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Volumn 10, Issue 4, 2013, Pages 610-618

Structure and RNA-binding properties of the bacterial LSm protein Hfq

Author keywords

3 end recognition; Crystal structure; Gene regulation; LSm ring; Non coding RNAs; Prokaryotes; RNA chaperone; RNA degradation

Indexed keywords

BACTERIAL PROTEIN; HFQ PROTEIN; MESSENGER RNA; PROTEIN SM; RNA; SMALL UNTRANSLATED RNA; UNCLASSIFIED DRUG;

EID: 84879005493     PISSN: 15476286     EISSN: 15558584     Source Type: Journal    
DOI: 10.4161/rna.24201     Document Type: Review
Times cited : (77)

References (99)
  • 1
    • 60149089144 scopus 로고    scopus 로고
    • Regulatory RNAs in bacteria
    • PMID:19239884
    • Waters LS, Storz G. Regulatory RNAs in bacteria. Cell 2009; 136:615-28; PMID:19239884; http://dx.doi.org/10.1016/j.cell.2009.01.043.
    • (2009) Cell , vol.136 , pp. 615-628
    • Waters, L.S.1    Storz, G.2
  • 2
    • 84863924309 scopus 로고    scopus 로고
    • Bacterial small RNA regulators: Versatile roles and rapidly evolving variations
    • PMID:20980440
    • Gottesman S, Storz G. Bacterial small RNA regulators: versatile roles and rapidly evolving variations. Cold Spring Harb Perspect Biol 2011; 3; PMID:20980440; http://dx.doi.org/10.1101/cshperspect.a003798.
    • (2011) Cold Spring Harb Perspect Biol , vol.3
    • Gottesman, S.1    Storz, G.2
  • 3
    • 67349192582 scopus 로고    scopus 로고
    • Multiple target regulation by small noncoding RNAs rewires gene expression at the post-transcriptional level
    • PMID:19366629
    • Papenfort K, Vogel J. Multiple target regulation by small noncoding RNAs rewires gene expression at the post-transcriptional level. Res Microbiol 2009; 160:278-87; PMID:19366629; http://dx.doi.org/10.1016/j.resmic.2009.03.004.
    • (2009) Res Microbiol , vol.160 , pp. 278-287
    • Papenfort, K.1    Vogel, J.2
  • 4
    • 80053019485 scopus 로고    scopus 로고
    • Regulation by small RNAs in bacteria: Expanding frontiers
    • PMID:21925377
    • Storz G, Vogel J, Wassarman KM. Regulation by small RNAs in bacteria: expanding frontiers. Mol Cell 2011; 43:880-91; PMID:21925377; http://dx.doi.org/10.1016/j.molcel.2011.08.022.
    • (2011) Mol Cell , vol.43 , pp. 880-891
    • Storz, G.1    Vogel, J.2    Wassarman, K.M.3
  • 5
    • 79960433506 scopus 로고    scopus 로고
    • Hfq and its constellation of RNA
    • PMID:21760622
    • Vogel J, Luisi BF. Hfq and its constellation of RNA. Nat Rev Microbiol 2011; 9:578-89; PMID:21760622; http://dx.doi.org/10.1038/nrmicro2615.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 578-589
    • Vogel, J.1    Luisi, B.F.2
  • 6
    • 0036645689 scopus 로고    scopus 로고
    • Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: A bacterial Sm-like protein
    • PMID:12093755
    • Schumacher MA, Pearson RF, Møller T, Valentin-Hansen P, Brennan RG. Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: a bacterial Sm-like protein. EMBO J 2002; 21:3546-56; PMID:12093755; http://dx.doi.org/10.1093/emboj/cdf322.
    • (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
  • 7
    • 72049095718 scopus 로고    scopus 로고
    • Structure of Escherichia coli Hfq bound to polyriboadenylate RNA
    • PMID:19889981
    • Link TM, Valentin-Hansen P, Brennan RG. Structure of Escherichia coli Hfq bound to polyriboadenylate RNA. Proc Natl Acad Sci USA 2009; 106:19292-7; PMID:19889981; http://dx.doi.org/10.1073/pnas.0908744106.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 19292-19297
    • Link, T.M.1    Valentin-Hansen, P.2    Brennan, R.G.3
  • 8
    • 16544365115 scopus 로고    scopus 로고
    • Escherichia coli Hfq has distinct interaction surfaces for DsrA, rpoS and poly(A) RNAs
    • PMID:15531892
    • Mikulecky PJ, Kaw MK, Brescia CC, Takach JC, Sledjeski DD, Feig AL. Escherichia coli Hfq has distinct interaction surfaces for DsrA, rpoS and poly(A) RNAs. Nat Struct Mol Biol 2004; 11:1206-14; PMID:15531892; http://dx.doi.org/10.1038/nsmb858.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 1206-1214
    • Mikulecky, P.J.1    Kaw, M.K.2    Brescia, C.C.3    Takach, J.C.4    Sledjeski, D.D.5    Feig, A.L.6
  • 9
    • 80051962605 scopus 로고    scopus 로고
    • Structural basis for RNA 3′-end recognition by Hfq
    • PMID:21737752
    • Sauer E, Weichenrieder O. Structural basis for RNA 3′-end recognition by Hfq. Proc Natl Acad Sci USA 2011; 108:13065-70; PMID:21737752; http://dx.doi.org/10.1073/pnas.1103420108.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 13065-13070
    • Sauer, E.1    Weichenrieder, O.2
  • 10
    • 80051973174 scopus 로고    scopus 로고
    • PolyU tail of rho-independent terminator of bacterial small RNAs is essential for Hfq action
    • PMID:21788484
    • Otaka H, Ishikawa H, Morita T, Aiba H. PolyU tail of rho-independent terminator of bacterial small RNAs is essential for Hfq action. Proc Natl Acad Sci USA 2011; 108:13059-64; PMID:21788484; http://dx.doi.org/10.1073/pnas. 1107050108.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 13059-13064
    • Otaka, H.1    Ishikawa, H.2    Morita, T.3    Aiba, H.4
  • 11
    • 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
    • PMID:22454537
    • Ishikawa H, Otaka H, Maki K, Morita T, Aiba H. 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 2012; 18:1062-74; PMID:22454537; http://dx.doi.org/10.1261/rna.031575.111.
    • (2012) RNA , vol.18 , pp. 1062-1074
    • Ishikawa, H.1    Otaka, H.2    Maki, K.3    Morita, T.4    Aiba, H.5
  • 12
    • 84862232515 scopus 로고    scopus 로고
    • Small RNA binding to the lateral surface of Hfq hexamers and structural rearrangements upon mRNA target recognition
    • PMID:22645344
    • Sauer E, Schmidt S, Weichenrieder O. Small RNA binding to the lateral surface of Hfq hexamers and structural rearrangements upon mRNA target recognition. Proc Natl Acad Sci USA 2012; 109:9396-401; PMID:22645344; http://dx.doi.org/10.1073/pnas.1202521109.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 9396-9401
    • Sauer, E.1    Schmidt, S.2    Weichenrieder, O.3
  • 13
    • 0014409656 scopus 로고
    • Factor fraction required for the synthesis of bacteriophage Qbeta-RNA
    • PMID:4874917
    • Franze de Fernandez MT, Eoyang L, August JT. Factor fraction required for the synthesis of bacteriophage Qbeta-RNA. Nature 1968; 219:588-90; PMID:4874917; http://dx.doi.org/10.1038/219588a0.
