-1274
    • Ma, C.1    Simons, R.W.2
  • 32
    • 84922634643 scopus 로고    scopus 로고
    • The structure of bacterial regulatory RNAs determines their performance in competition for the chaperone protein Hfq
    • Małecka, E.M., Stróz˙ecka, J., Sobańska, D., and Olejniczak, M. (2015) The structure of bacterial regulatory RNAs determines their performance in competition for the chaperone protein Hfq. Biochemistry 54: 1157-1170.
    • (2015) Biochemistry , vol.54 , pp. 1157-1170
    • Małecka, E.M.1    Strózecka, J.2    Sobańska, D.3    Olejniczak, M.4
  • 33
    • 77956879952 scopus 로고    scopus 로고
    • Integrating anaerobic/aerobic sensing and the general stress response through the ArcZ small RNA
    • Mandin, P., and Gottesman, S. (2010) Integrating anaerobic/aerobic sensing and the general stress response through the ArcZ small RNA. EMBO J 29: 3094-3107.
    • (2010) EMBO J , vol.29 , pp. 3094-3107
    • Mandin, P.1    Gottesman, S.2
  • 35
    • 83355177980 scopus 로고    scopus 로고
    • Competition among Hfq-binding small RNAs in Escherichia coli
    • Moon, K., and Gottesman, S. (2011) Competition among Hfq-binding small RNAs in Escherichia coli. Mol Microbiol 82: 1545-1562.
    • (2011) Mol Microbiol , vol.82 , pp. 1545-1562
    • Moon, K.1    Gottesman, S.2
  • 36
    • 0020504897 scopus 로고
    • Tn10 transposase acts preferentially on nearby transposon ends in vivo
    • Morisato, D., Way, J.C., Kim, H.-J., and Kleckner, N. (1983) Tn10 transposase acts preferentially on nearby transposon ends in vivo. Cell 32: 799-807.
    • (1983) Cell , vol.32 , pp. 799-807
    • Morisato, D.1    Way, J.C.2    Kim, H.-J.3    Kleckner, N.4
  • 38
    • 84866949691 scopus 로고    scopus 로고
    • Hfq proximity and orientation controls RNA annealing
    • Panja, S., and Woodson, S.A. (2012) Hfq proximity and orientation controls RNA annealing. Nucleic Acids Res 40: 8690-8697.
    • (2012) Nucleic Acids Res , vol.40 , pp. 8690-8697
    • Panja, S.1    Woodson, S.A.2
  • 39
    • 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
  • 40
    • 84915760848 scopus 로고    scopus 로고
    • Small RNA functions in carbon metabolism and virulence of enteric pathogens
    • Papenfort, K., and Vogel, J. (2014) Small RNA functions in carbon metabolism and virulence of enteric pathogens. Front Cell Infect Microbiol 4. doi:10.3389/fcimb.2014.00091.
    • (2014) Front Cell Infect Microbiol , vol.4
    • Papenfort, K.1    Vogel, J.2
  • 41
    • 70350176597 scopus 로고    scopus 로고
    • Specific and pleiotropic patterns of mRNA regulation by ArcZ, a conserved, Hfq-dependent small RNA
    • Papenfort, K., Said, N., Welsink, T., Lucchini, S., Hinton, J.C.D., and Vogel, J. (2009) Specific and pleiotropic patterns of mRNA regulation by ArcZ, a conserved, Hfq-dependent small RNA. Mol Microbiol 74: 139-158.
    • (2009) Mol Microbiol , vol.74 , pp. 139-158
    • Papenfort, K.1    Said, N.2    Welsink, T.3    Lucchini, S.4    Hinton, J.C.D.5    Vogel, J.6
  • 42
    • 84891827418 scopus 로고    scopus 로고
    • Positional effects of AAN motifs in rpoS regulation by sRNAs and Hfq
    • Peng, Y., Soper, T.J., and Woodson, S.A. (2014) Positional effects of AAN motifs in rpoS regulation by sRNAs and Hfq. J Mol Biol 426: 275-285.
