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Volumn 38, Issue 4, 2012, Pages 276-299

The bacterial protein Hfq: Much more than a mere RNA-binding factor

Author keywords

Global regulator; Hfq; Nucleic acid binding protein; Sm protein; SRNAmRNA interactions

Indexed keywords

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

EID: 84866307118     PISSN: 1040841X     EISSN: 15497828     Source Type: Journal    
DOI: 10.3109/1040841X.2012.664540     Document Type: Review
Times cited : (117)

References (204)
  • 1
    • 80052338289 scopus 로고    scopus 로고
    • Essential requirements for robust signaling in Hfq dependent small RNA networks
    • Adamson DN, Lim HN. (2011). Essential requirements for robust signaling in Hfq dependent small RNA networks. PLoS Comput Biol, 7, e1002138.
    • (2011) PLoS Comput Biol , vol.7
    • Adamson, D.N.1    Lim, H.N.2
  • 2
    • 15044340366 scopus 로고    scopus 로고
    • Both RNase e and RNase III control the stability of sodB mRNA upon translational inhibition by the small regulatory RNA RyhB
    • Afonyushkin T, Vecerek B, Moll I, Bläsi U, Kaberdin VR. (2005). Both RNase E and RNase III control the stability of sodB mRNA upon translational inhibition by the small regulatory RNA RyhB. Nucleic Acids Res, 33, 1678-1689.
    • (2005) Nucleic Acids Res , vol.33 , pp. 1678-1689
    • Afonyushkin, T.1    Vecerek, B.2    Moll, I.3    Bläsi, U.4    Kaberdin, V.R.5
  • 3
    • 34247158257 scopus 로고    scopus 로고
    • Mechanism of RNA silencing by Hfq-binding small RNAs
    • Aiba H. (2007). Mechanism of RNA silencing by Hfq-binding small RNAs. Curr Opin Microbiol, 10, 134-139.
    • (2007) Curr Opin Microbiol , vol.10 , pp. 134-139
    • Aiba, H.1
  • 4
    • 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, 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
  • 5
    • 79951796751 scopus 로고    scopus 로고
    • Salmonella enterica serovar Typhimurium lacking hfq gene confers protective immunity against murine typhoid
    • Allam US, Krishna MG, Lahiri A, Joy O, Chakravortty D. (2011). Salmonella enterica serovar Typhimurium lacking hfq gene confers protective immunity against murine typhoid. PLoS ONE, 6, e16667.
    • (2011) PLoS ONE , vol.6
    • Allam, U.S.1    Krishna, M.G.2    Lahiri, A.3    Joy, O.4    Chakravortty, D.5
  • 8
    • 33847363604 scopus 로고    scopus 로고
    • Spectroscopic observation of RNA chaperone activities of Hfq in post-transcriptional regulation by a small non-coding RNA
    • Arluison V, Hohng S, Roy R, Pellegrini O, Régnier P, Ha T. (2007a). Spectroscopic observation of RNA chaperone activities of Hfq in post-transcriptional regulation by a small non-coding RNA. Nucleic Acids Res, 35, 999-1006.
    • (2007) Nucleic Acids Res , vol.35 , pp. 999-1006
    • Arluison, V.1    Hohng, S.2    Roy, R.3    Pellegrini, O.4    Régnier, P.5    Ha, T.6
  • 9
    • 34548388002 scopus 로고    scopus 로고
    • Sm-like protein Hfq: Location of the ATP-binding site and the effect of ATP on Hfq-RNA complexes
    • Arluison V, Mutyam SK, Mura C, Marco S, Sukhodolets MV. (2007b). Sm-like protein Hfq: location of the ATP-binding site and the effect of ATP on Hfq-RNA complexes. Protein Sci, 16, 1830-1841.
    • (2007) Protein Sci , vol.16 , pp. 1830-1841
    • Arluison, V.1    Mutyam, S.K.2    Mura, C.3    Marco, S.4    Sukhodolets, M.V.5
  • 10
    • 67651225588 scopus 로고    scopus 로고
    • Identification of small RNAs in Mycobacterium tuberculosis
    • Arnvig KB, Young DB. (2009). Identification of small RNAs in Mycobacterium tuberculosis. Mol Microbiol, 73, 397-408.
    • (2009) Mol Microbiol , vol.73 , pp. 397-408
    • Arnvig, K.B.1    Young, D.B.2
  • 14
    • 0032731196 scopus 로고    scopus 로고
    • Twelve species of the nucleoidassociated protein from Escherichia coli. Sequence recognition specificity and DNA binding affinity
    • Azam TA, Ishihama A. (1999). Twelve species of the nucleoidassociated protein from Escherichia coli. Sequence recognition specificity and DNA binding affinity. J Biol Chem, 274, 33105-33113.
    • (1999) J Biol Chem , vol.274 , pp. 33105-33113
    • Azam, T.A.1    Ishihama, A.2
  • 15
    • 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
    • Baba S, Someya T, Kawai G, Nakamura K, 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) Acta Crystallogr 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
  • 16
    • 69249232822 scopus 로고    scopus 로고
    • Regulation of translation initiation by RNA binding proteins
    • Babitzke P, Baker CS, Romeo T. (2009). Regulation of translation initiation by RNA binding proteins. Annu Rev Microbiol, 63, 27-44.
    • (2009) Annu Rev Microbiol , vol.63 , pp. 27-44
    • Babitzke, P.1    Baker, C.S.2    Romeo, T.3
  • 17
    • 77955958425 scopus 로고    scopus 로고
    • The importance of the small RNA chaperone Hfq for growth of epidemic Yersinia pestis, but not Yersinia pseudotuberculosis, with implications for plague biology
    • Bai G, Golubov A, Smith EA, McDonough KA. (2010). The importance of the small RNA chaperone Hfq for growth of epidemic Yersinia pestis, but not Yersinia pseudotuberculosis, with implications for plague biology. J Bacteriol, 192, 4239-4245.
    • (2010) J Bacteriol , vol.192 , pp. 4239-4245
    • Bai, G.1    Golubov, A.2    Smith, E.A.3    McDonough, K.A.4
  • 18
  • 19
    • 78649346987 scopus 로고    scopus 로고
    • Recognition of heptameric seed sequence underlies multitarget regulation by RybB small RNA in Salmonella enterica
    • Balbontín R, Fiorini F, Figueroa-Bossi N, Casadesús J, Bossi L. (2010). Recognition of heptameric seed sequence underlies multitarget regulation by RybB small RNA in Salmonella enterica. Mol Microbiol, 78, 380-394.
    • (2010) Mol Microbiol , vol.78 , pp. 380-394
    • Balbontín, R.1    Fiorini, F.2    Figueroa-Bossi, N.3    Casadesús, J.4    Bossi, L.5
  • 21
    • 77949373122 scopus 로고    scopus 로고
    • The Sinorhizobium meliloti RNA chaperone Hfq mediates symbiosis of S. meliloti and alfalfa
    • Barra-Bily L, Pandey SP, Trautwetter A, Blanco C, Walker GC. (2010b). The Sinorhizobium meliloti RNA chaperone Hfq mediates symbiosis of S. meliloti and alfalfa. J Bacteriol, 192, 1710-1718.
    • (2010) J Bacteriol , vol.192 , pp. 1710-1718
    • Barra-Bily, L.1    Pandey, S.P.2    Trautwetter, A.3    Blanco, C.4    Walker, G.C.5
  • 24
    • 77955155869 scopus 로고    scopus 로고
    • Base pairing small RNAs and their roles in global regulatory networks
    • Beisel CL, Storz G. (2010). Base pairing small RNAs and their roles in global regulatory networks. FEMS Microbiol Rev, 34, 866-882.
    • (2010) FEMS Microbiol Rev , vol.34 , pp. 866-882
    • Beisel, C.L.1    Storz, G.2
  • 25
    • 74149085645 scopus 로고    scopus 로고
    • Coordination of genomic structure and transcription by the main bacterial nucleoid-associated protein HU
    • Berger M, Farcas A, Geertz M, Zhelyazkova P, Brix K, Travers A, Muskhelishvili G. (2010). Coordination of genomic structure and transcription by the main bacterial nucleoid-associated protein HU. EMBO Rep, 11, 59-64.
    • (2010) EMBO Rep , vol.11 , pp. 59-64
    • Berger, M.1    Farcas, A.2    Geertz, M.3    Zhelyazkova, P.4    Brix, K.5    Travers, A.6    Muskhelishvili, G.7
  • 26
    • 79958786333 scopus 로고    scopus 로고
    • Contribution of Hfq to photooxidative stress resistance and global regulation in Rhodobacter sphaeroides
    • Berghoff BA, Glaeser J, Sharma CM, Zobawa M, Lottspeich F, Vogel J, Klug G. (2011). Contribution of Hfq to photooxidative stress resistance and global regulation in Rhodobacter sphaeroides. Mol Microbiol, 80, 1479-1495.
