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Volumn 417, Issue 5, 2012, Pages 406-412

Hexamer to monomer equilibrium of E. coli Hfq in solution and its impact on RNA annealing

Author keywords

fluorescence anisotropy; RNA chaperone; Sm Lsm proteins; sRNAs

Indexed keywords

BACTERIAL PROTEIN; BACTERIAL RNA; MONOMER; PROTEIN HFQ; UNCLASSIFIED DRUG;

EID: 84858276202     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.02.009     Document Type: Article
Times cited : (30)

References (32)
  • 1
    • 79960433506 scopus 로고    scopus 로고
    • Hfq and its constellation of RNA
    • Vogel J., and Luisi B.F. Hfq and its constellation of RNA Nat. Rev., Microbiol. 9 2011 578 589
    • (2011) Nat. Rev., Microbiol. , vol.9 , pp. 578-589
    • Vogel, J.1    Luisi, B.F.2
  • 2
    • 77955155869 scopus 로고    scopus 로고
    • Base pairing small RNAs and their roles in global regulatory networks
    • Beisel C.L., and Storz G. Base pairing small RNAs and their roles in global regulatory networks FEMS Microbiol. Rev. 34 2010 866 882
    • (2010) FEMS Microbiol. Rev. , vol.34 , pp. 866-882
    • Beisel, C.L.1    Storz, G.2
  • 4
    • 33750043437 scopus 로고    scopus 로고
    • Translation initiation and the fate of bacterial mRNAs
    • DOI 10.1111/j.1574-6976.2006.00043.x
    • Kaberdin V.R., and Blasi U. Translation initiation and the fate of bacterial mRNAs FEMS Microbiol. Rev. 30 2006 967 979 (Pubitemid 44583798)
    • (2006) FEMS Microbiology Reviews , vol.30 , Issue.6 , pp. 967-979
    • Kaberdin, V.R.1    Blasi, U.2
  • 5
    • 34247158257 scopus 로고    scopus 로고
    • Mechanism of RNA silencing by Hfq-binding small RNAs
    • DOI 10.1016/j.mib.2007.03.010, PII S1369527407000276, Cell Regulation (RNA Special Issue)
    • Aiba H. Mechanism of RNA silencing by Hfq-binding small RNAs Curr. Opin. Microbiol. 10 2007 134 139 (Pubitemid 46590050)
    • (2007) Current Opinion in Microbiology , vol.10 , Issue.2 , pp. 134-139
    • Aiba, H.1
  • 6
    • 77953753696 scopus 로고    scopus 로고
    • Small RNA-mediated regulation at the level of transcript stability
    • Caron M.P., Lafontaine D.A., and Masse E. Small RNA-mediated regulation at the level of transcript stability RNA Biol. 7 2010 140 144
    • (2010) RNA Biol. , vol.7 , pp. 140-144
    • Caron, M.P.1    Lafontaine, D.A.2    Masse, E.3
  • 7
    • 0036714801 scopus 로고    scopus 로고
    • Predicted structure and phyletic distribution of the RNA-binding protein Hfq
    • Sun X., Zhulin I., and Wartell R.M. Predicted structure and phyletic distribution of the RNA-binding protein Hfq Nucleic Acids Res. 30 2002 3662 3671 (Pubitemid 35021229)
    • (2002) Nucleic Acids Research , vol.30 , Issue.17 , pp. 3662-3671
    • Sun, X.1    Zhulin, I.2    Wartell, R.M.3
  • 8
    • 0036645689 scopus 로고    scopus 로고
    • Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: A bacterial Sm-like protein
    • DOI 10.1093/emboj/cdf322
    • Schumacher M.A., Pearson R.F., Moller T., Valentin-Hansen P., and Brennan R.G. Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: a bacterial Sm-like protein EMBO J. 21 2002 3546 3556 (Pubitemid 34760584)
    • (2002) EMBO Journal , vol.21 , Issue.13 , pp. 3546-3556
    • Schumacher, M.A.1    Pearson, R.F.2    Moller, T.3    Valentin-Hansen, P.4    Brennan, R.G.5
  • 9
    • 72049095718 scopus 로고    scopus 로고
    • Structure of Escherichia coli Hfq bound to polyriboadenylate RNA
