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Volumn 426, Issue 2, 2014, Pages 275-285

Positional effects of AAN motifs in rpoS regulation by sRNAs and Hfq

Author keywords

5 UTR; bacterial stress response; RNA chaperone; RNA protein interactions; translational control

Indexed keywords

BACTERIAL PROTEIN; MESSENGER RNA; PROTEIN HFQ; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR RPOS; TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 84891827418     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.08.026     Document Type: Article
Times cited : (39)

References (41)
  • 2
    • 77956879952 scopus 로고    scopus 로고
    • Integrating anaerobic/aerobic sensing and the general stress response through the ArcZ small RNA
    • P. Mandin, and S. Gottesman Integrating anaerobic/aerobic sensing and the general stress response through the ArcZ small RNA EMBO J 29 2010 3094 3107
    • (2010) EMBO J , vol.29 , pp. 3094-3107
    • Mandin, P.1    Gottesman, S.2
  • 3
    • 84860735686 scopus 로고    scopus 로고
    • The small RNA RybA regulates key-genes in the biosynthesis of aromatic amino acids under peroxide stress in E. Coli
    • K. Gerstle, K. Klatschke, U. Hahn, and N. Piganeau The small RNA RybA regulates key-genes in the biosynthesis of aromatic amino acids under peroxide stress in E. coli RNA Biol 9 2012 458 468
    • (2012) RNA Biol , vol.9 , pp. 458-468
    • Gerstle, K.1    Klatschke, K.2    Hahn, U.3    Piganeau, N.4
  • 4
    • 84863924309 scopus 로고    scopus 로고
    • Bacterial small RNA regulators: Versatile roles and rapidly evolving variations
    • 10.1101/cshperspect.a003798
    • S. Gottesman, and G. Storz Bacterial small RNA regulators: versatile roles and rapidly evolving variations Cold Spring Harbor Perspect Biol 3 2011 10.1101/cshperspect.a003798
    • (2011) Cold Spring Harbor Perspect Biol , vol.3
    • Gottesman, S.1    Storz, G.2
  • 5
    • 79960433506 scopus 로고    scopus 로고
    • Hfq and its constellation of RNA
    • J. Vogel, and B.F. Luisi 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
  • 6
    • 84866307118 scopus 로고    scopus 로고
    • The bacterial protein Hfq: Much more than a mere RNA-binding factor
    • P. Sobrero, and C. Valverde The bacterial protein Hfq: much more than a mere RNA-binding factor Crit Rev Microbiol 38 2012 276 299
    • (2012) Crit Rev Microbiol , vol.38 , pp. 276-299
    • Sobrero, P.1    Valverde, C.2
  • 7
    • 0036899077 scopus 로고    scopus 로고
    • Stationary phase gene regulation: What makes an Escherichia coli promoter sigmaS-selective?
    • R. Hengge-Aronis Stationary phase gene regulation: what makes an Escherichia coli promoter sigmaS-selective? Curr Opin Microbiol 5 2002 591 595
    • (2002) Curr Opin Microbiol , vol.5 , pp. 591-595
    • Hengge-Aronis, R.1
  • 8
    • 0032514739 scopus 로고    scopus 로고
    • DsrA RNA regulates translation of RpoS message by an anti-antisense mechanism, independent of its action as an antisilencer of transcription
    • N. Majdalani, C. Cunning, D. Sledjeski, T. Elliott, and S. Gottesman DsrA RNA regulates translation of RpoS message by an anti-antisense mechanism, independent of its action as an antisilencer of transcription Proc Natl Acad Sci USA 95 1998 12462 12467
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12462-12467
    • Majdalani, N.1    Cunning, C.2    Sledjeski, D.3    Elliott, T.4    Gottesman, S.5
  • 9
    • 80053226878 scopus 로고    scopus 로고
    • The RpoS-mediated general stress response in Escherichia coli
    • A. Battesti, N. Majdalani, and S. Gottesman The RpoS-mediated general stress response in Escherichia coli Annu Rev Microbiol 65 2011 189 213
    • (2011) Annu Rev Microbiol , vol.65 , pp. 189-213
    • Battesti, A.1    Majdalani, N.2    Gottesman, S.3
  • 11
    • 54849408366 scopus 로고    scopus 로고