    • (1968) Nature , vol.219 , pp. 588-590
    • Franze De Fernandez, M.T.1    Eoyang, L.2    August, J.T.3
  • 14
    • 0015500282 scopus 로고
    • Bacterial proteins required for replication of phage Q ribonucleic acid. Pruification and properties of host factor I, a ribonucleic acid-binding protein
    • PMID:4550762
    • Franze de Fernandez MT, Hayward WS, August JT. Bacterial proteins required for replication of phage Q ribonucleic acid. Pruification and properties of host factor I, a ribonucleic acid-binding protein. J Biol Chem 1972; 247:824-31; PMID:4550762.
    • (1972) J Biol Chem , vol.247 , pp. 824-831
    • Franze De Fernandez, M.T.1    Hayward, W.S.2    August, J.T.3
  • 15
    • 0027282394 scopus 로고
    • Different mechanisms of recognition of bacteriophage Q beta plus and minus strand RNAs by Q beta replicase
    • PMID:8345521
    • Barrera I, Schuppli D, Sogo JM, Weber H. Different mechanisms of recognition of bacteriophage Q beta plus and minus strand RNAs by Q beta replicase. J Mol Biol 1993; 232:512-21; PMID:8345521; http://dx.doi.org/10.1006/ jmbi.1993.1407.
    • (1993) J Mol Biol , vol.232 , pp. 512-521
    • Barrera, I.1    Schuppli, D.2    Sogo, J.M.3    Weber, H.4
  • 16
    • 0031576897 scopus 로고    scopus 로고
    • Recognition of bacteriophage Qbeta plus strand RNA as a template by Qbeta replicase: Role of RNA interactions mediated by ribosomal proteins S1 and host factor
    • PMID:9150398
    • Miranda G, Schuppli D, Barrera I, Hausherr C, Sogo JM, Weber H. Recognition of bacteriophage Qbeta plus strand RNA as a template by Qbeta replicase: role of RNA interactions mediated by ribosomal proteins S1 and host factor. J Mol Biol 1997; 267:1089-103; PMID:9150398; http://dx.doi.org/10.1006/ jmbi.1997.0939.
    • (1997) J Mol Biol , vol.267 , pp. 1089-1103
    • Miranda, G.1    Schuppli, D.2    Barrera, I.3    Hausherr, C.4    Sogo, J.M.5    Weber, H.6
  • 17
    • 0347519274 scopus 로고    scopus 로고
    • The poly(A) binding protein Hfq protects RNA from RNase E and exoribonucleolytic degradation
    • PMID:14654705
    • Folichon M, Arluison V, Pellegrini O, Huntzinger E, Régnier P, Hajnsdorf E. The poly(A) binding protein Hfq protects RNA from RNase E and exoribonucleolytic degradation. Nucleic Acids Res 2003; 31:7302-10; PMID:14654705; http://dx.doi.org/10.1093/nar/gkg915.
    • (2003) Nucleic Acids Res , vol.31 , pp. 7302-7310
    • Folichon, M.1    Arluison, V.2    Pellegrini, O.3    Huntzinger, E.4    Régnier, P.5    Hajnsdorf, E.6
  • 18
    • 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
    • PMID:15654883
    • Folichon M, Allemand F, Régnier P, Hajnsdorf E. Stimulation of poly(A) synthesis by Escherichia coli poly(A)polymerase I is correlated with Hfq binding to poly(A) tails. FEBS J 2005; 272:454-63; PMID:15654883; http://dx.doi.org/10.1111/j.1742-4658.2004.04485.x.
    • (2005) FEBS J , vol.272 , pp. 454-463
    • Folichon, M.1    Allemand, F.2    Régnier, P.3    Hajnsdorf, E.4
  • 19
    • 7044285063 scopus 로고    scopus 로고
    • The Sm-like protein Hfq regulates polyadenylation dependent mRNA decay in Escherichia coli
    • PMID:15522076
    • Mohanty BK, Maples VF, Kushner SR. The Sm-like protein Hfq regulates polyadenylation dependent mRNA decay in Escherichia coli. Mol Microbiol 2004; 54:905-20; PMID:15522076; http://dx.doi.org/10.1111/j.1365-2958.2004.04337.x.
    • (2004) Mol Microbiol , vol.54 , pp. 905-920
    • Mohanty, B.K.1    Maples, V.F.2    Kushner, S.R.3
  • 20
    • 0242380640 scopus 로고    scopus 로고
    • Hfq affects the length and the frequency of short oligo(A) tails at the 3′ end of Escherichia coli rpsO mRNAs
    • PMID:12853618
    • Le Derout J, Folichon M, Briani F, Dehò G, Régnier P, Hajnsdorf E. Hfq affects the length and the frequency of short oligo(A) tails at the 3′ end of Escherichia coli rpsO mRNAs. Nucleic Acids Res 2003; 31:4017-23; PMID:12853618; http://dx.doi.org/10.1093/nar/gkg456.
    • (2003) Nucleic Acids Res , vol.31 , pp. 4017-4023
    • Le Derout, J.1    Folichon, M.2    Briani, F.3    Dehò, G.4    Régnier, P.5    Hajnsdorf, E.6
  • 21
    • 0344389019 scopus 로고    scopus 로고
    • E. coli RpsO mRNA decay: RNase E processing at the beginning of the coding sequence stimulates poly(A)-dependent degradation of the mRNA
    • PMID:10047480
    • Hajnsdorf E, Régnier PE. E. coli RpsO mRNA decay: RNase E processing at the beginning of the coding sequence stimulates poly(A)-dependent degradation of the mRNA. J Mol Biol 1999; 286:1033-43; PMID:10047480; http://dx.doi.org/10.1006/jmbi.1999.2547.
    • (1999) J Mol Biol , vol.286 , pp. 1033-1043
    • Hajnsdorf, E.1    Régnier, P.E.2
  • 22
    • 0034652188 scopus 로고    scopus 로고
    • Host factor Hfq of Escherichia coli stimulates elongation of poly(A) tails by poly(A) polymerase I
    • PMID:10677490
    • Hajnsdorf E, Régnier P. Host factor Hfq of Escherichia coli stimulates elongation of poly(A) tails by poly(A) polymerase I. Proc Natl Acad Sci USA 2000; 97:1501-5; PMID:10677490; http://dx.doi.org/10.1073/pnas. 040549897.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1501-1505
    • Hajnsdorf, E.1    Régnier, P.2
  • 23
    • 34247109118 scopus 로고    scopus 로고
    • Hfq structure, function and ligand binding
    • PMID:17395525
    • Brennan RG, Link TM. Hfq structure, function and ligand binding. Curr Opin Microbiol 2007; 10:125-33; PMID:17395525; http://dx.doi.org/10.1016/j.mib. 2007.03.015.
    • (2007) Curr Opin Microbiol , vol.10 , pp. 125-133
    • Brennan, R.G.1    Link, T.M.2
  • 24
    • 51249099359 scopus 로고    scopus 로고
    • Reconstitution and analysis of the multienzyme Escherichia coli RNA degradosome
    • PMID:18691600
    • Worrall JA, Górna M, Crump NT, Phillips LG, Tuck AC, Price AJ, et al. Reconstitution and analysis of the multienzyme Escherichia coli RNA degradosome. J Mol Biol 2008; 382:870-83; PMID:18691600; http://dx.doi.org/10. 1016/j.jmb.2008.07.059.