    • (2014) J Mol Biol , vol.426 , pp. 275-285
    • Peng, Y.1    Soper, T.J.2    Woodson, S.A.3
  • 43
    • 0022369785 scopus 로고
    • IS10 transposition is regulated by DNA adenine methylation
    • Roberts, D., Hoopes, B.C., McClure, W.R., and Kleckner, N. (1985) IS10 transposition is regulated by DNA adenine methylation. Cell 43: 117-130.
    • (1985) Cell , vol.43 , pp. 117-130
    • Roberts, D.1    Hoopes, B.C.2    McClure, W.R.3    Kleckner, N.4
  • 44
    • 77958594047 scopus 로고    scopus 로고
    • Tn10/IS10 transposition is downregulated at the level of transposase expression by the RNA-binding protein Hfq
    • Ross, J.A., Wardle, S.J., and Haniford, D.B. (2010) Tn10/IS10 transposition is downregulated at the level of transposase expression by the RNA-binding protein Hfq. Mol Microbiol 78: 607-621.
    • (2010) Mol Microbiol , vol.78 , pp. 607-621
    • Ross, J.A.1    Wardle, S.J.2    Haniford, D.B.3
  • 45
    • 84876565196 scopus 로고    scopus 로고
    • Hfq restructures RNA-IN and RNA-OUT and facilitates antisense pairing in the Tn10/IS10 system
    • Ross, J.A., Ellis, M.J., Hossain, S., and Haniford, D.B. (2013) Hfq restructures RNA-IN and RNA-OUT and facilitates antisense pairing in the Tn10/IS10 system. RNA 19: 670-684.
    • (2013) RNA , vol.19 , pp. 670-684
    • Ross, J.A.1    Ellis, M.J.2    Hossain, S.3    Haniford, D.B.4
  • 46
    • 84885869888 scopus 로고    scopus 로고
    • Antagonistic functions between the RNA chaperone Hfq and an sRNA regulate sensitivity to the antibiotic colicin
    • Salvail, H., Caron, M.P., Belanger, J., and Masse, E. (2013) Antagonistic functions between the RNA chaperone Hfq and an sRNA regulate sensitivity to the antibiotic colicin. EMBO J 32: 2764-2778.
    • (2013) EMBO J , vol.32 , pp. 2764-2778
    • Salvail, H.1    Caron, M.P.2    Belanger, J.3    Masse, E.4
  • 47
    • 84879005493 scopus 로고    scopus 로고
    • Structure and RNA-binding properties of the bacterial LSm protein Hfq
    • Sauer, E. (2013) Structure and RNA-binding properties of the bacterial LSm protein Hfq. RNA Biol 10: 610-618.
    • (2013) RNA Biol , vol.10 , pp. 610-618
    • Sauer, E.1
  • 48
    • 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. PNAS 108: 13065-13070.
    • (2011) PNAS , vol.108 , pp. 13065-13070
    • Sauer, E.1    Weichenrieder, O.2
  • 49
    • 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
  • 50
    • 0020826922 scopus 로고
    • Translational control of IS10 transposition
    • Simons, R.W., and Kleckner, N. (1983) Translational control of IS10 transposition. Cell 34: 683-691.
    • (1983) Cell , vol.34 , pp. 683-691
    • Simons, R.W.1    Kleckner, N.2
  • 51
    • 50849105413 scopus 로고    scopus 로고
    • Deep sequencing analysis of small noncoding RNA and mRNA targets of the global post-transcriptional regulator, Hfq
    • Sittka, A., Lucchini, S., Papenfort, K., Sharma, C.M., Rolle, K., Binnewies, T.T., etal. (2008) Deep sequencing analysis of small noncoding RNA and mRNA targets of the global post-transcriptional regulator, Hfq. PLoS Genet 4: e1000163.