    • Effect of Hfq on RprA-rpoS mRNA pairing: Hfq-RNA binding and the influence of the 5′ rpoS mRNA leader region
    • T. Updegrove, N. Wilf, X. Sun, and R.M. Wartell Effect of Hfq on RprA-rpoS mRNA pairing: Hfq-RNA binding and the influence of the 5′ rpoS mRNA leader region Biochemistry 47 2008 11184 11195
    • (2008) Biochemistry , vol.47 , pp. 11184-11195
    • Updegrove, T.1    Wilf, N.2    Sun, X.3    Wartell, R.M.4
  • 12
    • 50649097486 scopus 로고    scopus 로고
    • The rpoS mRNA leader recruits Hfq to facilitate annealing with DsrA sRNA
    • T.J. Soper, and S.A. Woodson The rpoS mRNA leader recruits Hfq to facilitate annealing with DsrA sRNA RNA 14 2008 1907 1917
    • (2008) RNA , vol.14 , pp. 1907-1917
    • Soper, T.J.1    Woodson, S.A.2
  • 14
    • 72049095718 scopus 로고    scopus 로고
    • Structure of Escherichia coli Hfq bound to polyriboadenylate RNA
    • T.M. Link, P. Valentin-Hansen, and R.G. Brennan 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
  • 15
    • 0036645689 scopus 로고    scopus 로고
    • Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: A bacterial Sm-like protein
    • M.A. Schumacher, R.F. Pearson, T. Moller, P. Valentin-Hansen, and R.G. Brennan Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: a bacterial Sm-like protein EMBO J 21 2002 3546 3556
    • (2002) EMBO J , vol.21 , pp. 3546-3556
    • Schumacher, M.A.1    Pearson, R.F.2    Moller, T.3    Valentin-Hansen, P.4    Brennan, R.G.5
  • 16
    • 84879005493 scopus 로고    scopus 로고
    • Structure and RNA-binding properties of the bacterial Lsm protein Hfq
    • E. Sauer Structure and RNA-binding properties of the bacterial Lsm protein Hfq RNA Biol 10 2013 610 618
    • (2013) RNA Biol , vol.10 , pp. 610-618
    • Sauer, E.1
  • 17
    • 84883478358 scopus 로고    scopus 로고
    • Conserved arginines on the rim of Hfq catalyze base pair formation and exchange
    • S. Panja, D.J. Schu, and S.A. Woodson Conserved arginines on the rim of Hfq catalyze base pair formation and exchange Nucleic Acids Res 41 2013 7536 7546
    • (2013) Nucleic Acids Res , vol.41 , pp. 7536-7546
    • Panja, S.1    Schu, D.J.2    Woodson, S.A.3
  • 18
    • 84862232515 scopus 로고    scopus 로고
    • Small RNA binding to the lateral surface of Hfq hexamers and structural rearrangements upon mRNA target recognition
    • E. Sauer, S. Schmidt, and O. Weichenrieder Small RNA binding to the lateral surface of Hfq hexamers and structural rearrangements upon mRNA target recognition Proc Natl Acad Sci USA 109 2012 9396 9401
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 9396-9401
    • Sauer, E.1    Schmidt, S.2    Weichenrieder, O.3
  • 19
    • 84866949691 scopus 로고    scopus 로고
    • Hfq proximity and orientation controls RNA annealing
    • S. Panja, and S.A. Woodson Hfq proximity and orientation controls RNA annealing Nucleic Acids Res 40 2012 8690 8697
    • (2012) Nucleic Acids Res , vol.40 , pp. 8690-8697
    • Panja, S.1    Woodson, S.A.2
  • 20
    • 0037007078 scopus 로고    scopus 로고
    • A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli
    • E. Masse, and S. Gottesman A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli Proc Natl Acad Sci USA 99 2002 4620 4625
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 4620-4625
    • Masse, E.1    Gottesman, S.2
  • 21
    • 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
    • K. Prevost, H. Salvail, G. Desnoyers, J.F. Jacques, E. Phaneuf, and E. Masse The small RNA RyhB activates the translation of shiA mRNA encoding a permease of shikimate, a compound involved in siderophore synthesis Mol Microbiol 64 2007 1260 1273
    • (2007) Mol Microbiol , vol.64 , pp. 1260-1273
    • Prevost, K.1    Salvail, H.2    Desnoyers, G.3    Jacques, J.F.4    Phaneuf, E.5    Masse, E.6