    • (2008) J Mol Biol , vol.382 , pp. 870-883
    • Worrall, J.A.1    Górna, M.2    Crump, N.T.3    Phillips, L.G.4    Tuck, A.C.5    Price, A.J.6
  • 25
    • 0028243445 scopus 로고
    • Characterization of broadly pleiotropic phenotypes caused by an hfq insertion mutation in Escherichia coli K-12
    • PMID:7984093
    • Tsui HC, Leung HC, Winkler ME. Characterization of broadly pleiotropic phenotypes caused by an hfq insertion mutation in Escherichia coli K-12. Mol Microbiol 1994; 13:35-49; PMID:7984093; http://dx.doi.org/10.1111/j.1365-2958. 1994.tb00400.x.
    • (1994) Mol Microbiol , vol.13 , pp. 35-49
    • Tsui, H.C.1    Leung, H.C.2    Winkler, M.E.3
  • 26
    • 33845713571 scopus 로고    scopus 로고
    • The RNA chaperone Hfq is essential for the virulence of Salmonella typhimurium
    • PMID:17163975
    • Sittka A, Pfeiffer V, Tedin K, Vogel J. The RNA chaperone Hfq is essential for the virulence of Salmonella typhimurium. Mol Microbiol 2007; 63:193-217; PMID:17163975; http://dx.doi.org/10.1111/j.1365-2958.2006.05489.x.
    • (2007) Mol Microbiol , vol.63 , pp. 193-217
    • Sittka, A.1    Pfeiffer, V.2    Tedin, K.3    Vogel, J.4
  • 27
    • 50849105413 scopus 로고    scopus 로고
    • Deep sequencing analysis of small noncoding RNA and mRNA targets of the global post-transcriptional regulator, Hfq
    • PMID:18725932
    • Sittka A, Lucchini S, Papenfort K, Sharma CM, Rolle K, Binnewies TT, et al. Deep sequencing analysis of small noncoding RNA and mRNA targets of the global post-transcriptional regulator, Hfq. PLoS Genet 2008; 4:e1000163; PMID:18725932; http://dx.doi.org/10.1371/journal.pgen.1000163.
    • (2008) PLoS Genet , vol.4
    • Sittka, A.1    Lucchini, S.2    Papenfort, K.3    Sharma, C.M.4    Rolle, K.5    Binnewies, T.T.6
  • 28
    • 0031028155 scopus 로고    scopus 로고
    • The RNA-binding protein HF-I plays a global regulatory role which is largely, but not exclusively, due to its role in expression of the sigmaS subunit of RNA polymerase in Escherichia coli
    • PMID:8982015
    • Muffler A, Traulsen DD, Fischer D, Lange R, Hengge-Aronis R. The RNA-binding protein HF-I plays a global regulatory role which is largely, but not exclusively, due to its role in expression of the sigmaS subunit of RNA polymerase in Escherichia coli. J Bacteriol 1997; 179:297-300; PMID:8982015.
    • (1997) J Bacteriol , vol.179 , pp. 297-300
    • Muffler, A.1    Traulsen, D.D.2    Fischer, D.3    Lange, R.4    Hengge-Aronis, R.5
  • 29
    • 0030711638 scopus 로고    scopus 로고
    • Negative regulation of mutS and mutH repair gene expression by the Hfq and RpoS global regulators of Escherichia coli K-12
    • PMID:9393714
    • Tsui HC, Feng G, Winkler ME. Negative regulation of mutS and mutH repair gene expression by the Hfq and RpoS global regulators of Escherichia coli K-12. J Bacteriol 1997; 179:7476-87; PMID:9393714.
    • (1997) J Bacteriol , vol.179 , pp. 7476-7487
    • Tsui, H.C.1    Feng, G.2    Winkler, M.E.3
  • 30
    • 0034194572 scopus 로고    scopus 로고
    • Hfq (HF1) stimulates ompA mRNA decay by interfering with ribosome binding
    • PMID:10809669
    • Vytvytska O, Moll I, Kaberdin VR, von Gabain A, Bläsi U. Hfq (HF1) stimulates ompA mRNA decay by interfering with ribosome binding. Genes Dev 2000; 14:1109-18; PMID:10809669.
    • (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
  • 31
    • 23944455046 scopus 로고    scopus 로고
    • LSm proteins form heptameric rings that bind to RNA via repeating motifs
    • PMID:16051491
    • Khusial P, Plaag R, Zieve GW. LSm proteins form heptameric rings that bind to RNA via repeating motifs. Trends Biochem Sci 2005; 30:522-8; PMID:16051491; http://dx.doi.org/10.1016/j.tibs.2005.07.006.
    • (2005) Trends Biochem Sci , vol.30 , pp. 522-528
    • Khusial, P.1    Plaag, R.2    Zieve, G.W.3
  • 32
    • 28544442127 scopus 로고    scopus 로고
    • Eukaryotic Lsm proteins: Lessons from bacteria
    • PMID:16327775
    • Wilusz CJ, Wilusz J. Eukaryotic Lsm proteins: lessons from bacteria. Nat Struct Mol Biol 2005; 12:1031-6; PMID:16327775; http://dx.doi.org/10.1038/ nsmb1037.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 1031-1036
    • Wilusz, C.J.1    Wilusz, J.2
  • 33
    • 0035957394 scopus 로고    scopus 로고
    • The Sm domain is an ancient RNA-binding motif with oligo(U) specificity
    • PMID:11259661
    • Achsel T, Stark H, Lührmann R. The Sm domain is an ancient RNA-binding motif with oligo(U) specificity. Proc Natl Acad Sci USA 2001; 98:3685-9; PMID:11259661; http://dx.doi.org/10.1073/pnas.071033998.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 3685-3689
    • Achsel, T.1    Stark, H.2    Lührmann, R.3
  • 34
    • 0242380623 scopus 로고    scopus 로고
    • Sm-like proteins in Eubacteria: The crystal structure of the Hfq protein from Escherichia coli
    • PMID:12853626
    • Sauter C, Basquin J, Suck D. Sm-like proteins in Eubacteria: the crystal structure of the Hfq protein from Escherichia coli. Nucleic Acids Res 2003; 31:4091-8; PMID:12853626; http://dx.doi.org/10.1093/nar/gkg480.
    • (2003) Nucleic Acids Res , vol.31 , pp. 4091-4098
    • Sauter, C.1    Basquin, J.2    Suck, D.3
  • 35
    • 0035826794 scopus 로고    scopus 로고
    • The crystal structure of a heptameric archaeal Sm protein: Implications for the eukaryotic snRNP core
    • PMID:11331747
    • Mura C, Cascio D, Sawaya MR, Eisenberg DS. The crystal structure of a heptameric archaeal Sm protein: Implications for the eukaryotic snRNP core. Proc Natl Acad Sci USA 2001; 98:5532-7; PMID:11331747; http://dx.doi.org/10.1073/ pnas.091102298.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 5532-5537
    • Mura, C.1    Cascio, D.2    Sawaya, M.R.3    Eisenberg, D.S.4
  • 36
    • 36248940726 scopus 로고    scopus 로고
    • An Hfq-like protein in archaea: Crystal structure and functional characterization of the Sm protein from Methanococcus jannaschii
    • PMID:17959927
    • Nielsen JS, Bøggild A, Andersen CB, Nielsen G, Boysen A, Brodersen DE, et al. An Hfq-like protein in archaea: crystal structure and functional characterization of the Sm protein from Methanococcus jannaschii. RNA 2007; 13:2213-23; PMID:17959927; http://dx.doi.org/10.1261/rna.689007.