    • (2011) Mol Microbiol , vol.80 , pp. 1479-1495
    • Berghoff, B.A.1    Glaeser, J.2    Sharma, C.M.3    Zobawa, M.4    Lottspeich, F.5    Vogel, J.6    Klug, G.7
  • 27
    • 67650649464 scopus 로고    scopus 로고
    • Cyanobacteria contain a structural homologue of the Hfq protein with altered RNA-binding properties
    • Bøggild A, Overgaard M, Valentin-Hansen P, Brodersen DE. (2009). Cyanobacteria contain a structural homologue of the Hfq protein with altered RNA-binding properties. FEBS J, 276, 3904-3915.
    • (2009) FEBS J , vol.276 , pp. 3904-3915
    • Bøggild, A.1    Overgaard, M.2    Valentin-Hansen, P.3    Brodersen, D.E.4
  • 28
    • 33847095025 scopus 로고    scopus 로고
    • No detectable effect of RNAbinding protein Hfq absence in Staphylococcus aureus
    • Bohn C, Rigoulay C, Bouloc P. (2007). No detectable effect of RNAbinding protein Hfq absence in Staphylococcus aureus. BMC Microbiol, 7, 10.
    • (2007) BMC Microbiol , vol.7 , pp. 10
    • Bohn, C.1    Rigoulay, C.2    Bouloc, P.3
  • 29
    • 34247109118 scopus 로고    scopus 로고
    • Hfq structure, function and ligand binding
    • Brennan RG, Link TM. (2007). Hfq structure, function and ligand binding. Curr Opin Microbiol, 10, 125-133.
    • (2007) Curr Opin Microbiol , vol.10 , pp. 125-133
    • Brennan, R.G.1    Link, T.M.2
  • 31
    • 33646153053 scopus 로고    scopus 로고
    • Determination of RNA orientation during translocation through a biological nanopore
    • Butler TZ, Gundlach JH, Troll MA. (2006). Determination of RNA orientation during translocation through a biological nanopore. Biophys J, 90, 190-199.
    • (2006) Biophys J , vol.90 , pp. 190-199
    • Butler, T.Z.1    Gundlach, J.H.2    Troll, M.A.3
  • 32
    • 77953753696 scopus 로고    scopus 로고
    • Small RNA-mediated regulation at the level of transcript stability
    • Caron MP, Lafontaine DA, Massé E. (2010). Small RNA-mediated regulation at the level of transcript stability. RNA Biol, 7, 140-144.
    • (2010) RNA Biol , vol.7 , pp. 140-144
    • Caron, M.P.1    Lafontaine, D.A.2    Massé, E.3
  • 33
    • 35548995356 scopus 로고    scopus 로고
    • The RNA degradosome of Escherichia coli: An mRNA-degrading machine assembled on RNase e
    • Carpousis AJ. (2007). The RNA degradosome of Escherichia coli: an mRNA-degrading machine assembled on RNase E. Annu Rev Microbiol, 61, 71-87.
    • (2007) Annu Rev Microbiol , vol.61 , pp. 71-87
    • Carpousis, A.J.1
  • 34
    • 79955857381 scopus 로고    scopus 로고
    • The RNA chaperone Hfq is important for growth and stress tolerance in Francisella novicida
    • Chambers JR, Bender KS. (2011). The RNA chaperone Hfq is important for growth and stress tolerance in Francisella novicida. PLoS ONE, 6, e19797.
    • (2011) PLoS ONE , vol.6
    • Chambers, J.R.1    Bender, K.S.2
  • 36
    • 79960288286 scopus 로고    scopus 로고
    • Impact of Hfq on global gene expression and virulence in Klebsiella pneumoniae
    • Chiang MK, Lu MC, Liu LC, Lin CT, Lai YC. (2011). Impact of Hfq on global gene expression and virulence in Klebsiella pneumoniae. PLoS ONE, 6, e22248.
    • (2011) PLoS ONE , vol.6
    • Chiang, M.K.1    Lu, M.C.2    Liu, L.C.3    Lin, C.T.4    Lai, Y.C.5
  • 40
    • 77957252762 scopus 로고    scopus 로고
    • CspC regulates rpoS transcript levels and complements hfq deletions
    • Cohen-Or I, Shenhar Y, Biran D, Ron EZ. (2010). CspC regulates rpoS transcript levels and complements hfq deletions. Res Microbiol, 161, 694-700.
    • (2010) Res Microbiol , vol.161 , pp. 694-700
    • Cohen-Or, I.1    Shenhar, Y.2    Biran, D.3    Ron, E.Z.4
  • 41
    • 78650306521 scopus 로고    scopus 로고
    • Small RNA sorting: Matchmaking for Argonautes
    • Czech B, Hannon GJ. (2011). Small RNA sorting: matchmaking for Argonautes. Nat Rev Genet, 12, 19-31.
    • (2011) Nat Rev Genet , vol.12 , pp. 19-31
    • Czech, B.1    Hannon, G.J.2
  • 42
    • 34447328708 scopus 로고    scopus 로고
    • RNase E-dependent processing stabilizes MicX, a Vibrio cholerae sRNA
    • Davis BM, Waldor MK. (2007). RNase E-dependent processing stabilizes MicX, a Vibrio cholerae sRNA. Mol Microbiol, 65, 373-385.
    • (2007) Mol Microbiol , vol.65 , pp. 373-385
    • Davis, B.M.1    Waldor, M.K.2
  • 43
    • 0019254853 scopus 로고
    • Interaction of Escherichia coli host factor protein with oligoriboadenylates
    • de Haseth PL, Uhlenbeck OC. (1980a). 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
  • 44
    • 0019256070 scopus 로고
    • Interaction of Escherichia coli host factor protein with Q beta ribonucleic acid
    • de Haseth PL, Uhlenbeck OC. (1980b). 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
  • 45
    • 77955077136 scopus 로고    scopus 로고
    • Multiple small RNAs identified in Mycobacterium bovis BCG are also expressed in Mycobacterium tuberculosis and Mycobacterium smegmatis
    • DiChiara JM, Contreras-Martinez LM, Livny J, Smith D, McDonough KA, Belfort M. (2010). Multiple small RNAs identified in Mycobacterium bovis BCG are also expressed in Mycobacterium tuberculosis and Mycobacterium smegmatis. Nucleic Acids Res, 38, 4067-4078.
    • (2010) Nucleic Acids Res , vol.38 , pp. 4067-4078
    • Dichiara, J.M.1    Contreras-Martinez, L.M.2    Livny, J.3    Smith, D.4    McDonough, K.A.5    Belfort, M.6
  • 47
    • 77949512479 scopus 로고    scopus 로고
    • Cellular electron microscopy imaging reveals the localization of the Hfq protein close to the bacterial membrane
    • Diestra E, Cayrol B, Arluison V, Risco C. (2009). Cellular electron microscopy imaging reveals the localization of the Hfq protein close to the bacterial membrane. PLoS ONE, 4, e8301.
    • (2009) PLoS ONE , vol.4
    • Diestra, E.1    Cayrol, B.2    Arluison, V.3    Risco, C.4
  • 49
    • 3142550776 scopus 로고    scopus 로고
    • Hfq is essential for Vibrio cholerae virulence and downregulates sigma expression
    • Ding Y, Davis BM, Waldor MK. (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
  • 50
    • 0037044479 scopus 로고    scopus 로고
    • The Hfq-like protein NrfA of the phototrophic purple bacterium Rhodobacter capsulatus controls nitrogen fixation via regulation of nifA and anfA expression
    • Drepper T, Raabe K, Giaourakis D, Gendrullis M, Masepohl B, Klipp W. (2002). The Hfq-like protein NrfA of the phototrophic purple bacterium Rhodobacter capsulatus controls nitrogen fixation via regulation of nifA and anfA expression. FEMS Microbiol Lett, 215, 221-227.
    • (2002) FEMS Microbiol Lett , vol.215 , pp. 221-227
    • Drepper, T.1    Raabe, K.2    Giaourakis, D.3    Gendrullis, M.4    Masepohl, B.5    Klipp, W.6
  • 52
    • 65449172051 scopus 로고    scopus 로고
    • The RNA chaperone Hfq is involved in stress response and virulence in Neisseria meningitidis and is a pleiotropic regulator of protein expression
    • Fantappiè L, Metruccio MM, Seib KL, Oriente F, Cartocci E, Ferlicca F, Giuliani MM, Scarlato V, Delany I. (2009). The RNA chaperone Hfq is involved in stress response and virulence in Neisseria meningitidis and is a pleiotropic regulator of protein expression. Infect Immun, 77, 1842-1853.
    • (2009) Infect Immun , vol.77 , pp. 1842-1853
    • Fantappiè, L.1    Metruccio, M.M.2    Seib, K.L.3    Oriente, F.4    Cartocci, E.5    Ferlicca, F.6    Giuliani, M.M.7    Scarlato, V.8    Delany, I.9
  • 53
    • 0000461280 scopus 로고
    • Onfidence limits on phylogenies: An approach using the bootstrap
    • Felsenstein J. (1985). onfidence limits on phylogenies: An approach using the bootstrap. Evolution, 39, 783-791.