  • 22
    • 84859915108 scopus 로고    scopus 로고
    • Multiple factors dictate target selection by Hfq-binding small RNAs
    • C.L. Beisel, T.B. Updegrove, B.J. Janson, and G. Storz Multiple factors dictate target selection by Hfq-binding small RNAs EMBO J 31 2012 1961 1974
    • (2012) EMBO J , vol.31 , pp. 1961-1974
    • Beisel, C.L.1    Updegrove, T.B.2    Janson, B.J.3    Storz, G.4
  • 23
    • 77958563236 scopus 로고    scopus 로고
    • An upstream Hfq binding site in the fhlA mRNA leader region facilitates the OxyS-fhlA interaction
    • N.N. Salim, and A.L. Feig An upstream Hfq binding site in the fhlA mRNA leader region facilitates the OxyS-fhlA interaction PLoS One 5 2010 e13028
    • (2010) PLoS One , vol.5 , pp. 13028
    • Salim, N.N.1    Feig, A.L.2
  • 24
    • 33947720028 scopus 로고    scopus 로고
    • Selective 2′-hydroxyl acylation analyzed by primer extension (SHAPE): Quantitative RNA structure analysis at single nucleotide resolution
    • K.A. Wilkinson, E.J. Merino, and K.M. Weeks Selective 2′-hydroxyl acylation analyzed by primer extension (SHAPE): quantitative RNA structure analysis at single nucleotide resolution Nat Protoc 1 2006 1610 1616
    • (2006) Nat Protoc , vol.1 , pp. 1610-1616
    • Wilkinson, K.A.1    Merino, E.J.2    Weeks, K.M.3
  • 25
    • 46349099944 scopus 로고    scopus 로고
    • High-throughput single-nucleotide structural mapping by capillary automated footprinting analysis
    • S. Mitra, I.V. Shcherbakova, R.B. Altman, M. Brenowitz, and A. Laederach High-throughput single-nucleotide structural mapping by capillary automated footprinting analysis Nucleic Acids Res 36 2008 e63
    • (2008) Nucleic Acids Res , vol.36 , pp. 63
    • Mitra, S.1    Shcherbakova, I.V.2    Altman, R.B.3    Brenowitz, M.4    Laederach, A.5
  • 26
    • 16244412610 scopus 로고    scopus 로고
    • RNA structure analysis at single nucleotide resolution by selective 2′-hydroxyl acylation and primer extension (SHAPE)
    • E.J. Merino, K.A. Wilkinson, J.L. Coughlan, and K.M. Weeks RNA structure analysis at single nucleotide resolution by selective 2′-hydroxyl acylation and primer extension (SHAPE) J Am Chem Soc 127 2005 4223 4231
    • (2005) J Am Chem Soc , vol.127 , pp. 4223-4231
    • Merino, E.J.1    Wilkinson, K.A.2    Coughlan, J.L.3    Weeks, K.M.4
  • 28
    • 77957139491 scopus 로고    scopus 로고
    • SHAPE-directed RNA secondary structure prediction
    • J.T. Low, and K.M. Weeks SHAPE-directed RNA secondary structure prediction Methods 52 2010 150 158
    • (2010) Methods , vol.52 , pp. 150-158
    • Low, J.T.1    Weeks, K.M.2
  • 29
    • 9244253711 scopus 로고    scopus 로고
    • Cycling of the Sm-like protein Hfq on the DsrA small regulatory RNA
    • R.A. Lease, and S.A. Woodson Cycling of the Sm-like protein Hfq on the DsrA small regulatory RNA J Mol Biol 344 2004 1211 1223
    • (2004) J Mol Biol , vol.344 , pp. 1211-1223
    • Lease, R.A.1    Woodson, S.A.2
  • 30
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • M. Zuker Mfold web server for nucleic acid folding and hybridization prediction Nucleic Acids Res 31 2003 3406 3415
    • (2003) Nucleic Acids Res , vol.31 , pp. 3406-3415
    • Zuker, M.1
  • 31
    • 65349177758 scopus 로고    scopus 로고
    • A genetic approach for finding small RNAs regulators of genes of interest identifies RybC as regulating the DpiA/DpiB two-component system
    • P. Mandin, and S. Gottesman A genetic approach for finding small RNAs regulators of genes of interest identifies RybC as regulating the DpiA/DpiB two-component system Mol Microbiol 72 2009 551 565
    • (2009) Mol Microbiol , vol.72 , pp. 551-565
    • Mandin, P.1    Gottesman, S.2
  • 32
    • 84875457350 scopus 로고    scopus 로고
    • Bacterial small RNA-based negative regulation: Hfq and its accomplices