    • (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
  • 37
    • 0033524941 scopus 로고    scopus 로고
    • Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs
    • PMID:10025403
    • Kambach C, Walke S, Young R, Avis JM, de la Fortelle E, Raker VA, et al. Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs. Cell 1999; 96:375-87; PMID:10025403; http://dx.doi.org/10.1016/S0092-8674(00)80550-4.
    • (1999) Cell , vol.96 , pp. 375-387
    • Kambach, C.1    Walke, S.2    Young, R.3    Avis, J.M.4    De La Fortelle, E.5    Raker, V.A.6
  • 38
    • 63649099704 scopus 로고    scopus 로고
    • Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution
    • PMID:19325628
    • Pomeranz Krummel DA, Oubridge C, Leung AK, Li J, Nagai K. Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution. Nature 2009; 458:475-80; PMID:19325628; http://dx.doi.org/10.1038/nature07851.
    • (2009) Nature , vol.458 , pp. 475-480
    • Pomeranz Krummel, D.A.1    Oubridge, C.2    Leung, A.K.3    Li, J.4    Nagai, K.5
  • 39
    • 79957601559 scopus 로고    scopus 로고
    • Structure of the spliceosomal U4 snRNP core domain and its implication for snRNP biogenesis
    • PMID:21516107
    • Leung AK, Nagai K, Li J. Structure of the spliceosomal U4 snRNP core domain and its implication for snRNP biogenesis. Nature 2011; 473:536-9; PMID:21516107; http://dx.doi.org/10.1038/nature09956.
    • (2011) Nature , vol.473 , pp. 536-539
    • Leung, A.K.1    Nagai, K.2    Li, J.3
  • 40
    • 0035341325 scopus 로고    scopus 로고
    • RNA binding in an Sm core domain: X-ray structure and functional analysis of an archaeal Sm protein complex
    • PMID:11331594
    • Törö I, Thore S, Mayer C, Basquin J, Séraphin B, Suck D. RNA binding in an Sm core domain: X-ray structure and functional analysis of an archaeal Sm protein complex. EMBO J 2001; 20:2293-303; PMID:11331594; http://dx.doi.org/10.1093/emboj/20.9.2293.
    • (2001) EMBO J , vol.20 , pp. 2293-2303
    • Törö, I.1    Thore, S.2    Mayer, C.3    Basquin, J.4    Séraphin, B.5    Suck, D.6
  • 41
    • 1942520321 scopus 로고    scopus 로고
    • The C-terminal domain of Escherichia coli Hfq increases the stability of the hexamer
    • PMID:15030475
    • Arluison V, Folichon M, Marco S, Derreumaux P, Pellegrini O, Seguin J, et al. The C-terminal domain of Escherichia coli Hfq increases the stability of the hexamer. Eur J Biochem 2004; 271:1258-65; PMID:15030475; http://dx.doi.org/10.1111/j.1432-1033.2004.04026.x.
    • (2004) Eur J Biochem , vol.271 , pp. 1258-1265
    • Arluison, V.1    Folichon, M.2    Marco, S.3    Derreumaux, P.4    Pellegrini, O.5    Seguin, J.6
  • 43
    • 79959469361 scopus 로고    scopus 로고
    • Structural insights into the dynamics and function of the C-terminus of the E. coli RNA chaperone Hfq
    • PMID:21330354
    • Beich-Frandsen M, Vecerek B, Konarev PV, Sjöblom B, Kloiber K, Hämmerle H, et al. Structural insights into the dynamics and function of the C-terminus of the E. coli RNA chaperone Hfq. Nucleic Acids Res 2011; 39:4900-15; PMID:21330354; http://dx.doi.org/10.1093/nar/gkq1346.
    • (2011) Nucleic Acids Res , vol.39 , pp. 4900-4915
    • Beich-Frandsen, M.1    Vecerek, B.2    Konarev, P.V.3    Sjöblom, B.4    Kloiber, K.5    Hämmerle, H.6
  • 44
    • 78349305147 scopus 로고    scopus 로고
    • C-terminally truncated derivatives of Escherichia coli Hfq are proficient in riboregulation
    • PMID:20888338
    • Olsen AS, Møller-Jensen J, Brennan RG, Valentin-Hansen P. C-terminally truncated derivatives of Escherichia coli Hfq are proficient in riboregulation. J Mol Biol 2010; 404:173-82; PMID:20888338; http://dx.doi.org/ 10.1016/j.jmb.2010.09.038.
    • (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
  • 45
    • 38349138513 scopus 로고    scopus 로고
    • The C-terminal domain of Escherichia coli Hfq is required for regulation
    • PMID:18000007
    • Vecerek B, Rajkowitsch L, Sonnleitner E, Schroeder R, Bläsi U. The C-terminal domain of Escherichia coli Hfq is required for regulation. Nucleic Acids Res 2008; 36:133-43; PMID:18000007; http://dx.doi.org/10.1093/nar/gkm985.
    • (2008) Nucleic Acids Res , vol.36 , pp. 133-143
    • Vecerek, B.1    Rajkowitsch, L.2    Sonnleitner, E.3    Schroeder, R.4    Bläsi, U.5
  • 46
    • 0036129690 scopus 로고    scopus 로고
    • Functional replacement of the Escherichia coli hfq gene by the homologue of Pseudomonas aeruginosa
    • PMID:11882724
    • Sonnleitner E, Moll I, Bläsi U. Functional replacement of the Escherichia coli hfq gene by the homologue of Pseudomonas aeruginosa. Microbiology 2002; 148:883-91; PMID:11882724.
    • (2002) Microbiology , vol.148 , pp. 883-891
    • Sonnleitner, E.1    Moll, I.2    Bläsi, U.3
  • 47
    • 84870503889 scopus 로고    scopus 로고
    • Requirement of upstream Hfq-binding (ARN)x elements in glmS and the Hfq C-terminal region for GlmS upregulation by sRNAs GlmZ and GlmY
    • PMID:22661574
    • Salim NN, Faner MA, Philip JA, Feig AL. Requirement of upstream Hfq-binding (ARN)x elements in glmS and the Hfq C-terminal region for GlmS upregulation by sRNAs GlmZ and GlmY. Nucleic Acids Res 2012; 40:8021-32; PMID:22661574; http://dx.doi.org/10.1093/nar/gks392.
    • (2012) Nucleic Acids Res , vol.40 , pp. 8021-8032
    • Salim, N.N.1    Faner, M.A.2    Philip, J.A.3    Feig, A.L.4
  • 48
    • 0028107450 scopus 로고
    • Regulation of the Escherichia coli hfq gene encoding the host factor for phage Q beta
    • PMID:8288550
    • Kajitani M, Kato A, Wada A, Inokuchi Y, Ishihama A. Regulation of the Escherichia coli hfq gene encoding the host factor for phage Q beta. J Bacteriol 1994; 176:531-4; PMID:8288550.