    • Link T.M., Valentin-Hansen P., and Brennan R.G. Structure of Escherichia coli Hfq bound to polyriboadenylate RNA Proc. Natl Acad. Sci. USA 106 2009 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
  • 10
    • 80051962605 scopus 로고    scopus 로고
    • Structural basis for RNA 3′-end recognition by Hfq
    • Sauer E., and Weichenrieder O. Structural basis for RNA 3′-end recognition by Hfq Proc. Natl Acad. Sci. USA 108 2011 13065 13070
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 13065-13070
    • Sauer, E.1    Weichenrieder, O.2
  • 13
    • 0019254853 scopus 로고
    • Interaction of Escherichia coli host factor protein with oligoriboadenylates
    • DOI 10.1021/bi00567a029
    • de Haseth P.L., and Uhlenbeck O.C. Interaction of Escherichia coli host factor protein with oligoriboadenylates Biochemistry 19 1980 6138 6146 (Pubitemid 11134695)
    • (1980) Biochemistry , vol.19 , Issue.26 , pp. 6138-6146
    • De Haseth, P.L.1    Uhlenbeck, O.C.2
  • 14
    • 0037378351 scopus 로고    scopus 로고
    • The oligomerization and ligand-binding properties of Sm-like archaeal proteins (SmAPs)
    • DOI 10.1110/ps.0224703
    • Mura C., Kozhukhovsky A., Gingery M., Phillips M., and Eisenberg D. The oligomerization and ligand-binding properties of Sm-like archaeal proteins (SmAPs) Protein Sci. 12 2003 832 847 (Pubitemid 36348470)
    • (2003) Protein Science , vol.12 , Issue.4 , pp. 832-847
    • Mura, C.1    Kozhukhovsky, A.2    Gingery, M.3    Phillips, M.4    Eisenberg, D.5
  • 16
    • 9244253711 scopus 로고    scopus 로고
    • Cycling of the Sm-like protein Hfq on the DsrA small regulatory RNA
    • DOI 10.1016/j.jmb.2004.10.006, PII S0022283604012872
    • Lease R.A., and Woodson S.A. Cycling of the Sm-like protein Hfq on the DsrA small regulatory RNA J. Mol. Biol. 344 2004 1211 1223 (Pubitemid 39550474)
    • (2004) Journal of Molecular Biology , vol.344 , Issue.5 , pp. 1211-1223
    • Lease, R.A.1    Woodson, S.A.2
  • 17
    • 70350699443 scopus 로고    scopus 로고
    • Effect of salt and RNA structure on annealing and strand displacement by Hfq
    • Hopkins J.F., Panja S., McNeil S.A., and Woodson S.A. Effect of salt and RNA structure on annealing and strand displacement by Hfq Nucleic Acids Res. 37 2009 6205 6213
    • (2009) Nucleic Acids Res. , vol.37 , pp. 6205-6213
    • Hopkins, J.F.1    Panja, S.2    McNeil, S.A.3    Woodson, S.A.4
  • 18
    • 79958095005 scopus 로고    scopus 로고
    • Rapid binding and release of Hfq from ternary complexes during RNA annealing
    • Hopkins J.F., Panja S., and Woodson S.A. Rapid binding and release of Hfq from ternary complexes during RNA annealing Nucleic Acids Res. 39 2011 5193 5202
    • (2011) Nucleic Acids Res. , vol.39 , pp. 5193-5202
    • Hopkins, J.F.1    Panja, S.2    Woodson, S.A.3
  • 19
    • 0028107450 scopus 로고
    • Regulation of the Escherichia coli hfq gene encoding the host factor for phage Q(β)
    • Kajitani M., Kato A., Wada A., Inokuchi Y., and Ishihama A. Regulation of the Escherichia coli hfq gene encoding the host factor for phage Q beta J. Bacteriol. 176 1994 531 534 (Pubitemid 24034076)
    • (1994) Journal of Bacteriology , vol.176 , Issue.2 , pp. 531-534
    • Kajitani, M.1    Kato, A.2    Wada, A.3    Inokuchi, Y.4    Ishihama, A.5
  • 20
    • 0027469771 scopus 로고
    • A fluorescence anisotropy study of tetramer-dimer equilibrium of λ repressor and its implication for function
