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Volumn 404, Issue 2, 2010, Pages 173-182

C-Terminally Truncated Derivatives of Escherichia coli Hfq Are Proficient in Riboregulation

Author keywords

Hfq; Posttranscriptional control; Role of C terminus; RpoS expression; SRNA regulation

Indexed keywords

ESCHERICHIA COLI PROTEIN; MESSENGER RNA; PROTEIN HFQ; TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 78349305147     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.09.038     Document Type: Article
Times cited : (49)

References (72)
  • 1
    • 28544442127 scopus 로고    scopus 로고
    • Eukaryotic Lsm proteins: lessons from bacteria
    • Wilusz C.J., Wilusz J. Eukaryotic Lsm proteins: lessons from bacteria. Nat. Struct. Mol. Biol. 2005, 12:1031-1036.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 1031-1036
    • Wilusz, C.J.1    Wilusz, J.2
  • 2
    • 18344396487 scopus 로고    scopus 로고
    • Lsm proteins and RNA processing
    • Beggs J. Lsm proteins and RNA processing. Biochem. Soc. Trans. 2005, 33:433-438.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 433-438
    • Beggs, J.1
  • 3
    • 23944455046 scopus 로고    scopus 로고
    • Lsm proteins form heptameric rings that bind to RNA via repeating motifs
    • Khusial P., Plaag R., Zieve G.W. Lsm proteins form heptameric rings that bind to RNA via repeating motifs. Trends Biochem. Sci. 2005, 30:522-528.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 522-528
    • Khusial, P.1    Plaag, R.2    Zieve, G.W.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., Winkler M.E. Characterization of broadly pleiotropic phenotypes caused by an Hfq insertion mutation in Escherichia coli K-12. Mol. Microbiol. 1994, 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
    • 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. Sm-like proteins in Eubacteria: the crystal structure of the Hfq protein from Escherichia coli. Nucleic Acids Res. 2003, 31:4091-4098.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 4091-4098
    • Sauter, C.1    Basquin, J.2    Suck, D.3
  • 6
    • 0036645689 scopus 로고    scopus 로고
    • Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: a bacterial Sm-like protein
    • Schumacher M.A., Pearson R.F., Møller T., Valentin-Hansen P., Brennan R.G. Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: a bacterial Sm-like protein. EMBO J. 2002, 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
  • 7
    • 72049095718 scopus 로고    scopus 로고
    • Structure of Escherichia coli Hfq bound to polyriboadenylate RNA
    • Link T.M., Valentin-Hansen P., Brennan R.G. Structure of Escherichia coli Hfq bound to polyriboadenylate RNA. Proc. Natl Acad. Sci. USA 2009, 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
  • 9
    • 0029054375 scopus 로고
    • Identification and characterization of Uss1p (Sdb23p): a novel U6 snRNA-associated protein with significant similarity to core proteins of small nuclear ribonucleoproteins
    • Cooper M., Johnston L.H., Beggs J.D. Identification and characterization of Uss1p (Sdb23p): a novel U6 snRNA-associated protein with significant similarity to core proteins of small nuclear ribonucleoproteins. EMBO J. 1995, 14:2066-2075.
    • (1995) EMBO J. , vol.14 , pp. 2066-2075
    • Cooper, M.1    Johnston, L.H.2    Beggs, J.D.3
  • 10
    • 0028997105 scopus 로고
    • Sm and Sm-like proteins belong to a large family: identification of proteins of the U6 as well as the U1, U2, U4 and U5 snRNPs
    • Séraphin B. Sm and Sm-like proteins belong to a large family: identification of proteins of the U6 as well as the U1, U2, U4 and U5 snRNPs. EMBO J. 1995, 14:2089-2098.
    • (1995) EMBO J. , vol.14 , pp. 2089-2098
    • Séraphin, B.1
  • 11
    • 0033524941 scopus 로고    scopus 로고
    • Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs
    • Kambach C., Walke S., Young R., Avis J.M., de la Fortelle E., Raker V.A., et al. Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs. Cell 1999, 96:375-387.
    • (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
  • 12
    • 0035876146 scopus 로고    scopus 로고