    • (1994) J Bacteriol , vol.176 , pp. 531-534
    • Kajitani, M.1    Kato, A.2    Wada, A.3    Inokuchi, Y.4    Ishihama, A.5
  • 49
    • 66149131462 scopus 로고    scopus 로고
    • Crystal structure of a novel Sm-like protein of putative cyanophage origin at 2.60 A resolution
    • PMID:19173316
    • Das D, Kozbial P, Axelrod HL, Miller MD, McMullan D, Krishna SS, et al. Crystal structure of a novel Sm-like protein of putative cyanophage origin at 2.60 A resolution. Proteins 2009; 75:296-307; PMID:19173316; http://dx.doi.org/10.1002/prot.22360.
    • (2009) Proteins , vol.75 , pp. 296-307
    • Das, D.1    Kozbial, P.2    Axelrod, H.L.3    Miller, M.D.4    McMullan, D.5    Krishna, S.S.6
  • 50
    • 0035876146 scopus 로고    scopus 로고
    • Crystal structure of a heptameric Sm-like protein complex from archaea: Implications for the structure and evolution of snRNPs
    • PMID:11399068
    • Collins BM, Harrop SJ, Kornfeld GD, Dawes IW, Curmi PM, Mabbutt BC. Crystal structure of a heptameric Sm-like protein complex from archaea: implications for the structure and evolution of snRNPs. J Mol Biol 2001; 309:915-23; PMID:11399068; http://dx.doi.org/10.1006/jmbi.2001.4693.
    • (2001) J Mol Biol , vol.309 , pp. 915-923
    • Collins, B.M.1    Harrop, S.J.2    Kornfeld, G.D.3    Dawes, I.W.4    Curmi, P.M.5    Mabbutt, B.C.6
  • 51
    • 40849094144 scopus 로고    scopus 로고
    • Crystal structure of Lsm3 octamer from Saccharomyces cerevisiae: Implications for Lsm ring organisation and recruitment
    • PMID:18329667
    • Naidoo N, Harrop SJ, Sobti M, Haynes PA, Szymczyna BR, Williamson JR, et al. Crystal structure of Lsm3 octamer from Saccharomyces cerevisiae: implications for Lsm ring organisation and recruitment. J Mol Biol 2008; 377:1357-71; PMID:18329667; http://dx.doi.org/10.1016/j.jmb.2008.01.007.
    • (2008) J Mol Biol , vol.377 , pp. 1357-1371
    • Naidoo, N.1    Harrop, S.J.2    Sobti, M.3    Haynes, P.A.4    Szymczyna, B.R.5    Williamson, J.R.6
  • 53
    • 67650649464 scopus 로고    scopus 로고
    • Cyanobacteria contain a structural homologue of the Hfq protein with altered RNA-binding properties
    • PMID:19777643
    • Bøggild A, Overgaard M, Valentin-Hansen P, Brodersen DE. Cyanobacteria contain a structural homologue of the Hfq protein with altered RNA-binding properties. FEBS J 2009; 276:3904-15; PMID:19777643; http://dx.doi.org/10.1111/j.1742-4658.2009.07104.x.
    • (2009) FEBS J , vol.276 , pp. 3904-3915
    • Bøggild, A.1    Overgaard, M.2    Valentin-Hansen, P.3    Brodersen, D.E.4
  • 54
    • 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
    • PMID:20445260
    • Baba S, Someya T, Kawai G, Nakamura K, Kumasaka T. 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 2010; 66:563-6; PMID:20445260; http://dx.doi.org/10.1107/S1744309110009942.
    • (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
  • 55
    • 30344461900 scopus 로고    scopus 로고
    • Three-dimensional structures of fibrillar Sm proteins: Hfq and other Sm-like proteins
    • PMID:16337963
    • Arluison V, Mura C, Guzmán MR, Liquier J, Pellegrini O, Gingery M, et al. Three-dimensional structures of fibrillar Sm proteins: Hfq and other Sm-like proteins. J Mol Biol 2006; 356:86-96; PMID:16337963; http://dx.doi.org/10.1016/j.jmb.2005.11.010.
    • (2006) J Mol Biol , vol.356 , pp. 86-96
    • Arluison, V.1    Mura, C.2    Guzmán, M.R.3    Liquier, J.4    Pellegrini, O.5    Gingery, M.6
  • 56
    • 78650273324 scopus 로고    scopus 로고
    • Functional organization of the Sm core in the crystal structure of human U1 snRNP
    • PMID:21113136
    • Weber G, Trowitzsch S, Kastner B, Lührmann R, Wahl MC. Functional organization of the Sm core in the crystal structure of human U1 snRNP. EMBO J 2010; 29:4172-84; PMID:21113136; http://dx.doi.org/10.1038/emboj.2010.295.
    • (2010) EMBO J , vol.29 , pp. 4172-4184
    • Weber, G.1    Trowitzsch, S.2    Kastner, B.3    Lührmann, R.4    Wahl, M.C.5
  • 57
    • 79961137129 scopus 로고    scopus 로고
    • Structure of a key intermediate of the SMN complex reveals Gemin2's crucial function in snRNP assembly
    • PMID:21816274
    • Zhang R, So BR, Li P, Yong J, Glisovic T, Wan L, et al. Structure of a key intermediate of the SMN complex reveals Gemin2's crucial function in snRNP assembly. Cell 2011; 146:384-95; PMID:21816274; http://dx.doi.org/10.1016/j. cell.2011.06.043.
    • (2011) Cell , vol.146 , pp. 384-395
    • Zhang, R.1    So, B.R.2    Li, P.3    Yong, J.4    Glisovic, T.5    Wan, L.6
  • 58
    • 84858276202 scopus 로고    scopus 로고
    • Hexamer to monomer equilibrium of E. coli Hfq in solution and its impact on RNA annealing
    • PMID:22326348
    • Panja S, Woodson SA. Hexamer to monomer equilibrium of E. coli Hfq in solution and its impact on RNA annealing. J Mol Biol 2012; 417:406-12; PMID:22326348; http://dx.doi.org/10.1016/j.jmb.2012.02.009.
    • (2012) J Mol Biol , vol.417 , pp. 406-412
    • Panja, S.1    Woodson, S.A.2
  • 59
    • 0016189410 scopus 로고
    • Nucleotide sequence specific interaction of host factor I with bacteriophage Q beta RNA
    • PMID:4604832
    • Hori K, Yanazaki Y. Nucleotide sequence specific interaction of host factor I with bacteriophage Q beta RNA. FEBS Lett 1974; 43:20-2; PMID:4604832; http://dx.doi.org/10.1016/0014-5793(74)81095-1.
    • (1974) FEBS Lett , vol.43 , pp. 20-22
    • Hori, K.1    Yanazaki, Y.2
  • 60
    • 0016712465 scopus 로고
    • Isolation of bacterial and phage proteins by homopolymer RNA-cellulose chromatography
    • PMID:807580
    • Carmichael GG. Isolation of bacterial and phage proteins by homopolymer RNA-cellulose chromatography. J Biol Chem 1975; 250:6160-7; PMID:807580.
    • (1975) J Biol Chem , vol.250 , pp. 6160-6167
    • Carmichael, G.G.1
  • 61
    • 50649097486 scopus 로고    scopus 로고
    • The rpoS mRNA leader recruits Hfq to facilitate annealing with DsrA sRNA
    • PMID:18658123
    • Soper TJ, Woodson SA. The rpoS mRNA leader recruits Hfq to facilitate annealing with DsrA sRNA. RNA 2008; 14:1907-17; PMID:18658123; http://dx.doi.org/10.1261/rna.1110608.