    • (2008) PLoS Genet , vol.4 , pp. e1000163
    • Sittka, A.1    Lucchini, S.2    Papenfort, K.3    Sharma, C.M.4    Rolle, K.5    Binnewies, T.T.6
  • 52
    • 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
  • 53
    • 84866307118 scopus 로고    scopus 로고
    • The bacterial protein Hfq: much more than a mere RNA-binding factor
    • Sobrero, P., and Valverde, C. (2012) The bacterial protein Hfq: much more than a mere RNA-binding factor. Crit Rev Microbiol 38: 276-299.
    • (2012) Crit Rev Microbiol , vol.38 , pp. 276-299
    • Sobrero, P.1    Valverde, C.2
  • 54
    • 77953090678 scopus 로고    scopus 로고
    • Positive regulation by small RNAs and the role of Hfq
    • Soper, T., Mandin, P., Majdalani, N., Gottesman, S., and Woodson, S.A. (2010) Positive regulation by small RNAs and the role of Hfq. PNAS 107: 9602-9607.
    • (2010) PNAS , vol.107 , pp. 9602-9607
    • Soper, T.1    Mandin, P.2    Majdalani, N.3    Gottesman, S.4    Woodson, S.A.5
  • 55
    • 79960441320 scopus 로고    scopus 로고
    • Major role for mRNA binding and restructuring in sRNA recruitment by Hfq
    • Soper, T.J., Doxzen, K., and Woodson, S.A. (2011) Major role for mRNA binding and restructuring in sRNA recruitment by Hfq. RNA 17: 1544-1550.
    • (2011) RNA , vol.17 , pp. 1544-1550
    • Soper, T.J.1    Doxzen, K.2    Woodson, S.A.3
  • 56
    • 80053019485 scopus 로고    scopus 로고
    • Regulation by small RNAs in bacteria: expanding frontiers
    • Storz, G., Vogel, J., and Wassarman, K.M. (2011) Regulation by small RNAs in bacteria: expanding frontiers. Mol Cell 43: 880-891.
    • (2011) Mol Cell , vol.43 , pp. 880-891
    • Storz, G.1    Vogel, J.2    Wassarman, K.M.3
  • 57
    • 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
  • 58
    • 84904467798 scopus 로고    scopus 로고
    • Identification of bacteriophage-encoded anti-sRNAs in pathogenic escherichia coli
    • Tree, J.J., Granneman, S., McAteer, S.P., Tollervey, D., and Gally, D.L. (2014) Identification of bacteriophage-encoded anti-sRNAs in pathogenic escherichia coli. Mol Cell 55: 199-213.
    • (2014) Mol Cell , vol.55 , pp. 199-213
    • Tree, J.J.1    Granneman, S.2    McAteer, S.P.3    Tollervey, D.4    Gally, D.L.5
  • 59
    • 77955663530 scopus 로고    scopus 로고
    • E. coli DNA associated with isolated Hfq interacts with Hfq's distal surface and C-terminal domain
    • Updegrove, T.B., Correia, J.J., Galletto, R., Bujalowski, W., and Wartell, R.M. (2010) E. coli DNA associated with isolated Hfq interacts with Hfq's distal surface and C-terminal domain. Biochim Biophys Acta 1799: 588-596.
    • (2010) Biochim Biophys Acta , vol.1799 , pp. 588-596
    • Updegrove, T.B.1    Correia, J.J.2    Galletto, R.3    Bujalowski, W.4    Wartell, R.M.5
  • 60
    • 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
  • 61
    • 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
  • 63
    • 0034194572 scopus 로고    scopus 로고
    • Hfq (HF1) stimulates ompA mRNA decay by interfering with ribosome binding
    • Vytvytska, O., Moll, I., Kaberdin, V.R., von Gabain, A., and Bläsi, U. (2000) Hfq (HF1) stimulates ompA mRNA decay by interfering with ribosome binding. Genes Dev 14: 1109-1118.
    • (2000) Genes Dev , vol.14 , pp. 1109-1118
    • Vytvytska, O.1    Moll, I.2    Kaberdin, V.R.3    von Gabain, A.4    Bläsi, U.5
  • 64
    • 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
  • 66
    • 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


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