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 55
    • 12544256747 scopus 로고    scopus 로고
    • Stimulation of poly(A) synthesis by Escherichia coli poly(A)polymerase i is correlated with Hfq binding to poly(A) tails
    • Folichon M, Allemand F, Régnier P, Hajnsdorf E. (2005). Stimulation of poly(A) synthesis by Escherichia coli poly(A)polymerase I is correlated with Hfq binding to poly(A) tails. FEBS J, 272, 454-463.
    • (2005) FEBS J , vol.272 , pp. 454-463
    • Folichon, M.1    Allemand, F.2    Régnier, P.3    Hajnsdorf, E.4
  • 56
    • 0014409656 scopus 로고
    • Factor fraction required for the synthesis of bacteriophage Qbeta-RNA
    • Franze de Fernandez MT, Eoyang L, August JT. (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
  • 57
    • 0015500282 scopus 로고
    • Bacterial proteins required for replication of phage Q ribonucleic acid. Pruification and properties of host factor I, a ribonucleic acidbinding protein
    • Franze de Fernandez MT, Hayward WS, August JT. (1972). Bacterial proteins required for replication of phage Q ribonucleic acid. Pruification and properties of host factor I, a ribonucleic acidbinding 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
  • 58
    • 71549126189 scopus 로고    scopus 로고
    • Activation of gene expression by small RNA
    • Fröhlich KS, Vogel J. (2009). Activation of gene expression by small RNA. Curr Opin Microbiol, 12, 674-682.
    • (2009) Curr Opin Microbiol , vol.12 , pp. 674-682
    • Fröhlich, K.S.1    Vogel, J.2
  • 61
    • 1542320707 scopus 로고    scopus 로고
    • Hfq, a new chaperoning role: Binding to messenger RNA determines access for small RNA regulator
    • Geissmann TA, 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
  • 63
    • 79958047291 scopus 로고    scopus 로고
    • Cis-antisense RNA, another level of gene regulation in bacteria
    • Georg J, Hess WR. (2011). cis-antisense RNA, another level of gene regulation in bacteria. Microbiol Mol Biol Rev, 75, 286-300.
    • (2011) Microbiol Mol Biol Rev , vol.75 , pp. 286-300
    • Georg, J.1    Hess, W.R.2
  • 64
    • 57149118846 scopus 로고    scopus 로고
    • The 5′ end of two redundant sRNAs is involved in the regulation of multiple targets, including their own regulator
    • Guillier M, Gottesman S. (2008). The 5′ end of two redundant sRNAs is involved in the regulation of multiple targets, including their own regulator. Nucleic Acids Res, 36, 6781-6794.
    • (2008) Nucleic Acids Res , vol.36 , pp. 6781-6794
    • Guillier, M.1    Gottesman, S.2
  • 65
    • 33947361601 scopus 로고    scopus 로고
    • Hfq modulates the sigmaE-mediated envelope stress response and the sigma32-mediated cytoplasmic stress response in Escherichia coli
    • Guisbert E, Rhodius VA, Ahuja N, Witkin E, Gross CA. (2007). Hfq modulates the sigmaE-mediated envelope stress response and the sigma32-mediated cytoplasmic stress response in Escherichia coli. J Bacteriol, 189, 1963-1973.
    • (2007) J Bacteriol , vol.189 , pp. 1963-1973
    • Guisbert, E.1    Rhodius, V.A.2    Ahuja, N.3    Witkin, E.4    Gross, C.A.5
  • 66
    • 67651204873 scopus 로고    scopus 로고
    • Hfq affects the expression of the LEE pathogenicity island in enterohaemorrhagic Escherichia coli
    • Hansen AM, Kaper JB. (2009). Hfq affects the expression of the LEE pathogenicity island in enterohaemorrhagic Escherichia coli. Mol Microbiol, 73, 446-465.
    • (2009) Mol Microbiol , vol.73 , pp. 446-465
    • Hansen, A.M.1    Kaper, J.B.2
  • 68
    • 77953120292 scopus 로고    scopus 로고
    • Two antisense RNAs target the transcriptional regulator CsgD to inhibit curli synthesis
    • Holmqvist E, Reimegård J, Sterk M, Grantcharova N, Römling U, Wagner EG. (2010). Two antisense RNAs target the transcriptional regulator CsgD to inhibit curli synthesis. EMBO J, 29, 1840-1850.
    • (2010) EMBO J , vol.29 , pp. 1840-1850
    • Holmqvist, E.1    Reimegård, J.2    Sterk, M.3    Grantcharova, N.4    Römling, U.5    Wagner, E.G.6
  • 69
    • 79958095005 scopus 로고    scopus 로고
    • Rapid binding and release of Hfq from ternary complexes during RNA annealing
    • Hopkins JF, Panja S, Woodson SA. (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
  • 71
    • 79551650983 scopus 로고    scopus 로고
    • Disruption of small RNA signaling caused by competition for Hfq
    • Hussein R, Lim HN. (2011). Disruption of small RNA signaling caused by competition for Hfq. Proc Natl Acad Sci USA, 108, 1110-1115.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 1110-1115
    • Hussein, R.1    Lim, H.N.2
  • 72
    • 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, 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
  • 73
    • 78651067735 scopus 로고    scopus 로고
    • Hfq binding at RhlBrecognition region of RNase e is crucial for the rapid degradation of target mRNAs mediated by sRNAs in Escherichia coli
    • Ikeda Y, Yagi M, Morita T, Aiba H. (2011). Hfq binding at RhlBrecognition region of RNase E is crucial for the rapid degradation of target mRNAs mediated by sRNAs in Escherichia coli. Mol Microbiol, 79, 419-432.
    • (2011) Mol Microbiol , vol.79 , pp. 419-432
    • Ikeda, Y.1    Yagi, M.2    Morita, T.3    Aiba, H.4
  • 74
    • 0016945206 scopus 로고
    • Proceedings: Control of RNA polymerase synthesis in Escherichia coli
    • Ishihama A. (1976). Proceedings: Control of RNA polymerase synthesis in Escherichia coli. J Biochem, 79, 33P-34P.
    • (1976) J Biochem , vol.79
    • Ishihama, A.1
  • 76
    • 52049089226 scopus 로고    scopus 로고
    • Down-regulation of outer membrane proteins by noncoding RNAs: Unraveling the cAMP-CRP-and sigmaE-dependent CyaRompX regulatory case
    • Johansen J, Eriksen M, Kallipolitis B, Valentin-Hansen P. (2008). Down-regulation of outer membrane proteins by noncoding RNAs: unraveling the cAMP-CRP-and sigmaE-dependent CyaRompX regulatory case. J Mol Biol, 383, 1-9.
    • (2008) J Mol Biol , vol.383 , pp. 1-9
    • Johansen, J.1    Eriksen, M.2    Kallipolitis, B.3    Valentin-Hansen, P.4
  • 78
    • 65549117835 scopus 로고    scopus 로고
    • Identification of genes contributing to the virulence of Francisella tularensis SCHU S4 in a mouse intradermal infection model
    • Kadzhaev K, Zingmark C, Golovliov I, Bolanowski M, Shen H, Conlan W, Sjöstedt A. (2009). Identification of genes contributing to the virulence of Francisella tularensis SCHU S4 in a mouse intradermal infection model. PLoS ONE, 4, e5463.
    • (2009) PLoS ONE , vol.4
    • Kadzhaev, K.1    Zingmark, C.2    Golovliov, I.3    Bolanowski, M.4    Shen, H.5    Conlan, W.6    Sjöstedt, A.7
  • 79
    • 0026067069 scopus 로고
    • Identification and sequence determination of the host factor gene for bacteriophage Q beta
    • Kajitani M, Ishihama A. (1991). Identification and sequence determination of the host factor gene for bacteriophage Q beta. Nucleic Acids Res, 19, 1063-1066.
    • (1991) Nucleic Acids Res , vol.19 , pp. 1063-1066
    • Kajitani, M.1    Ishihama, A.2
  • 80
    • 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, 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
  • 81
    • 0028246273 scopus 로고
    • The expression of nifA in Azorhizobium caulinodans requires a gene product homologous to Escherichia coli HF-I, an RNA-binding protein involved in the replication of phage Q beta RNA
    • Kaminski PA, Desnoues N, Elmerich C. (1994). The expression of nifA in Azorhizobium caulinodans requires a gene product homologous to Escherichia coli HF-I, an RNA-binding protein involved in the replication of phage Q beta RNA. Proc Natl Acad Sci USA, 91, 4663-4667.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4663-4667
    • Kaminski, P.A.1    Desnoues, N.2    Elmerich, C.3
  • 82
    • 0031979601 scopus 로고    scopus 로고
    • The control of Azorhizobium caulinodans nifA expression by oxygen, ammonia and by the HF-Ilike protein, NrfA
    • Kaminski PA, Elmerich C. (1998). The control of Azorhizobium caulinodans nifA expression by oxygen, ammonia and by the HF-Ilike protein, NrfA. Mol Microbiol, 28, 603-613.