    • (2008) RNA , vol.14 , pp. 1907-1917
    • Soper, T.J.1    Woodson, S.A.2
  • 62
    • 77958563236 scopus 로고    scopus 로고
    • An upstream Hfq binding site in the fhlA mRNA leader region facilitates the OxyS-fhlA interaction
    • PMID:20927406
    • Salim NN, Feig AL. An upstream Hfq binding site in the fhlA mRNA leader region facilitates the OxyS-fhlA interaction. PLoS One 2010; 5; PMID:20927406; http://dx.doi.org/10.1371/journal.pone.0013028.
    • (2010) PLoS One , vol.5
    • Salim, N.N.1    Feig, A.L.2
  • 63
    • 77954378224 scopus 로고    scopus 로고
    • Genomic SELEX for Hfq-binding RNAs identifies genomic aptamers predominantly in antisense transcripts
    • PMID:20348540
    • Lorenz C, Gesell T, Zimmermann B, Schoeberl U, Bilusic I, Rajkowitsch L, et al. Genomic SELEX for Hfq-binding RNAs identifies genomic aptamers predominantly in antisense transcripts. Nucleic Acids Res 2010; 38:3794-808; PMID:20348540; http://dx.doi.org/10.1093/nar/gkq032.
    • (2010) Nucleic Acids Res , vol.38 , pp. 3794-3808
    • Lorenz, C.1    Gesell, T.2    Zimmermann, B.3    Schoeberl, U.4    Bilusic, I.5    Rajkowitsch, L.6
  • 65
    • 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
    • PMID:22053080
    • Someya T, Baba S, Fujimoto M, Kawai G, Kumasaka T, Nakamura K. 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 2012; 40:1856-67; PMID:22053080; http://dx.doi.org/10.1093/nar/gkr892.
    • (2012) Nucleic Acids Res , vol.40 , pp. 1856-1867
    • Someya, T.1    Baba, S.2    Fujimoto, M.3    Kawai, G.4    Kumasaka, T.5    Nakamura, K.6
  • 66
    • 0142240435 scopus 로고    scopus 로고
    • Coincident Hfq binding and RNase E cleavage sites on mRNA and small regulatory RNAs
    • PMID:14561880
    • Moll I, Afonyushkin T, Vytvytska O, Kaberdin VR, Bläsi U. Coincident Hfq binding and RNase E cleavage sites on mRNA and small regulatory RNAs. RNA 2003; 9:1308-14; PMID:14561880; http://dx.doi.org/10.1261/rna.5850703.
    • (2003) RNA , vol.9 , pp. 1308-1314
    • Moll, I.1    Afonyushkin, T.2    Vytvytska, O.3    Kaberdin, V.R.4    Bläsi, U.5
  • 67
    • 25844458478 scopus 로고    scopus 로고
    • Hfq-dependent regulation of OmpA synthesis is mediated by an antisense RNA
    • PMID:16204185
    • Udekwu KI, Darfeuille F, Vogel J, Reimegård J, Holmqvist E, Wagner EG. Hfq-dependent regulation of OmpA synthesis is mediated by an antisense RNA. Genes Dev 2005; 19:2355-66; PMID:16204185; http://dx.doi.org/10.1101/gad.354405.
    • (2005) Genes Dev , vol.19 , pp. 2355-2366
    • Udekwu, K.I.1    Darfeuille, F.2    Vogel, J.3    Reimegård, J.4    Holmqvist, E.5    Wagner, E.G.6
  • 68
    • 79958095005 scopus 로고    scopus 로고
    • Rapid binding and release of Hfq from ternary complexes during RNA annealing
    • PMID:21378124
    • Hopkins JF, Panja S, Woodson SA. Rapid binding and release of Hfq from ternary complexes during RNA annealing. Nucleic Acids Res 2011; 39:5193-202; PMID:21378124; http://dx.doi.org/10.1093/nar/gkr062.
    • (2011) Nucleic Acids Res , vol.39 , pp. 5193-5202
    • Hopkins, J.F.1    Panja, S.2    Woodson, S.A.3
  • 69
    • 58149139033 scopus 로고    scopus 로고
    • A rough guide to the non-coding RNA world of Salmonella
    • PMID:19007416
    • Vogel J. A rough guide to the non-coding RNA world of Salmonella. Mol Microbiol 2009; 71:1-11; PMID:19007416; http://dx.doi.org/10.1111/j.1365-2958. 2008.06505.x.
    • (2009) Mol Microbiol , vol.71 , pp. 1-11
    • Vogel, J.1
  • 70
    • 9244253711 scopus 로고    scopus 로고
    • Cycling of the Sm-like protein Hfq on the DsrA small regulatory RNA
    • PMID:15561140
    • Lease RA, Woodson SA. Cycling of the Sm-like protein Hfq on the DsrA small regulatory RNA. J Mol Biol 2004; 344:1211-23; PMID:15561140; http://dx.doi.org/10.1016/j.jmb.2004.10.006.
    • (2004) J Mol Biol , vol.344 , pp. 1211-1223
    • Lease, R.A.1    Woodson, S.A.2
  • 71
    • 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
    • PMID:16605255
    • Sun X, Wartell RM. Escherichia coli Hfq binds A18 and DsrA domain II with similar 2:1 Hfq6/RNA stoichiometry using different surface sites. Biochemistry 2006; 45:4875-87; PMID:16605255; http://dx.doi.org/10.1021/bi0523613.
    • (2006) Biochemistry , vol.45 , pp. 4875-4887
    • Sun, X.1    Wartell, R.M.2
  • 72
    • 0035104707 scopus 로고    scopus 로고
    • Hfq is necessary for regulation by the untranslated RNA DsrA
    • PMID:11222598
    • Sledjeski DD, Whitman C, Zhang A. Hfq is necessary for regulation by the untranslated RNA DsrA. J Bacteriol 2001; 183:1997-2005; PMID:11222598; http://dx.doi.org/10.1128/JB.183.6.1997-2005.2001.
    • (2001) J Bacteriol , vol.183 , pp. 1997-2005
    • Sledjeski, D.D.1    Whitman, C.2    Zhang, A.3
  • 73
    • 79951540365 scopus 로고    scopus 로고
    • The stoichiometry of the Escherichia coli Hfq protein bound to RNA
    • PMID:21205841
    • Updegrove TB, Correia JJ, Chen Y, Terry C, Wartell RM. The stoichiometry of the Escherichia coli Hfq protein bound to RNA. RNA 2011; 17:489-500; PMID:21205841; http://dx.doi.org/10.1261/rna.2452111.
    • (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
  • 74
    • 78650532236 scopus 로고    scopus 로고
    • Evidence for an autonomous 5' target recognition domain in an Hfq-associated small RNA
    • PMID:21059903
    • Papenfort K, Bouvier M, Mika F, Sharma CM, Vogel J. Evidence for an autonomous 5' target recognition domain in an Hfq-associated small RNA. Proc Natl Acad Sci USA 2010; 107:20435-40; PMID:21059903; http://dx.doi.org/10.1073/ pnas.1009784107.
