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Volumn 39, Issue 12, 2011, Pages 5131-5139

Dynamic competition of DsrA and rpoS fragments for the proximal binding site of Hfq as a means for efficient annealing

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL RNA; MESSENGER RNA; TRANSFER RNA;

EID: 79958146262     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkr075     Document Type: Article
Times cited : (56)

References (31)
  • 2
    • 36249019206 scopus 로고    scopus 로고
    • Dissecting RNA chaperone activity
    • DOI 10.1261/rna.671807
    • Rajkowitsch, L. and Schroeder, R. (2007) Dissecting RNA chaperone activity. RNA, 13, 2053-2060. (Pubitemid 350127547)
    • (2007) RNA , vol.13 , Issue.12 , pp. 2053-2060
    • Rajkowitsch, L.1    Schroeder, R.2
  • 3
    • 0015500282 scopus 로고
    • Bacterial proteins required for replication of phage Qb ribonucleic acid
    • Franze de Fernandez, M.T., Hayward, W.S. and August, J.T. (1972) Bacterial proteins required for replication of phage Qb ribonucleic acid. J. Biol. Chem., 247, 824-821.
    • (1972) J. Biol. Chem. , vol.247 , pp. 824-821
    • Franze De Fernandez, M.T.1    Hayward, W.S.2    August, J.T.3
  • 4
    • 0028243445 scopus 로고
    • Characterization of broadly pleiotropic phenotypes caused by an hfq insertion mutation in Escherichia coli K-12
    • Tsui, H.-C.T., Leung, H.-C.E. and Winkler, M.E. (1994) Characterization of broadly pleiotropic phenotypes caused by an hfq insertion mutation in Escherichia coli K-12. Mol. Microbiol., 13, 35-49.
    • (1994) Mol. Microbiol. , vol.13 , pp. 35-49
    • Tsui, H.-C.T.1    Leung, H.-C.E.2    Winkler, M.E.3
  • 5
    • 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. (2002) The Sm-like Hfq Protein Increases OxyS RNA Interaction with Target mRNAs. Mol. Cell, 9, 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
  • 8
    • 60149089144 scopus 로고    scopus 로고
    • Regulatory RNAs in bacteria
    • Waters, L.S. and Storz, G. (2009) Regulatory RNAs in bacteria. Cell, 136, 615-628.
    • (2009) Cell , vol.136 , pp. 615-628
    • Waters, L.S.1    Storz, G.2
  • 10
    • 0347519274 scopus 로고    scopus 로고
    • The poly(A) binding protein Hfq protects RNA from RNase E and exoribonucleolytic degradation
    • DOI 10.1093/nar/gkg915
    • Folichon, M., Arluison, V., Pellegrini, O., Huntzinger, E., Regnier, P. and Hajnsdorf, E. (2003) The poly(A) binding protein Hfq protects RNA from RNase E and exoribonucleolytic degradation. Nucleic Acids Res., 31, 7302-7310. (Pubitemid 38008458)
    • (2003) Nucleic Acids Research , vol.31 , Issue.24 , pp. 7302-7310
    • Folichon, M.1    Arluison, V.2    Pellegrini, O.3    Huntzinger, E.4    Regnier, P.5    Hajnsdorf, E.6
  • 11
    • 77953753696 scopus 로고    scopus 로고
    • Small RNA-mediated regulation at the level of transcript stability
    • Caron, M.P., Lafontaine, D.A. and Masse, 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    Masse, E.3
  • 12
    • 75249100904 scopus 로고    scopus 로고
    • The role of Hfq in bacterial pathogens
    • Chao, Y. and Vogel, J. (2010) The role of Hfq in bacterial pathogens. Curr. Opin. Microbiol., 13, 24-33.
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 24-33
    • Chao, Y.1    Vogel, J.2
  • 15
    • 58049161508 scopus 로고    scopus 로고
    • Roles of eukaryotic Lsm proteins in the regulation of mRNA function
    • Tharun, S. (2009) Roles of eukaryotic Lsm proteins in the regulation of mRNA function. Int. Rev. Cell Mol. Biol., 272, 149-189.
    • (2009) Int. Rev. Cell Mol. Biol. , vol.272 , pp. 149-189
    • Tharun, S.1
  • 16
    • 72049095718 scopus 로고    scopus 로고
    • Structure of Escherichia coli Hfq bound to polyriboadenylate RNA
    • Link, T.M., Valentin-Hansen, P. and Brennan, R.G. (2009) Structure of Escherichia coli Hfq bound to polyriboadenylate RNA. Proc. Natl Acad. Sci. USA, 106, 19292-19297.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 19292-19297
    • Link, T.M.1    Valentin-Hansen, P.2    Brennan, R.G.3
  • 17