    • (1998) Mol Microbiol , vol.28 , pp. 603-613
    • Kaminski, P.A.1    Elmerich, C.2
  • 83
    • 28044436995 scopus 로고    scopus 로고
    • Nucleoid remodeling by an altered HU protein: Reorganization of the transcription program
    • Kar S, Edgar R, Adhya S. (2005). Nucleoid remodeling by an altered HU protein: reorganization of the transcription program. Proc Natl Acad Sci USA, 102, 16397-16402.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 16397-16402
    • Kar, S.1    Edgar, R.2    Adhya, S.3
  • 84
    • 33746553370 scopus 로고    scopus 로고
    • Base-pairing requirement for RNA silencing by a bacterial small RNA and acceleration of duplex formation by Hfq
    • Kawamoto H, Koide Y, Morita T, Aiba H. (2006). Base-pairing requirement for RNA silencing by a bacterial small RNA and acceleration of duplex formation by Hfq. Mol Microbiol, 61, 1013-1022.
    • (2006) Mol Microbiol , vol.61 , pp. 1013-1022
    • Kawamoto, H.1    Koide, Y.2    Morita, T.3    Aiba, H.4
  • 85
    • 77957917685 scopus 로고    scopus 로고
    • Transmembrane helix i and periplasmic loop 1 of Escherichia coli ProP are involved in osmosensing and osmoprotectant transport
    • Keates RA, Culham DE, Vernikovska YI, Zuiani AJ, Boggs JM, Wood JM. (2010). Transmembrane helix I and periplasmic loop 1 of Escherichia coli ProP are involved in osmosensing and osmoprotectant transport. Biochemistry, 49, 8847-8856.
    • (2010) Biochemistry , vol.49 , pp. 8847-8856
    • Keates, R.A.1    Culham, D.E.2    Vernikovska, Y.I.3    Zuiani, A.J.4    Boggs, J.M.5    Wood, J.M.6
  • 86
    • 46449132381 scopus 로고    scopus 로고
    • Impact of the RNA chaperone Hfq on the fitness and virulence potential of uropathogenic Escherichia coli
    • Kulesus RR, Diaz-Perez K, Slechta ES, Eto DS, Mulvey MA. (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
  • 87
    • 77953930251 scopus 로고    scopus 로고
    • Molecular Dynamics Simulation Study for Ionic Strength Dependence of RNA-host factor Interaction in Staphylococcus aureus Hfq
    • Lazar P, Lee Y, Kim S, Chandrasekaran M, Lee KW. (2010). Molecular Dynamics Simulation Study for Ionic Strength Dependence of RNA-host factor Interaction in Staphylococcus aureus Hfq. Bull Korean Chem Soc, 31, 1519-1526.
    • (2010) Bull Korean Chem Soc , vol.31 , pp. 1519-1526
    • Lazar, P.1    Lee, Y.2    Kim, S.3    Chandrasekaran, M.4    Lee, K.W.5
  • 89
    • 9244253711 scopus 로고    scopus 로고
    • Cycling of the Sm-like protein Hfq on the DsrA small regulatory RNA
    • Lease RA, Woodson SA. (2004). Cycling of the Sm-like protein Hfq on the DsrA small regulatory RNA. J Mol Biol, 344, 1211-1223.
    • (2004) J Mol Biol , vol.344 , pp. 1211-1223
    • Lease, R.A.1    Woodson, S.A.2
  • 90
    • 40449137036 scopus 로고    scopus 로고
    • The RNA binding protein Hfq interacts specifically with tRNAs
    • Lee T, Feig AL. (2008). The RNA binding protein Hfq interacts specifically with tRNAs. RNA, 14, 514-523.
    • (2008) RNA , vol.14 , pp. 514-523
    • Lee, T.1    Feig, A.L.2
  • 91
    • 72049095718 scopus 로고    scopus 로고
    • Structure of Escherichia coli Hfq bound to polyriboadenylate RNA
    • Link TM, Valentin-Hansen P, Brennan RG. (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
  • 92
    • 79960701781 scopus 로고    scopus 로고
    • Roles of Hfq in the stress adaptation and virulence in fish pathogen Vibrio alginolyticus and its potential application as a target for live attenuated vaccine
    • Liu H, Wang Q, Liu Q, Cao X, Shi C, Zhang Y. (2011). Roles of Hfq in the stress adaptation and virulence in fish pathogen Vibrio alginolyticus and its potential application as a target for live attenuated vaccine. Appl Microbiol Biotechnol, 91, 353-364.
    • (2011) Appl Microbiol Biotechnol , vol.91 , pp. 353-364
    • Liu, H.1    Wang, Q.2    Liu, Q.3    Cao, X.4    Shi, C.5    Zhang, Y.6
  • 93
    • 64549149245 scopus 로고    scopus 로고
    • Experimental discovery of sRNAs in Vibrio cholerae by direct cloning, 5S/tRNA depletion and parallel sequencing
    • Liu JM, Livny J, Lawrence MS, Kimball MD, Waldor MK, Camilli A. (2009). Experimental discovery of sRNAs in Vibrio cholerae by direct cloning, 5S/tRNA depletion and parallel sequencing. Nucleic Acids Res, 37, e46.
    • (2009) Nucleic Acids Res , vol.37
    • Liu, J.M.1    Livny, J.2    Lawrence, M.S.3    Kimball, M.D.4    Waldor, M.K.5    Camilli, A.6
  • 94
    • 77958547418 scopus 로고    scopus 로고
    • Hfq is a global regulator that controls the pathogenicity of Staphylococcus aureus
    • Liu Y, Wu N, Dong J, Gao Y, Zhang X, Mu C, Shao N, Yang G. (2010). Hfq is a global regulator that controls the pathogenicity of Staphylococcus aureus. PLoS One, 5, pii: e13069.
    • (2010) PLoS One , vol.5
    • Liu, Y.1    Wu, N.2    Dong, J.3    Gao, Y.4    Zhang, X.5    Mu, C.6    Shao, N.7    Yang, G.8
  • 95
    • 0025820457 scopus 로고
    • Growth rate regulation of translation initiation factor IF3 biosynthesis in Escherichia coli
    • Liveris D, Klotsky RA, Schwartz I. (1991). Growth rate regulation of translation initiation factor IF3 biosynthesis in Escherichia coli. J Bacteriol, 173, 3888-3893.
    • (1991) J Bacteriol , vol.173 , pp. 3888-3893
    • Liveris, D.1    Klotsky, R.A.2    Schwartz, I.3
  • 96
    • 33746533172 scopus 로고    scopus 로고
    • Identification of 17 Pseudomonas aeruginosa sRNAs and prediction of sRNAencoding genes in 10 diverse pathogens using the bioinformatic tool sRNAPredict2
    • Livny J, Brencic A, Lory S, Waldor MK. (2006). Identification of 17 Pseudomonas aeruginosa sRNAs and prediction of sRNAencoding genes in 10 diverse pathogens using the bioinformatic tool sRNAPredict2. Nucleic Acids Res, 34, 3484-3493.
    • (2006) Nucleic Acids Res , vol.34 , pp. 3484-3493
    • Livny, J.1    Brencic, A.2    Lory, S.3    Waldor, M.K.4
  • 98
    • 77958605759 scopus 로고    scopus 로고
    • Identification and function of the RNA chaperone Hfq in the Lyme disease spirochete Borrelia burgdorferi
    • Lybecker MC, Abel CA, Feig AL, Samuels DS. (2010). Identification and function of the RNA chaperone Hfq in the Lyme disease spirochete Borrelia burgdorferi. Mol Microbiol, 78, 622-635.
    • (2010) Mol Microbiol , vol.78 , pp. 622-635
    • Lybecker, M.C.1    Abel, C.A.2    Feig, A.L.3    Samuels, D.S.4
  • 99
    • 77951519861 scopus 로고    scopus 로고
    • A minimal base-pairing region of a bacterial small RNA SgrS required for translational repression of ptsG mRNA
    • Maki K, Morita T, Otaka H, Aiba H. (2010). A minimal base-pairing region of a bacterial small RNA SgrS required for translational repression of ptsG mRNA. Mol Microbiol, 76, 782-792.
    • (2010) Mol Microbiol , vol.76 , pp. 782-792
    • Maki, K.1    Morita, T.2    Otaka, H.3    Aiba, H.4
  • 100
    • 79955607368 scopus 로고    scopus 로고
    • Artificial trans-encoded small non-coding RNAs specifically silence the selected gene expression in bacteria
    • Man S, Cheng R, Miao C, Gong Q, Gu Y, Lu X, Han F, Yu W. (2011). Artificial trans-encoded small non-coding RNAs specifically silence the selected gene expression in bacteria. Nucleic Acids Res, 39, e50.
    • (2011) Nucleic Acids Res , vol.39
    • Man, S.1    Cheng, R.2    Miao, C.3    Gong, Q.4    Gu, Y.5    Lu, X.6    Han, F.7    Yu, W.8
  • 101
    • 0141860088 scopus 로고    scopus 로고
    • Coupled degradation of a small regulatory RNA and its mRNA targets in Escherichia coli
    • Massé E, Escorcia FE, Gottesman S. (2003). Coupled degradation of a small regulatory RNA and its mRNA targets in Escherichia coli. Genes Dev, 17, 2374-2383.