    • (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
  • 75
    • 84866788439 scopus 로고    scopus 로고
    • The seed region of a small RNA drives the controlled destruction of the target mRNA by the endoribonuclease RNase E
    • PMID:22902561
    • Bandyra KJ, Said N, Pfeiffer V, Górna MW, Vogel J, Luisi BF. The seed region of a small RNA drives the controlled destruction of the target mRNA by the endoribonuclease RNase E. Mol Cell 2012; 47:943-53; PMID:22902561; http://dx.doi.org/10.1016/j.molcel.2012.07.015.
    • (2012) Mol Cell , vol.47 , pp. 943-953
    • Bandyra, K.J.1    Said, N.2    Pfeiffer, V.3    Górna, M.W.4    Vogel, J.5    Luisi, B.F.6
  • 76
    • 34447499141 scopus 로고    scopus 로고
    • Rapid, accurate, computational discovery of Rho-independent transcription terminators illuminates their relationship to DNA uptake
    • PMID:17313685
    • Kingsford CL, Ayanbule K, Salzberg SL. Rapid, accurate, computational discovery of Rho-independent transcription terminators illuminates their relationship to DNA uptake. Genome Biol 2007; 8:R22; PMID:17313685; http://dx.doi.org/10.1186/gb-2007-8-2-r22.
    • (2007) Genome Biol , vol.8
    • Kingsford, C.L.1    Ayanbule, K.2    Salzberg, S.L.3
  • 77
    • 0029073396 scopus 로고
    • Transcription termination at intrinsic terminators: The role of the RNA hairpin
    • PMID:7568019
    • Wilson KS, von Hippel PH. Transcription termination at intrinsic terminators: the role of the RNA hairpin. Proc Natl Acad Sci USA 1995; 92:8793-7; PMID:7568019; http://dx.doi.org/10.1073/pnas.92.19.8793.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8793-8797
    • Wilson, K.S.1    Von Hippel, P.H.2
  • 78
    • 79954597274 scopus 로고    scopus 로고
    • Termination and anti-termination: RNA polymerase runs a stop sign
    • PMID:21478900
    • Santangelo TJ, Artsimovitch I. Termination and anti-termination: RNA polymerase runs a stop sign. Nat Rev Microbiol 2011; 9:319-29; PMID:21478900; http://dx.doi.org/10.1038/nrmicro2560.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 319-329
    • Santangelo, T.J.1    Artsimovitch, I.2
  • 79
    • 79951701614 scopus 로고    scopus 로고
    • RNase E action at a distance: Degradation of target mRNAs mediated by an Hfq-binding small RNA in bacteria
    • PMID:21325130
    • Morita T, Aiba H. RNase E action at a distance: degradation of target mRNAs mediated by an Hfq-binding small RNA in bacteria. Genes Dev 2011; 25:294-8; PMID:21325130; http://dx.doi.org/10.1101/gad.2030311.
    • (2011) Genes Dev , vol.25 , pp. 294-298
    • Morita, T.1    Aiba, H.2
  • 80
    • 0037276123 scopus 로고    scopus 로고
    • Identification of the Hfq-binding site on DsrA RNA: Hfq binds without altering DsrA secondary structure
    • PMID:12554874
    • Brescia CC, Mikulecky PJ, Feig AL, Sledjeski DD. Identification of the Hfq-binding site on DsrA RNA: Hfq binds without altering DsrA secondary structure. RNA 2003; 9:33-43; PMID:12554874; http://dx.doi.org/10.1261/rna. 2570803.
    • (2003) RNA , vol.9 , pp. 33-43
    • Brescia, C.C.1    Mikulecky, P.J.2    Feig, A.L.3    Sledjeski, D.D.4
  • 81
    • 80053440900 scopus 로고    scopus 로고
    • The influence of Escherichia coli Hfq mutations on RNA binding and sRNA•mRNA duplex formation in rpoS riboregulation
    • PMID:21889623
    • Updegrove TB, Wartell RM. The influence of Escherichia coli Hfq mutations on RNA binding and sRNA•mRNA duplex formation in rpoS riboregulation. Biochim Biophys Acta 2011; 1809:532-40; PMID:21889623; http://dx.doi.org/10. 1016/j.bbagrm.2011.08.006.
    • (2011) Biochim Biophys Acta , vol.1809 , pp. 532-540
    • Updegrove, T.B.1    Wartell, R.M.2
  • 82
    • 28344450939 scopus 로고    scopus 로고
    • Arginine-rich motifs present multiple interfaces for specific binding by RNA
    • PMID:16314457
    • Bayer TS, Booth LN, Knudsen SM, Ellington AD. Arginine-rich motifs present multiple interfaces for specific binding by RNA. RNA 2005; 11:1848-57; PMID:16314457; http://dx.doi.org/10.1261/rna.2167605.
    • (2005) RNA , vol.11 , pp. 1848-1857
    • Bayer, T.S.1    Booth, L.N.2    Knudsen, S.M.3    Ellington, A.D.4
  • 83
    • 0032419957 scopus 로고    scopus 로고
    • RNA recognition by arginine-rich peptide motifs
    • PMID:10333744
    • Weiss MA, Narayana N. RNA recognition by arginine-rich peptide motifs. Biopolymers 1998; 48:167-80; PMID:10333744; http://dx.doi.org/10.1002/(SICI) 1097-0282(1998)48:2〈167::AIDBIP6〉 3.0.CO;2-8.
    • (1998) Biopolymers , vol.48 , pp. 167-180
    • Weiss, M.A.1    Narayana, N.2
  • 84
    • 84860769484 scopus 로고    scopus 로고
    • Current knowledge on regulatory RNAs and their machineries in Staphylococcus aureus
    • PMID:22546940
    • Romilly C, Caldelari I, Parmentier D, Lioliou E, Romby P, Fechter P. Current knowledge on regulatory RNAs and their machineries in Staphylococcus aureus. RNA Biol 2012; 9:402-13; PMID:22546940; http://dx.doi.org/10.4161/rna. 20103.
    • (2012) RNA Biol , vol.9 , pp. 402-413
    • Romilly, C.1    Caldelari, I.2    Parmentier, D.3    Lioliou, E.4    Romby, P.5    Fechter, P.6
  • 85
    • 78649885541 scopus 로고    scopus 로고
    • RNAs actively cycle on the Sm-like protein Hfq
    • PMID:21123649
    • Fender A, Elf J, Hampel K, Zimmermann B, Wagner EG. RNAs actively cycle on the Sm-like protein Hfq. Genes Dev 2010; 24:2621-6; PMID:21123649; http://dx.doi.org/10.1101/gad.591310.
    • (2010) Genes Dev , vol.24 , pp. 2621-2626
    • Fender, A.1    Elf, J.2    Hampel, K.3    Zimmermann, B.4    Wagner, E.G.5
  • 86
    • 83355177980 scopus 로고    scopus 로고
    • Competition among Hfq-binding small RNAs in Escherichia coli
    • PMID:22040174
    • Moon K, Gottesman S. Competition among Hfq-binding small RNAs in Escherichia coli. Mol Microbiol 2011; 82:1545-62; PMID:22040174; http://dx.doi.org/10.1111/j.1365-2958.2011.07907.x.
    • (2011) Mol Microbiol , vol.82 , pp. 1545-1562
    • Moon, K.1    Gottesman, S.2
  • 87
    • 70350699443 scopus 로고    scopus 로고
    • Effect of salt and RNA structure on annealing and strand displacement by Hfq
    • PMID:19671524
    • Hopkins JF, Panja S, McNeil SA, Woodson SA. Effect of salt and RNA structure on annealing and strand displacement by Hfq. Nucleic Acids Res 2009; 37:6205-13; PMID:19671524; http://dx.doi.org/10.1093/nar/gkp646.