    • 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. (2002) Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: a bacterial Sm-like protein. EMBO J., 21, 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
  • 18
    • 50649097486 scopus 로고    scopus 로고
    • The rpoS mRNA leader recruits Hfq to facilitate annealing with DsrA sRNA
    • Soper, T.J. and Woodson, S.A. (2008) The rpoS mRNA leader recruits Hfq to facilitate annealing with DsrA sRNA. RNA, 14, 1907-1917.
    • (2008) RNA , vol.14 , pp. 1907-1917
    • Soper, T.J.1    Woodson, S.A.2
  • 20
    • 33847363604 scopus 로고    scopus 로고
    • Spectroscopic observation of RNA chaperone activities of Hfq in post-transcriptional regulation by a small non-coding RNA
    • DOI 10.1093/nar/gkl1124
    • Arluison, V., Hohng, S., Roy, R., Pellegrini, O., Regnier, P. and Ha, T. (2007) Spectroscopic observation of RNA chaperone activities of Hfq in post-transcriptional regulation by a small non-coding RNA. Nucleic Acids Res., 35, 999-1006. (Pubitemid 46344724)
    • (2007) Nucleic Acids Research , vol.35 , Issue.3 , pp. 999-1006
    • Arluison, V.1    Hohng, S.2    Roy, R.3    Pellegrini, O.4    Regnier, P.5    Ha, T.6
  • 21
    • 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. (2004) Cycling of the Sm-like protein Hfq on the DsrA small regulatory RNA. J. Mol. Biol., 344, 1211-1223. (Pubitemid 39550474)
    • (2004) Journal of Molecular Biology , vol.344 , Issue.5 , pp. 1211-1223
    • Lease, R.A.1    Woodson, S.A.2
  • 23
    • 44449134820 scopus 로고    scopus 로고
    • A practical guide to single-molecule FRET
    • DOI 10.1038/nmeth.1208, PII NMETH.1208
    • Roy, R., Hohng, S. and Ha, T. (2008) A practical guide to single-molecule FRET. Nat. Methods, 5, 507-516. (Pubitemid 351761757)
    • (2008) Nature Methods , vol.5 , Issue.6 , pp. 507-516
    • Roy, R.1    Hohng, S.2    Ha, T.3
  • 24
    • 77957903226 scopus 로고    scopus 로고
    • Single-molecule three-color FRET with both negligible spectral overlap and long observation time
    • Lee, S., Lee, J. and Hohng, S. (2010) Single-molecule three-color FRET with both negligible spectral overlap and long observation time. PLoS ONE, 5, e12270.
    • (2010) PLoS ONE , vol.5
    • Lee, S.1    Lee, J.2    Hohng, S.3
  • 26
    • 60749124538 scopus 로고    scopus 로고
    • Cytosolic viral sensor RIG-I is a 5'-triphosphate-dependent translocase on double-stranded RNA
    • Myong, S., Cui, S., Cornish, P.V., Kirchhofer, A., Gack, M.U., Jung, J.U., Hopfner, K.P. and Ha, T. (2009) Cytosolic viral sensor RIG-I is a 5'-triphosphate-dependent translocase on double-stranded RNA. Science, 323, 1070-1074.
    • (2009) Science , vol.323 , pp. 1070-1074
    • Myong, S.1    Cui, S.2    Cornish, P.V.3    Kirchhofer, A.4    Gack, M.U.5    Jung, J.U.6    Hopfner, K.P.7    Ha, T.8
  • 27
    • 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. (2009) Effect of salt and RNA structure on annealing and strand displacement by Hfq. Nucleic Acids Res., 37, 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
  • 28
    • 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. (2007) Hfq structure, function and ligand binding. Curr. Opin. Microbiol., 10, 125-133. (Pubitemid 46590055)
    • (2007) Current Opinion in Microbiology , vol.10 , Issue.2 , pp. 125-133
    • Brennan, R.G.1    Link, T.M.2
  • 29
    • 63649099704 scopus 로고    scopus 로고
    • Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution
    • Pomeranz Krummel, D.A., Oubridge, C., Leung, A.K., Li, J. and Nagai, K. (2009) Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution. Nature, 458, 475-480.
    • (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
  • 30
    • 1842453716 scopus 로고    scopus 로고
    • Controlling mRNA stability and translation with small, noncoding RNAs
    • DOI 10.1016/j.mib.2004.02.015, PII S1369527404000281
    • Storz, G., Opdyke, J.A. and Zhang, A. (2004) Controlling mRNA stability and translation with small, noncoding RNAs. Curr. Opin. Microbiol., 7, 140-144. (Pubitemid 38447046)
    • (2004) Current Opinion in Microbiology , vol.7 , Issue.2 , pp. 140-144
    • Storz, G.1    Opdyke, J.A.2    Zhang, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.