    • (2003) Genes Dev , vol.17 , pp. 2374-2383
    • Massé, E.1    Escorcia, F.E.2    Gottesman, S.3
  • 102
    • 14544288359 scopus 로고    scopus 로고
    • The Hfq homolog in Legionella pneumophila demonstrates regulation by LetA and RpoS and interacts with the global regulator CsrA
    • McNealy TL, Forsbach-Birk V, Shi C, Marre R. (2005). The Hfq homolog in Legionella pneumophila demonstrates regulation by LetA and RpoS and interacts with the global regulator CsrA. J Bacteriol, 187, 1527-1532.
    • (2005) J Bacteriol , vol.187 , pp. 1527-1532
    • McNealy, T.L.1    Forsbach-Birk, V.2    Shi, C.3    Marre, R.4
  • 103
    • 54049118804 scopus 로고    scopus 로고
    • A quantitative comparison of sRNA-based and protein-based gene regulation
    • Mehta P, Goyal S, Wingreen NS. (2008). A quantitative comparison of sRNA-based and protein-based gene regulation. Mol Syst Biol, 4, 221.
    • (2008) Mol Syst Biol , vol.4 , pp. 221
    • Mehta, P.1    Goyal, S.2    Wingreen, N.S.3
  • 107
    • 67649329734 scopus 로고    scopus 로고
    • Involvement of RNA-binding protein Hfq in the osmotic-response regulation of invE gene expression in Shigella sonnei
    • Mitobe J, Morita-Ishihara T, Ishihama A, Watanabe H. (2009). Involvement of RNA-binding protein Hfq in the osmotic-response regulation of invE gene expression in Shigella sonnei. BMC Microbiol, 9, 110.
    • (2009) BMC Microbiol , vol.9 , pp. 110
    • Mitobe, J.1    Morita-Ishihara, T.2    Ishihama, A.3    Watanabe, H.4
  • 109
    • 7044285063 scopus 로고    scopus 로고
    • The Sm-like protein Hfq regulates polyadenylation dependent mRNA decay in Escherichia coli
    • Mohanty BK, Maples VF, Kushner SR. (2004). The Sm-like protein Hfq regulates polyadenylation dependent mRNA decay in Escherichia coli. Mol Microbiol, 54, 905-920.
    • (2004) Mol Microbiol , vol.54 , pp. 905-920
    • Mohanty, B.K.1    Maples, V.F.2    Kushner, S.R.3
  • 110
    • 0037367939 scopus 로고    scopus 로고
    • RNA chaperone activity of the Sm-like Hfq protein
    • Moll I, Leitsch D, Steinhauser T, Bläsi U. (2003). RNA chaperone activity of the Sm-like Hfq protein. EMBO Rep, 4, 284-289.
    • (2003) EMBO Rep , vol.4 , pp. 284-289
    • Moll, I.1    Leitsch, D.2    Steinhauser, T.3    Bläsi, U.4
  • 112
    • 83355177980 scopus 로고    scopus 로고
    • Competition among Hfq-binding small RNAs in Escherichia coli
    • Moon K, 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
  • 113
    • 24944507588 scopus 로고    scopus 로고
    • RNase E-based ribonucleoprotein complexes: Mechanical basis of mRNA destabilization mediated by bacterial noncoding RNAs
    • Morita T, Maki K, Aiba H. (2005). RNase E-based ribonucleoprotein complexes: mechanical basis of mRNA destabilization mediated by bacterial noncoding RNAs. Genes Dev, 19, 2176-2186.
    • (2005) Genes Dev , vol.19 , pp. 2176-2186
    • Morita, T.1    Maki, K.2    Aiba, H.3
  • 114
    • 33645508496 scopus 로고    scopus 로고
    • Translational repression is sufficient for gene silencing by bacterial small noncoding RNAs in the absence of mRNA destruction
    • Morita T, Mochizuki Y, Aiba H. (2006). Translational repression is sufficient for gene silencing by bacterial small noncoding RNAs in the absence of mRNA destruction. Proc Natl Acad Sci USA, 103, 4858-4863.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 4858-4863
    • Morita, T.1    Mochizuki, Y.2    Aiba, H.3
  • 116
    • 79953066020 scopus 로고    scopus 로고
    • Mutation of GOGAT prevents pea bacteroid formation and N2 fixation by globally downregulating transport of organic nitrogen sources
    • Mulley G, White JP, Karunakaran R, Prell J, Bourdes A, Bunnewell S, Hill L, Poole PS. (2011). Mutation of GOGAT prevents pea bacteroid formation and N2 fixation by globally downregulating transport of organic nitrogen sources. Mol Microbiol, 80, 149-167.
    • (2011) Mol Microbiol , vol.80 , pp. 149-167
    • Mulley, G.1    White, J.P.2    Karunakaran, R.3    Prell, J.4    Bourdes, A.5    Bunnewell, S.6    Hill, L.7    Poole, P.S.8
  • 119
    • 53249156098 scopus 로고    scopus 로고
    • Hfq regulates the expression of the thermostable direct hemolysin gene in Vibrio parahaemolyticus
    • Nakano M, Takahashi A, Su Z, Harada N, Mawatari K, Nakaya Y. (2008). Hfq regulates the expression of the thermostable direct hemolysin gene in Vibrio parahaemolyticus. BMC Microbiol, 8, 155.
    • (2008) BMC Microbiol , vol.8 , pp. 155
    • Nakano, M.1    Takahashi, A.2    Su, Z.3    Harada, N.4    Mawatari, K.5    Nakaya, Y.6
  • 121
    • 36248940726 scopus 로고    scopus 로고
    • An Hfq-like protein in archaea: Crystal structure and functional characterization of the Sm protein from Methanococcus jannaschii
    • Nielsen JS, Bøggild A, Andersen CB, Nielsen G, Boysen A, Brodersen DE, Valentin-Hansen P. (2007). An Hfq-like protein in archaea: crystal structure and functional characterization of the Sm protein from Methanococcus jannaschii. RNA, 13, 2213-2223.
    • (2007) RNA , vol.13 , pp. 2213-2223
    • Nielsen, J.S.1    Bøggild, A.2    Andersen, C.B.3    Nielsen, G.4    Boysen, A.5    Brodersen, D.E.6    Valentin-Hansen, P.7
  • 124
    • 79955588726 scopus 로고    scopus 로고
    • Proteomic analyses of nucleoid-associated proteins in Escherichia coli, Pseudomonas aeruginosa, Bacillus subtilis, and Staphylococcus aureus
    • Ohniwa RL, Ushijima Y, Saito S, Morikawa K. (2011). Proteomic analyses of nucleoid-associated proteins in Escherichia coli, Pseudomonas aeruginosa, Bacillus subtilis, and Staphylococcus aureus. PLoS ONE, 6, e19172.
    • (2011) PLoS ONE , vol.6
    • Ohniwa, R.L.1    Ushijima, Y.2    Saito, S.3    Morikawa, K.4
  • 125
    • 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
  • 126
    • 78349305147 scopus 로고    scopus 로고
    • C-terminally truncated derivatives of Escherichia coli Hfq are proficient in riboregulation
    • Olsen AS, Møller-Jensen J, Brennan RG, Valentin-Hansen P. (2010). C-terminally truncated derivatives of Escherichia coli Hfq are proficient in riboregulation. J Mol Biol, 404, 173-182.
    • (2010) J Mol Biol , vol.404 , pp. 173-182
    • Olsen, A.S.1    Møller-Jensen, J.2    Brennan, R.G.3    Valentin-Hansen, P.4
  • 127
    • 4944264194 scopus 로고    scopus 로고
    • GadY, a small-RNA regulator of acid response genes in Escherichia coli
    • Opdyke JA, Kang JG, Storz G. (2004). GadY, a small-RNA regulator of acid response genes in Escherichia coli. J Bacteriol, 186, 6698-6705.
    • (2004) J Bacteriol , vol.186 , pp. 6698-6705
    • Opdyke, J.A.1    Kang, J.G.2    Storz, G.3
  • 128
    • 80051973174 scopus 로고    scopus 로고
    • PolyU tail of rhoindependent terminator of bacterial small RNAs is essential for Hfq action
    • Otaka H, Ishikawa H, Morita T, Aiba H. (2011). PolyU tail of rhoindependent terminator of bacterial small RNAs is essential for Hfq action. Proc Natl Acad Sci USA, 108, 13059-13064.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 13059-13064
    • Otaka, H.1    Ishikawa, H.2    Morita, T.3    Aiba, H.4
  • 129
    • 79959486063 scopus 로고    scopus 로고
    • A highly conserved protein of unknown function in Sinorhizobium meliloti affects sRNA regulation similar to Hfq
    • Pandey SP, Minesinger BK, Kumar J, Walker GC. (2011). A highly conserved protein of unknown function in Sinorhizobium meliloti affects sRNA regulation similar to Hfq. Nucleic Acids Res, 39, 4691-4708.