    • N. De Lay, D.J. Schu, and S. Gottesman Bacterial small RNA-based negative regulation: Hfq and its accomplices J Biol Chem 288 2013 7996 8003
    • (2013) J Biol Chem , vol.288 , pp. 7996-8003
    • De Lay, N.1    Schu, D.J.2    Gottesman, S.3
  • 33
    • 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
    • K.J. Bandyra, N. Said, V. Pfeiffer, M.W. Gorna, J. Vogel, and B.F. Luisi The seed region of a small RNA drives the controlled destruction of the target mRNA by the endoribonuclease RNase E Mol Cell 47 2012 943 953
    • (2012) Mol Cell , vol.47 , pp. 943-953
    • Bandyra, K.J.1    Said, N.2    Pfeiffer, V.3    Gorna, M.W.4    Vogel, J.5    Luisi, B.F.6
  • 34
    • 78651067735 scopus 로고    scopus 로고
    • Hfq binding at RhlB-recognition region of RNase e is crucial for the rapid degradation of target mRNAs mediated by sRNAs in Escherichia coli
    • Y. Ikeda, M. Yagi, T. Morita, and H. Aiba Hfq binding at RhlB-recognition region of RNase E is crucial for the rapid degradation of target mRNAs mediated by sRNAs in Escherichia coli Mol Microbiol 79 2011 419 432
    • (2011) Mol Microbiol , vol.79 , pp. 419-432
    • Ikeda, Y.1    Yagi, M.2    Morita, T.3    Aiba, H.4
  • 35
    • 1542320707 scopus 로고    scopus 로고
    • Hfq, a new chaperoning role: Binding to messenger RNA determines access for small RNA regulator
    • T.A. Geissmann, and D. Touati Hfq, a new chaperoning role: binding to messenger RNA determines access for small RNA regulator EMBO J 23 2004 396 405
    • (2004) EMBO J , vol.23 , pp. 396-405
    • Geissmann, T.A.1    Touati, D.2
  • 36
    • 79960441320 scopus 로고    scopus 로고
    • Major role for mRNA binding and restructuring in sRNA recruitment by Hfq
    • T.J. Soper, K. Doxzen, and S.A. Woodson Major role for mRNA binding and restructuring in sRNA recruitment by Hfq RNA 17 2011 1544 1550
    • (2011) RNA , vol.17 , pp. 1544-1550
    • Soper, T.J.1    Doxzen, K.2    Woodson, S.A.3
  • 37
    • 52949152433 scopus 로고    scopus 로고
    • ShapeFinder: A software system for high-throughput quantitative analysis of nucleic acid reactivity information resolved by capillary electrophoresis
    • S.M. Vasa, N. Guex, K.A. Wilkinson, K.M. Weeks, and M.C. Giddings ShapeFinder: a software system for high-throughput quantitative analysis of nucleic acid reactivity information resolved by capillary electrophoresis RNA 14 2008 1979 1990
    • (2008) RNA , vol.14 , pp. 1979-1990
    • Vasa, S.M.1    Guex, N.2    Wilkinson, K.A.3    Weeks, K.M.4    Giddings, M.C.5
  • 39
    • 80052935371 scopus 로고    scopus 로고
    • Assembling new Escherichia coli strains by transduction using phage P1
    • S.D. Moore Assembling new Escherichia coli strains by transduction using phage P1 Methods Mol Biol 765 2011 155 169
    • (2011) Methods Mol Biol , vol.765 , pp. 155-169
    • Moore, S.D.1
  • 40
    • 0024285808 scopus 로고
    • Sequence-specific endoribonuclease activity of the Tetrahymena ribozyme: Enhanced cleavage of certain oligonucleotide substrates that form mismatched ribozyme-substrate complexes
    • A.J. Zaug, C.A. Grosshans, and T.R. Cech Sequence-specific endoribonuclease activity of the Tetrahymena ribozyme: enhanced cleavage of certain oligonucleotide substrates that form mismatched ribozyme-substrate complexes Biochemistry 27 1988 8924 8931
    • (1988) Biochemistry , vol.27 , pp. 8924-8931
    • Zaug, A.J.1    Grosshans, C.A.2    Cech, T.R.3
  • 41
    • 0036163624 scopus 로고    scopus 로고
    • The Sm-like Hfq protein increases OxyS RNA interaction with target mRNAs
    • A. Zhang, K.M. Wassarman, J. Ortega, A.C. Steven, and G. Storz The Sm-like Hfq protein increases OxyS RNA interaction with target mRNAs Mol Cell 9 2002 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


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