    • Banik U., Mandal N.C., Bhattacharyya B., and Roy S. A fluorescence anisotropy study of tetramer-dimer equilibrium of lambda repressor and its implication for function J. Biol. Chem. 268 1993 3938 3943 (Pubitemid 23072924)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.6 , pp. 3938-3943
    • Banik, U.1    Mandal, N.C.2    Bhattacharyya, B.3    Roy, S.4
  • 21
    • 79951540365 scopus 로고    scopus 로고
    • The stoichiometry of the Escherichia coli Hfq protein bound to RNA
    • Updegrove T.B., Correia J.J., Chen Y., Terry C., and Wartell R.M. The stoichiometry of the Escherichia coli Hfq protein bound to RNA RNA 17 2011 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
  • 24
    • 80053643342 scopus 로고    scopus 로고
    • Cooperation of Escherichia coli Hfq hexamers in DsrA binding
    • Wang W., Wang L., Zou Y., Zhang J., Gong Q., Wu J., and Shi Y. Cooperation of Escherichia coli Hfq hexamers in DsrA binding Genes Dev. 25 2011 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
  • 25
  • 26
    • 0037276123 scopus 로고    scopus 로고
    • Identification of the Hfq-binding site on DsrA RNA: Hfq binds without altering DsrA secondary structure
    • DOI 10.1261/rna.2570803
    • Brescia C.C., Mikulecky P.J., Feig A.L., and Sledjeski D.D. Identification of the Hfq-binding site on DsrA RNA: Hfq binds without altering DsrA secondary structure RNA 9 2003 33 43 (Pubitemid 36206300)
    • (2003) RNA , vol.9 , Issue.1 , pp. 33-43
    • Brescia, C.C.1    Mikulecky, P.J.2    Feig, A.L.3    Sledjeski, D.D.4
  • 27
    • 34247109118 scopus 로고    scopus 로고
    • Hfq structure, function and ligand binding
    • DOI 10.1016/j.mib.2007.03.015, PII S1369527407000331, Cell Regulation (RNA Special Issue)
    • Brennan R.G., and Link T.M. Hfq structure, function and ligand binding Curr. Opin. Microbiol. 10 2007 125 133 (Pubitemid 46590055)
    • (2007) Current Opinion in Microbiology , vol.10 , Issue.2 , pp. 125-133
    • Brennan, R.G.1    Link, T.M.2
  • 28
    • 0015500282 scopus 로고
    • Bacterial proteins required for replication of phage Q ribonucleic acid. Purification and properties of host factor I, a ribonucleic acid-binding protein
    • Franze de Fernandez M.T., Hayward W.S., and August J.T. Bacterial proteins required for replication of phage Q ribonucleic acid. Purification and properties of host factor I, a ribonucleic acid-binding protein J. Biol. Chem. 247 1972 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
  • 29
    • 0036163624 scopus 로고    scopus 로고
    • The Sm-like Hfq protein increases OxyS RNA interaction with target mRNAs
    • DOI 10.1016/S1097-2765(01)00437-3
    • Zhang A., Wassarman K.M., Ortega J., Steven A.C., and Storz G. The Sm-like Hfq protein increases OxyS RNA interaction with target mRNAs Mol. Cell 9 2002 11 22 (Pubitemid 34127767)
    • (2002) Molecular Cell , vol.9 , Issue.1 , pp. 11-22
    • Zhang, A.1    Wassarman, K.M.2    Ortega, J.3    Steven, A.C.4    Storz, G.5
  • 31
    • 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., and Wartell R.M. Escherichia coli Hfq binds A18 and DsrA domain II with similar 2:1 Hfq6/RNA stoichiometry using different surface sites Biochemistry 45 2006 4875 4887
    • (2006) Biochemistry , vol.45 , pp. 4875-4887
    • Sun, X.1    Wartell, R.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.