    • (2011) Nucleic Acids Res , vol.39 , pp. 4691-4708
    • Pandey, S.P.1    Minesinger, B.K.2    Kumar, J.3    Walker, G.C.4
  • 130
    • 78650532236 scopus 로고    scopus 로고
    • Evidence for an autonomous 5′ target recognition domain in an Hfqassociated small RNA
    • Papenfort K, Bouvier M, Mika F, Sharma CM, Vogel J. (2010). Evidence for an autonomous 5′ target recognition domain in an Hfqassociated small RNA. Proc Natl Acad Sci USA, 107, 20435-20440.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 20435-20440
    • Papenfort, K.1    Bouvier, M.2    Mika, F.3    Sharma, C.M.4    Vogel, J.5
  • 131
    • 33751383274 scopus 로고    scopus 로고
    • SigmaE-dependent small RNAs of Salmonella respond to membrane stress by accelerating global omp mRNA decay
    • Papenfort K, Pfeiffer V, Mika F, Lucchini S, Hinton JC, Vogel J. (2006). SigmaE-dependent small RNAs of Salmonella respond to membrane stress by accelerating global omp mRNA decay. Mol Microbiol, 62, 1674-1688.
    • (2006) Mol Microbiol , vol.62 , pp. 1674-1688
    • Papenfort, K.1    Pfeiffer, V.2    Mika, F.3    Lucchini, S.4    Hinton, J.C.5    Vogel, J.6
  • 132
    • 77958028354 scopus 로고    scopus 로고
    • Regulatory RNA in bacterial pathogens
    • Papenfort K, Vogel J. (2010). Regulatory RNA in bacterial pathogens. Cell Host Microbe, 8, 116-127.
    • (2010) Cell Host Microbe , vol.8 , pp. 116-127
    • Papenfort, K.1    Vogel, J.2
  • 133
    • 68249156618 scopus 로고    scopus 로고
    • Coding sequence targeting by MicC RNA reveals bacterial mRNA silencing downstream of translational initiation
    • Pfeiffer V, Papenfort K, Lucchini S, Hinton JC, Vogel J. (2009). Coding sequence targeting by MicC RNA reveals bacterial mRNA silencing downstream of translational initiation. Nat Struct Mol Biol, 16, 840-846.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 840-846
    • Pfeiffer, V.1    Papenfort, K.2    Lucchini, S.3    Hinton, J.C.4    Vogel, J.5
  • 136
    • 34249777280 scopus 로고    scopus 로고
    • The small RNA RyhB activates the translation of shiA mRNA encoding a permease of shikimate, a compound involved in siderophore synthesis
    • Prévost K, Salvail H, Desnoyers G, Jacques JF, Phaneuf E, Massé E. (2007). The small RNA RyhB activates the translation of shiA mRNA encoding a permease of shikimate, a compound involved in siderophore synthesis. Mol Microbiol, 64, 1260-1273.
    • (2007) Mol Microbiol , vol.64 , pp. 1260-1273
    • Prévost, K.1    Salvail, H.2    Desnoyers, G.3    Jacques, J.F.4    Phaneuf, E.5    Massé, E.6
  • 137
    • 79960623040 scopus 로고    scopus 로고
    • The Sm-like RNA chaperone Hfq mediates transcription antitermination at Rho-dependent terminators
    • Rabhi M, Espéli O, Schwartz A, Cayrol B, Rahmouni AR, Arluison V, Boudvillain M. (2011). The Sm-like RNA chaperone Hfq mediates transcription antitermination at Rho-dependent terminators. EMBO J, 30, 2805-2816.
    • (2011) EMBO J , vol.30 , pp. 2805-2816
    • Rabhi, M.1    Espéli, O.2    Schwartz, A.3    Cayrol, B.4    Rahmouni, A.R.5    Arluison, V.6    Boudvillain, M.7
  • 138
    • 80052526246 scopus 로고    scopus 로고
    • Genome-wide detection of novel regulatory RNAs in E. coli
    • Raghavan R, Groisman EA, Ochman H. (2011). Genome-wide detection of novel regulatory RNAs in E. coli. Genome Res, 21, 1487-1497.
    • (2011) Genome Res , vol.21 , pp. 1487-1497
    • Raghavan, R.1    Groisman, E.A.2    Ochman, H.3
  • 139
    • 79952810034 scopus 로고    scopus 로고
    • The second RNA chaperone, Hfq2, is also required for survival under stress and full virulence of Burkholderia cenocepacia J2315
    • Ramos CG, Sousa SA, Grilo AM, Feliciano JR, Leitão JH. (2011). The second RNA chaperone, Hfq2, is also required for survival under stress and full virulence of Burkholderia cenocepacia J2315. J Bacteriol, 193, 1515-1526.
    • (2011) J Bacteriol , vol.193 , pp. 1515-1526
    • Ramos, C.G.1    Sousa, S.A.2    Grilo, A.M.3    Feliciano, J.R.4    Leitão, J.H.5
  • 140
    • 0032702842 scopus 로고    scopus 로고
    • The Brucella abortus host factor i (HF-I) protein contributes to stress resistance during stationary phase and is a major determinant of virulence in mice
    • Robertson GT, Roop RM Jr. (1999). The Brucella abortus host factor I (HF-I) protein contributes to stress resistance during stationary phase and is a major determinant of virulence in mice. Mol Microbiol, 34, 690-700.
    • (1999) Mol Microbiol , vol.34 , pp. 690-700
    • Robertson, G.T.1    Roop Jr., R.M.2
  • 141
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N, Nei M. (1987). The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol, 4, 406-425.
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 142
    • 77958563236 scopus 로고    scopus 로고
    • An upstream Hfq binding site in the fhlA mRNA leader region facilitates the OxyS-fhlA interaction
    • Salim NN, Feig AL. (2010). An upstream Hfq binding site in the fhlA mRNA leader region facilitates the OxyS-fhlA interaction. PLoS ONE, 5, pii: e13028.
    • (2010) PLoS ONE , vol.5
    • Salim, N.N.1    Feig, A.L.2
  • 143
  • 144
    • 80051962605 scopus 로고    scopus 로고
    • Structural basis for RNA 3′-end recognition by Hfq
    • Sauer E, 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
  • 145
    • 0242380623 scopus 로고    scopus 로고
    • Sm-like proteins in Eubacteria: The crystal structure of the Hfq protein from Escherichia coli
    • Sauter C, Basquin J, 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
  • 146
    • 77951226115 scopus 로고    scopus 로고
    • The small RNA chaperone Hfq is required for the virulence of Yersinia pseudotuberculosis
    • Schiano CA, Bellows LE, Lathem WW. (2010). The small RNA chaperone Hfq is required for the virulence of Yersinia pseudotuberculosis. Infect Immun, 78, 2034-2044.
    • (2010) Infect Immun , vol.78 , pp. 2034-2044
    • Schiano, C.A.1    Bellows, L.E.2    Lathem, W.W.3
  • 147
    • 68949147832 scopus 로고    scopus 로고
    • The Acinetobacter baylyi Hfq gene encodes a large protein with an unusual C terminus
    • Schilling D, Gerischer U. (2009). The Acinetobacter baylyi Hfq gene encodes a large protein with an unusual C terminus. J Bacteriol, 191, 5553-5562.
    • (2009) J Bacteriol , vol.191 , pp. 5553-5562
    • Schilling, D.1    Gerischer, U.2
  • 149
    • 0036645689 scopus 로고    scopus 로고
    • Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: A bacterial Sm-like protein
    • Schumacher MA, Pearson RF, Møller T, Valentin-Hansen P, Brennan RG. (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    Møller, T.3    Valentin-Hansen, P.4    Brennan, R.G.5
  • 150
    • 0030886280 scopus 로고    scopus 로고
    • Altered 3′-terminal RNA structure in phage Qbeta adapted to host factor-less Escherichia coli
    • Schuppli D, Miranda G, Tsui HC, Winkler ME, Sogo JM, Weber H. (1997). Altered 3′-terminal RNA structure in phage Qbeta adapted to host factor-less Escherichia coli. Proc Natl Acad Sci USA, 94, 10239-10242.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10239-10242
    • Schuppli, D.1    Miranda, G.2    Tsui, H.C.3    Winkler, M.E.4    Sogo, J.M.5    Weber, H.6
  • 151
    • 0017227834 scopus 로고
    • Site-specific interaction of Qbeta host factor and ribosomal protein S1 with Qbeta and R17 bacteriophage RNAs
    • Senear AW, Steitz JA. (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
  • 152
    • 35948970194 scopus 로고    scopus 로고
    • A small RNA regulates multiple ABC transporter mRNAs by targeting C/A-rich elements inside and upstream of ribosome-binding sites
    • Sharma CM, Darfeuille F, Plantinga TH, Vogel J. (2007). A small RNA regulates multiple ABC transporter mRNAs by targeting C/A-rich elements inside and upstream of ribosome-binding sites. Genes Dev, 21, 2804-2817.
    • (2007) Genes Dev , vol.21 , pp. 2804-2817
    • Sharma, C.M.1    Darfeuille, F.2    Plantinga, T.H.3    Vogel, J.4
  • 154
    • 70449566969 scopus 로고    scopus 로고
    • Toward understanding the function of the universally conserved GTPase HflX from Escherichia coli: A kinetic approach
    • Shields MJ, Fischer JJ, Wieden HJ. (2009). Toward understanding the function of the universally conserved GTPase HflX from Escherichia coli: a kinetic approach. Biochemistry, 48, 10793-10802.