    • (2009) Nucleic Acids Res , vol.37 , pp. 6205-6213
    • Hopkins, J.F.1    Panja, S.2    McNeil, S.A.3    Woodson, S.A.4
  • 88
    • 79960441320 scopus 로고    scopus 로고
    • Major role for mRNA binding and restructuring in sRNA recruitment by Hfq
    • PMID:21705431
    • Soper TJ, Doxzen K, Woodson SA. Major role for mRNA binding and restructuring in sRNA recruitment by Hfq. RNA 2011; 17:1544-50; PMID:21705431; http://dx.doi.org/10.1261/rna.2767211.
    • (2011) RNA , vol.17 , pp. 1544-1550
    • Soper, T.J.1    Doxzen, K.2    Woodson, S.A.3
  • 89
    • 79958095005 scopus 로고    scopus 로고
    • Rapid binding and release of Hfq from ternary complexes during RNA annealing
    • PMID:21378124
    • Hopkins JF, Panja S, Woodson SA. Rapid binding and release of Hfq from ternary complexes during RNA annealing. Nucleic Acids Res 2011; 39:5193-202; PMID:21378124; http://dx.doi.org/10.1093/nar/gkr062.
    • (2011) Nucleic Acids Res , vol.39 , pp. 5193-5202
    • Hopkins, J.F.1    Panja, S.2    Woodson, S.A.3
  • 90
    • 84866949691 scopus 로고    scopus 로고
    • Hfq proximity and orientation controls RNA annealing
    • PMID:22761405
    • Panja S, Woodson SA. Hfq proximity and orientation controls RNA annealing. Nucleic Acids Res 2012; 40:8690-7; PMID:22761405; http://dx.doi.org/10.1093/nar/gks618.
    • (2012) Nucleic Acids Res , vol.40 , pp. 8690-8697
    • Panja, S.1    Woodson, S.A.2
  • 91
    • 39049131090 scopus 로고    scopus 로고
    • RNA chaperones, RNA annealers and RNA helicases
    • PMID:18347437
    • Rajkowitsch L, Chen D, Stampfl S, Semrad K, Waldsich C, Mayer O, et al. RNA chaperones, RNA annealers and RNA helicases. RNA Biol 2007; 4:118-30; PMID:18347437; http://dx.doi.org/10.4161/rna.4.3.5445.
    • (2007) RNA Biol , vol.4 , pp. 118-130
    • Rajkowitsch, L.1    Chen, D.2    Stampfl, S.3    Semrad, K.4    Waldsich, C.5    Mayer, O.6
  • 92
    • 0038352109 scopus 로고    scopus 로고
    • Regulatory roles for small RNAs in bacteria
    • PMID:12732300
    • Massé E, Majdalani N, Gottesman S. Regulatory roles for small RNAs in bacteria. Curr Opin Microbiol 2003; 6:120-4; PMID:12732300; http://dx.doi.org/10.1016/S1369-5274(03)00027-4.
    • (2003) Curr Opin Microbiol , vol.6 , pp. 120-124
    • Massé, E.1    Majdalani, N.2    Gottesman, S.3
  • 93
    • 24944507588 scopus 로고    scopus 로고
    • RNase E-based ribonucleo-protein complexes: Mechanical basis of mRNA destabilization mediated by bacterial noncoding RNAs
    • PMID:16166379
    • Morita T, Maki K, Aiba H. RNase E-based ribonucleo-protein complexes: mechanical basis of mRNA destabilization mediated by bacterial noncoding RNAs. Genes Dev 2005; 19:2176-86; PMID:16166379; http://dx.doi.org/10.1101/gad. 1330405.
    • (2005) Genes Dev , vol.19 , pp. 2176-2186
    • Morita, T.1    Maki, K.2    Aiba, H.3
  • 94
    • 79951700321 scopus 로고    scopus 로고
    • Small RNA-induced mRNA degradation achieved through both translation block and activated cleavage
    • PMID:21289064
    • Prévost K, Desnoyers G, Jacques JF, Lavoie F, Massé E. Small RNA-induced mRNA degradation achieved through both translation block and activated cleavage. Genes Dev 2011; 25:385-96; PMID:21289064; http://dx.doi.org/10.1101/gad.2001711.
    • (2011) Genes Dev , vol.25 , pp. 385-396
    • Prévost, K.1    Desnoyers, G.2    Jacques, J.F.3    Lavoie, F.4    Massé, E.5
  • 95
    • 70350699443 scopus 로고    scopus 로고
    • Effect of salt and RNA structure on annealing and strand displacement by Hfq
    • PMID:19671524
    • Hopkins JF, Panja S, McNeil SA, Woodson SA. Effect of salt and RNA structure on annealing and strand displacement by Hfq. Nucleic Acids Res 2009; 37:6205-13; PMID:19671524; http://dx.doi.org/10.1093/nar/gkp646.
    • (2009) Nucleic Acids Res , vol.37 , pp. 6205-6213
    • Hopkins, J.F.1    Panja, S.2    McNeil, S.A.3    Woodson, S.A.4
  • 96
    • 68249156618 scopus 로고    scopus 로고
    • Coding sequence targeting by MicC RNA reveals bacterial mRNA silencing downstream of translational initiation
    • PMID:19620966
    • Pfeiffer V, Papenfort K, Lucchini S, Hinton JC, Vogel J. Coding sequence targeting by MicC RNA reveals bacterial mRNA silencing downstream of translational initiation. Nat Struct Mol Biol 2009; 16:840-6; PMID:19620966; http://dx.doi.org/10.1038/nsmb.1631.
    • (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
  • 97
    • 84866926513 scopus 로고    scopus 로고
    • The low-resolution solution structure of Vibrio cholerae Hfq in complex with Qrr1 sRNA
    • PMID:22730296
    • Vincent HA, Henderson CA, Stone CM, Cary PD, Gowers DM, Sobott F, et al. The low-resolution solution structure of Vibrio cholerae Hfq in complex with Qrr1 sRNA. Nucleic Acids Res 2012; 40:8698-710; PMID:22730296; http://dx.doi.org/10.1093/nar/gks582.
    • (2012) Nucleic Acids Res , vol.40 , pp. 8698-8710
    • Vincent, H.A.1    Henderson, C.A.2    Stone, C.M.3    Cary, P.D.4    Gowers, D.M.5    Sobott, F.6
  • 98
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • PMID:15572765
    • Emsley P, Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 2004; 60:2126-32; PMID:15572765; http://dx.doi.org/10.1107/S0907444904019158.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 99
    • 33747856166 scopus 로고    scopus 로고
    • The MPI Bioinformatics Toolkit for protein sequence analysis
    • PMID:16845021
    • Biegert A, Mayer C, Remmert M, Söding J, Lupas AN. The MPI Bioinformatics Toolkit for protein sequence analysis. Nucleic Acids Res 2006; 34(Web Server issue):W335-9; PMID:16845021; http://dx.doi.org/10.1093/nar/ gkl217.
    • (2006) Nucleic Acids Res , vol.34 , Issue.WEB SERVER ISSUE
    • Biegert, A.1    Mayer, C.2    Remmert, M.3    Söding, J.4    Lupas, A.N.5


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