    • Crystal structure of a heptameric Sm-like protein complex from archaea: implications for the structure and evolution of snRNPs
    • Collins B.M., Harrop S.J., Kornfeld G.D., Dawes I.W., Curmi P.M., Mabbutt B.C. Crystal structure of a heptameric Sm-like protein complex from archaea: implications for the structure and evolution of snRNPs. J. Mol. Biol. 2001, 309:915-923.
    • (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
  • 13
    • 0035826794 scopus 로고    scopus 로고
    • The crystal structure of a heptameric archaeal Sm protein: implications for the eukaryotic snRNP core
    • Mura C., Cascio D., Sawaya M.R., Eisenberg D.S. The crystal structure of a heptameric archaeal Sm protein: implications for the eukaryotic snRNP core. Proc. Natl Acad. Sci. USA 2001, 98:5532-5537.
    • (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
  • 14
    • 0037428440 scopus 로고    scopus 로고
    • Crystal structures of the Pyrococcus abyssi Sm core and its complex with RNA. Common features of RNA binding in archaea and eukarya
    • Thore S., Mayer C., Sauter C., Weeks S., Suck D. Crystal structures of the Pyrococcus abyssi Sm core and its complex with RNA. Common features of RNA binding in archaea and eukarya. J. Biol. Chem. 2003, 278:1239-1247.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1239-1247
    • Thore, S.1    Mayer, C.2    Sauter, C.3    Weeks, S.4    Suck, D.5
  • 15
    • 0035341325 scopus 로고    scopus 로고
    • RNA binding in an Sm core domain: X-ray structure and functional analysis of an archaeal Sm protein complex
    • Toro I., Thore S., Mayer C., Basquin J., Seraphin 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, 20:2293-2303.
    • (2001) EMBO J. , vol.20 , pp. 2293-2303
    • Toro, I.1    Thore, S.2    Mayer, C.3    Basquin, J.4    Seraphin, B.5    Suck, D.6
  • 16
    • 36248940726 scopus 로고    scopus 로고
    • An Hfq-like protein in archaea: crystal structure and functional characterization of the Sm protein from Methanococcus jannaschii
    • Nielsen J.S., Bøggild A., Andersen C.B., Nielsen G., Boysen A., Brodersen D.E., Valentin-Hansen P. An Hfq-like protein in archaea: crystal structure and functional characterization of the Sm protein from Methanococcus jannaschii. RNA 2007, 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
  • 17
    • 0036714801 scopus 로고    scopus 로고
    • Predicted structure and phyletic distribution of the RNA-binding protein Hfq
    • Sun X.G., Zhulin I., Wartell R.M. Predicted structure and phyletic distribution of the RNA-binding protein Hfq. Nucleic Acids Res. 2002, 30:3662-3671.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3662-3671
    • Sun, X.G.1    Zhulin, I.2    Wartell, R.M.3
  • 19
    • 68949147832 scopus 로고    scopus 로고
    • The Acinetobacter baylyi Hfq gene encodes a large protein with an unusual C terminus
    • Schilling D., Gerischer U. The Acinetobacter baylyi Hfq gene encodes a large protein with an unusual C terminus. J. Bacteriol. 2009, 191:5553-5562.
    • (2009) J. Bacteriol. , vol.191 , pp. 5553-5562
    • Schilling, D.1    Gerischer, U.2
  • 20
    • 1842453716 scopus 로고    scopus 로고
    • Controlling mRNA stability and translation with small, noncoding RNAs
    • Storz G., Opdyke J.A., Zhang A. Controlling mRNA stability and translation with small, noncoding RNAs. Curr. Opin. Microbiol. 2004, 7:140-144.
    • (2004) Curr. Opin. Microbiol. , vol.7 , pp. 140-144
    • Storz, G.1    Opdyke, J.A.2    Zhang, A.3
  • 21
    • 1642565815 scopus 로고    scopus 로고
    • The bacterial Sm-like protein Hfq: a key player in RNA transactions
    • Valentin-Hansen P., Eriksen M., Udesen C. The bacterial Sm-like protein Hfq: a key player in RNA transactions. Mol. Microbiol. 2004, 51:1525-1533.
    • (2004) Mol. Microbiol. , vol.51 , pp. 1525-1533
    • Valentin-Hansen, P.1    Eriksen, M.2    Udesen, C.3
  • 22
    • 58149139033 scopus 로고    scopus 로고
    • A rough guide to the non-coding RNA world of Salmonella
    • Vogel J. A rough guide to the non-coding RNA world of Salmonella. Mol. Microbiol. 2009, 71:1-11.
    • (2009) Mol. Microbiol. , vol.71 , pp. 1-11
    • Vogel, J.1