    • (2009) Biochemistry , vol.48 , pp. 10793-10802
    • Shields, M.J.1    Fischer, J.J.2    Wieden, H.J.3
  • 156
    • 33845713571 scopus 로고    scopus 로고
    • The RNA chaperone Hfq is essential for the virulence of Salmonella typhimurium
    • Sittka A, Pfeiffer V, Tedin K, 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
  • 157
    • 67349278437 scopus 로고    scopus 로고
    • Deep sequencing of Salmonella RNA associated with heterologous Hfq proteins in vivo reveals small RNAs as a major target class and identifies RNA processing phenotypes
    • Sittka A, Sharma CM, Rolle K, Vogel J. (2009). Deep sequencing of Salmonella RNA associated with heterologous Hfq proteins in vivo reveals small RNAs as a major target class and identifies RNA processing phenotypes. RNA Biol, 6, 266-275.
    • (2009) RNA Biol , vol.6 , pp. 266-275
    • Sittka, A.1    Sharma, C.M.2    Rolle, K.3    Vogel, J.4
  • 158
    • 0035104707 scopus 로고    scopus 로고
    • Hfq is necessary for regulation by the untranslated RNA DsrA
    • Sledjeski DD, Whitman C, Zhang A. (2001). Hfq is necessary for regulation by the untranslated RNA DsrA. J Bacteriol, 183, 1997-2005.
    • (2001) J Bacteriol , vol.183 , pp. 1997-2005
    • Sledjeski, D.D.1    Whitman, C.2    Zhang, A.3
  • 159
    • 80054716344 scopus 로고    scopus 로고
    • Evidences of autoregulation of hfq expression in Sinorhizobium meliloti strain 2011
    • Sobrero P, 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
  • 160
    • 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, Nakamura K. (2011). 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.
    • (2011) 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
  • 162
    • 0036129690 scopus 로고    scopus 로고
    • Functional replacement of the Escherichia coli hfq gene by the homologue of Pseudomonas aeruginosa
    • Sonnleitner E, Moll I, Bläsi U. (2002). Functional replacement of the Escherichia coli hfq gene by the homologue of Pseudomonas aeruginosa. Microbiology (Reading, Engl), 148, 883-891.
    • (2002) Microbiology (Reading, Engl) , vol.148 , pp. 883-891
    • Sonnleitner, E.1    Moll, I.2    Bläsi, U.3
  • 164
    • 79960441320 scopus 로고    scopus 로고
    • Major role for mRNA binding and restructuring in sRNA recruitment by Hfq
    • Soper TJ, Doxzen K, Woodson SA. (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
  • 165
    • 50649097486 scopus 로고    scopus 로고
    • The rpoS mRNA leader recruits Hfq to facilitate annealing with DsrA sRNA
    • Soper TJ, Woodson SA. (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
  • 166
    • 33845365065 scopus 로고    scopus 로고
    • Distinct and overlapping binding sites of Pseudomonas aeruginosa Hfq and RsmA proteins on the non-coding RNA RsmY
    • Sorger-Domenigg T, Sonnleitner E, Kaberdin VR, Bläsi U. (2007). Distinct and overlapping binding sites of Pseudomonas aeruginosa Hfq and RsmA proteins on the non-coding RNA RsmY. Biochem Biophys Res Commun, 352, 769-773.
    • (2007) Biochem Biophys Res Commun , vol.352 , pp. 769-773
    • Sorger-Domenigg, T.1    Sonnleitner, E.2    Kaberdin, V.R.3    Bläsi, U.4
  • 167
    • 77749301868 scopus 로고    scopus 로고
    • The hfq gene is required for stress resistance and full virulence of Burkholderia cepacia to the nematode Caenorhabditis elegans
    • Sousa SA, Ramos CG, Moreira LM, Leitão JH. (2010). The hfq gene is required for stress resistance and full virulence of Burkholderia cepacia to the nematode Caenorhabditis elegans. Microbiology (Reading, Engl), 156, 896-908.
    • (2010) Microbiology (Reading, Engl) , vol.156 , pp. 896-908
    • Sousa, S.A.1    Ramos, C.G.2    Moreira, L.M.3    Leitão, J.H.4
  • 168
    • 0037709369 scopus 로고    scopus 로고
    • Interaction of Escherichia coli RNA polymerase with the ribosomal protein S1 and the Sm-like ATPase Hfq
    • Sukhodolets MV, Garges S. (2003). Interaction of Escherichia coli RNA polymerase with the ribosomal protein S1 and the Sm-like ATPase Hfq. Biochemistry, 42, 8022-8034.
    • (2003) Biochemistry , vol.42 , pp. 8022-8034
    • Sukhodolets, M.V.1    Garges, S.2
  • 169
    • 33645939935 scopus 로고    scopus 로고
    • Escherichia coli Hfq binds A18 and DsrA domain II with similar 2:1 Hfq6/RNA stoichiometry using different surface sites
    • Sun X, Wartell RM. (2006). Escherichia coli Hfq binds A18 and DsrA domain II with similar 2:1 Hfq6/RNA stoichiometry using different surface sites. Biochemistry, 45, 4875-4887.
    • (2006) Biochemistry , vol.45 , pp. 4875-4887
    • Sun, X.1    Wartell, R.M.2
  • 170
    • 0036714801 scopus 로고    scopus 로고
    • Predicted structure and phyletic distribution of the RNA-binding protein Hfq
    • Sun X, Zhulin I, Wartell RM. (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
  • 174
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K, Peterson D, Peterson N, Stecher G, Nei M, Kumar S. (2011). MEGA5: Molecular Evolutionary Genetics Analysis using Maximum Likelihood, Evolutionary Distance, and Maximum Parsimony Methods. Mol Biol Evol, 28, 2731-2739.
    • (2011) Mol Biol Evol , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 175
    • 82655181911 scopus 로고    scopus 로고
    • Intrinsic disorder in cell signaling and gene transcription
    • Tantos A, Han KH, Tompa P. (2012). Intrinsic disorder in cell signaling and gene transcription. Mol Cell Endocrinol, 348, 457-465.
    • (2012) Mol Cell Endocrinol , vol.348 , pp. 457-465
    • Tantos, A.1    Han, K.H.2    Tompa, P.3
  • 176
    • 22444439358 scopus 로고    scopus 로고
    • A-tract clusters may facilitate DNA packaging in bacterial nucleoid
    • Tolstorukov MY, Virnik KM, Adhya S, Zhurkin VB. (2005). A-tract clusters may facilitate DNA packaging in bacterial nucleoid. Nucleic Acids Res, 33, 3907-3918.
    • (2005) Nucleic Acids Res , vol.33 , pp. 3907-3918
    • Tolstorukov, M.Y.1    Virnik, K.M.2    Adhya, S.3    Zhurkin, V.B.4
  • 178
    • 0029824724 scopus 로고    scopus 로고
    • Transcription of the mutL repair, miaA tRNA modification, hfq pleiotropic regulator, and hflA region protease genes of Escherichia coli K-12 from clustered Esigma32-specific promoters during heat shock
    • Tsui HC, Feng G, Winkler ME. (1996). Transcription of the mutL repair, miaA tRNA modification, hfq pleiotropic regulator, and hflA region protease genes of Escherichia coli K-12 from clustered Esigma32-specific promoters during heat shock. J Bacteriol, 178, 5719-5731.
    • (1996) J Bacteriol , vol.178 , pp. 5719-5731
    • Tsui, H.C.1    Feng, G.2    Winkler, M.E.3
  • 179
    • 0028243445 scopus 로고
    • Characterization of broadly pleiotropic phenotypes caused by an hfq insertion mutation in Escherichia coli K-12
    • Tsui HC, Leung HC, Winkler ME. (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
  • 180
    • 73849125970 scopus 로고    scopus 로고
    • Identification and characterization of noncoding small RNAs in Streptococcus pneumoniae serotype 2 strain D39
    • Tsui HC, Mukherjee D, Ray VA, Sham LT, Feig AL, Winkler ME. (2010). Identification and characterization of noncoding small RNAs in Streptococcus pneumoniae serotype 2 strain D39. J Bacteriol, 192, 264-279.
    • (2010) J Bacteriol , vol.192 , pp. 264-279
    • Tsui, H.C.1    Mukherjee, D.2    Ray, V.A.3    Sham, L.T.4    Feig, A.L.5    Winkler, M.E.6
  • 181
    • 0028652278 scopus 로고
    • Transcriptional patterns of the mutLmiaA superoperon of Escherichia coli K-12 suggest a model for posttranscriptional regulation
    • Tsui HC, Winkler ME. (1994). Transcriptional patterns of the mutLmiaA superoperon of Escherichia coli K-12 suggest a model for posttranscriptional regulation. Biochimie, 76, 1168-1177.
    • (1994) Biochimie , vol.76 , pp. 1168-1177
    • Tsui, H.C.1    Winkler, M.E.2
  • 182
    • 79951540365 scopus 로고    scopus 로고
    • The stoichiometry of the Escherichia coli Hfq protein bound to RNA
    • Updegrove TB, Correia JJ, Chen Y, Terry C, Wartell RM. (2011). The stoichiometry of the Escherichia coli Hfq protein bound to RNA. RNA, 17, 489-500.
    • (2011) RNA , vol.17 , pp. 489-500
    • Updegrove, T.B.1    Correia, J.J.2    Chen, Y.3    Terry, C.4    Wartell, R.M.5
  • 183
    • 77955663530 scopus 로고    scopus 로고
    • E. coli DNA associated with isolated Hfq interacts with Hfq's distal surface and C-terminal domain
    • Updegrove TB, Correia JJ, Galletto R, Bujalowski W, Wartell RM. (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
  • 184
    • 80053440900 scopus 로고    scopus 로고
    • The influence of Escherichia coli Hfq mutations on RNA binding and sRNA•mRNA duplex formation in rpoS riboregulation
    • Updegrove TB, Wartell RM. (2011). The influence of Escherichia coli Hfq mutations on RNA binding and sRNA•mRNA duplex formation in rpoS riboregulation. Biochim Biophys Acta, 1809, 532-540.
    • (2011) Biochim Biophys Acta , vol.1809 , pp. 532-540
    • Updegrove, T.B.1    Wartell, R.M.2
  • 185
    • 1642565815 scopus 로고    scopus 로고
    • The bacterial Sm-like protein Hfq: A key player in RNA transactions
    • Valentin-Hansen P, Eriksen M, 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
  • 187
    • 8544271637 scopus 로고    scopus 로고
    • Involvement of a novel transcriptional activator and small RNA in post-transcriptional regulation of the glucose phosphoenolpyruvate phosphotransferase system
    • Vanderpool CK, Gottesman S. (2004). Involvement of a novel transcriptional activator and small RNA in post-transcriptional regulation of the glucose phosphoenolpyruvate phosphotransferase system. Mol Microbiol, 54, 1076-1089.
    • (2004) Mol Microbiol , vol.54 , pp. 1076-1089
    • Vanderpool, C.K.1    Gottesman, S.2
  • 188
    • 77950345032 scopus 로고    scopus 로고
    • Translational activation of rpoS mRNA by the non-coding RNA DsrA and Hfq does not require ribosome binding
    • Vecerek B, Beich-Frandsen M, Resch A, Bläsi U. (2010). Translational activation of rpoS mRNA by the non-coding RNA DsrA and Hfq does not require ribosome binding. Nucleic Acids Res, 38, 1284-1293.
    • (2010) Nucleic Acids Res , vol.38 , pp. 1284-1293
    • Vecerek, B.1    Beich-Frandsen, M.2    Resch, A.3    Bläsi, U.4
  • 189
    • 21844476794 scopus 로고    scopus 로고
    • Translational autocontrol of the Escherichia coli hfq RNA chaperone gene
    • Vecerek B, Moll I, Bläsi 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    Bläsi, U.3
  • 191
    • 4344673615 scopus 로고    scopus 로고
    • Lsm proteins promote regeneration of pre-mRNA splicing activity
    • Verdone L, Galardi S, Page D, Beggs JD. (2004). Lsm proteins promote regeneration of pre-mRNA splicing activity. Curr Biol, 14, 1487-1491.
    • (2004) Curr Biol , vol.14 , pp. 1487-1491
    • Verdone, L.1    Galardi, S.2    Page, D.3    Beggs, J.D.4
  • 192
    • 0030959071 scopus 로고    scopus 로고
    • High-mobility group (HMG) protein HMG-1 and TATAbinding protein-associated factor TAF(II)30 affect estrogen receptor-mediated transcriptional activation
    • Verrier CS, Roodi N, Yee CJ, Bailey LR, Jensen RA, Bustin M, Parl FF. (1997). High-mobility group (HMG) protein HMG-1 and TATAbinding protein-associated factor TAF(II)30 affect estrogen receptor-mediated transcriptional activation. Mol Endocrinol, 11, 1009-1019.
    • (1997) Mol Endocrinol , vol.11 , pp. 1009-1019
    • Verrier, C.S.1    Roodi, N.2    Yee, C.J.3    Bailey, L.R.4    Jensen, R.A.5    Bustin, M.6    Parl, F.F.7
  • 193
    • 57349181413 scopus 로고    scopus 로고
    • Regulating the regulators: How ribonucleases dictate the rules in the control of small non-coding RNAs
    • Viegas SC, Arraiano CM. (2008). Regulating the regulators: How ribonucleases dictate the rules in the control of small non-coding RNAs. RNA Biol, 5, 230-243.
    • (2008) RNA Biol , vol.5 , pp. 230-243
    • Viegas, S.C.1    Arraiano, C.M.2
  • 195
    • 79960433506 scopus 로고    scopus 로고
    • Hfq and its constellation of RNA
    • Vogel J, Luisi BF. (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
  • 196
    • 0032564363 scopus 로고    scopus 로고
    • Host factor I, Hfq, binds to Escherichia coli ompA mRNA in a growth rate-dependent fashion and regulates its stability
    • Vytvytska O, Jakobsen JS, Balcunaite G, Andersen JS, Baccarini M, von Gabain A. (1998). Host factor I, Hfq, binds to Escherichia coli ompA mRNA in a growth rate-dependent fashion and regulates its stability. Proc Natl Acad Sci USA, 95, 14118-14123.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 14118-14123
    • Vytvytska, O.1    Jakobsen, J.S.2    Balcunaite, G.3    Andersen, J.S.4    Baccarini, M.5    Von Gabain, A.6
  • 197
    • 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, 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
  • 198
    • 0029073396 scopus 로고
    • Transcription termination at intrinsic terminators: The role of the RNA hairpin
    • Wilson KS, von Hippel PH. (1995). Transcription termination at intrinsic terminators: the role of the RNA hairpin. Proc Natl Acad Sci USA, 92, 8793-8797.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8793-8797
    • Wilson, K.S.1    Von Hippel, P.H.2
  • 199
    • 85046912592 scopus 로고    scopus 로고
    • Isolation of small RNA-binding proteins from E. coli: Evidence for frequent interaction of RNAs with RNA polymerase
    • Windbichler N, von Pelchrzim F, Mayer O, Csaszar E, Schroeder R. (2008). Isolation of small RNA-binding proteins from E. coli: evidence for frequent interaction of RNAs with RNA polymerase. RNA Biol, 5, 30-40.
    • (2008) RNA Biol , vol.5 , pp. 30-40
    • Windbichler, N.1    Von Pelchrzim, F.2    Mayer, O.3    Csaszar, E.4    Schroeder, R.5
  • 200
    • 77954360442 scopus 로고    scopus 로고
    • Effect of the hfq gene on 2,4-diacetylphloroglucinol production and the PcoI/PcoR quorum-sensing system in Pseudomonas fluorescens 2P24
    • Wu XG, Duan HM, Tian T, Yao N, Zhou HY, Zhang LQ. (2010). Effect of the hfq gene on 2,4-diacetylphloroglucinol production and the PcoI/PcoR quorum-sensing system in Pseudomonas fluorescens 2P24. FEMS Microbiol Lett, 309, 16-24.
    • (2010) FEMS Microbiol Lett , vol.309 , pp. 16-24
    • Wu, X.G.1    Duan, H.M.2    Tian, T.3    Yao, N.4    Zhou, H.Y.5    Zhang, L.Q.6
  • 201
    • 18144402771 scopus 로고    scopus 로고
    • Reconstitution of two recombinant LSm protein complexes reveals aspects of their architecture, assembly, and function
    • Zaric B, Chami M, Rémigy H, Engel A, Ballmer-Hofer K, Winkler FK, Kambach C. (2005). Reconstitution of two recombinant LSm protein complexes reveals aspects of their architecture, assembly, and function. J Biol Chem, 280, 16066-16075.
    • (2005) J Biol Chem , vol.280 , pp. 16066-16075
    • Zaric, B.1    Chami, M.2    Rémigy, H.3    Engel, A.4    Ballmer-Hofer, K.5    Winkler, F.K.6    Kambach, C.7
  • 202
    • 0036163624 scopus 로고    scopus 로고
    • The Sm-like Hfq protein increases OxyS RNA interaction with target mRNAs
    • Zhang A, Wassarman KM, Ortega J, Steven AC, Storz G. (2002). The Sm-like Hfq protein increases OxyS RNA interaction with target mRNAs. Mol Cell, 9, 11-22.
    • (2002) Mol Cell , vol.9 , pp. 11-22
    • Zhang, A.1    Wassarman, K.M.2    Ortega, J.3    Steven, A.C.4    Storz, G.5
  • 204
    • 73349140525 scopus 로고    scopus 로고
    • Post-transcriptional regulation of NifA expression by Hfq and RNase e complex in Rhizobium leguminosarum bv. viciae
    • Zhang Y, Hong G. (2009). Post-transcriptional regulation of NifA expression by Hfq and RNase E complex in Rhizobium leguminosarum bv. viciae. Acta Biochim Biophys Sin (Shanghai), 41, 719-730.
    • (2009) Acta Biochim Biophys Sin (Shanghai) , vol.41 , pp. 719-730
    • Zhang, Y.1    Hong, G.2


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