  • 23
    • 60149089144 scopus 로고    scopus 로고
    • Regulatory RNAs in bacteria
    • Waters L.S., Storz G. Regulatory RNAs in bacteria. Cell 2009, 136:615-628.
    • (2009) Cell , vol.136 , pp. 615-628
    • Waters, L.S.1    Storz, G.2
  • 24
    • 0017227834 scopus 로고
    • Site-specific interaction of Qbeta host factor and ribosomal protein S1 with Qbeta and R17 bacteriophage RNAs
    • Senear A.W., Steitz J.A. Site-specific interaction of Qbeta host factor and ribosomal protein S1 with Qbeta and R17 bacteriophage RNAs. J. Biol. Chem. 1976, 251:1902-1912.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1902-1912
    • Senear, A.W.1    Steitz, J.A.2
  • 25
    • 0019254853 scopus 로고
    • Interaction of Escherichia coli host factor protein with oligoriboadenylates
    • de Haseth P.L., Uhlenbeck O.C. Interaction of Escherichia coli host factor protein with oligoriboadenylates. Biochemistry 1980, 19:6138-6146.
    • (1980) Biochemistry , vol.19 , pp. 6138-6146
    • de Haseth, P.L.1    Uhlenbeck, O.C.2
  • 26
    • 0019256070 scopus 로고
    • Interaction of Escherichia coli host factor protein with Q beta ribonucleic acid
    • de Haseth P.L., Uhlenbeck O.C. Interaction of Escherichia coli host factor protein with Q beta ribonucleic acid. Biochemistry 1980, 19:6146-6151.
    • (1980) Biochemistry , vol.19 , pp. 6146-6151
    • de Haseth, P.L.1    Uhlenbeck, O.C.2
  • 27
    • 0036163624 scopus 로고    scopus 로고
    • The Sm-like Hfq protein increases OxyS RNA interaction with target mRNAs
    • Zhang A., Wassarman K.M., Ortega J., Steven A.C., Storz G. The Sm-like Hfq protein increases OxyS RNA interaction with target mRNAs. Mol. Cell 2002, 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
  • 29
    • 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. Base-pairing requirement for RNA silencing by a bacterial small RNA and acceleration of duplex formation by Hfq. Mol. Microbiol. 2006, 61:1013-1022.
    • (2006) Mol. Microbiol. , vol.61 , pp. 1013-1022
    • Kawamoto, H.1    Koide, Y.2    Morita, T.3    Aiba, H.4
  • 30
    • 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., Regnier P., Ha T. Spectroscopic observation of RNA chaperone activities of Hfq in post-transcriptional regulation by a small non-coding RNA. Nucleic Acids Res. 2007, 35:999-1006.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 999-1006
    • Arluison, V.1    Hohng, S.2    Roy, R.3    Pellegrini, O.4    Regnier, P.5    Ha, T.6
  • 31
    • 36249019206 scopus 로고    scopus 로고
    • Dissecting RNA chaperone activity
    • Rajkowitsch L., Schroeder R. Dissecting RNA chaperone activity. RNA 2007, 13:2053-2060.
    • (2007) RNA , vol.13 , pp. 2053-2060
    • Rajkowitsch, L.1    Schroeder, R.2
  • 32
    • 50649097486 scopus 로고    scopus 로고
    • The rpoS mRNA leader recruits Hfq to facilitate annealing with DsrA sRNA
    • Soper T.J., Woodson S.A. The rpoS mRNA leader recruits Hfq to facilitate annealing with DsrA sRNA. RNA 2008, 14:1907-1917.
    • (2008) RNA , vol.14 , pp. 1907-1917
    • Soper, T.J.1    Woodson, S.A.2
  • 34
    • 16544365115 scopus 로고    scopus 로고
    • Escherichia coli Hfq has distinct interaction surfaces for DsrA, rpoS and poly(A) RNAs
    • Mikulecky P.J. Escherichia coli Hfq has distinct interaction surfaces for DsrA, rpoS and poly(A) RNAs. Nat. Struct. Mol. Biol. 2004, 11:1206-1214.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 1206-1214
    • Mikulecky, P.J.1
  • 35
    • 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 R.M. Escherichia coli Hfq binds A18 and DsrA domain II with similar 2:1 Hfq6/RNA stoichiometry using different surface sites. Biochemistry 2006, 45:4875-4887.
    • (2006) Biochemistry , vol.45 , pp. 4875-4887
    • Sun, X.1    Wartell, R.M.2
  • 36
    • 0034652188 scopus 로고    scopus 로고
    • Host factor Hfq of Escherichia coli stimulates elongation of poly(A) tails by poly(A) polymerase I
    • 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, 97:1501-1505.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 1501-1505
    • Hajnsdorf, E.1    Régnier, P.2
  • 37
    • 7044285063 scopus 로고    scopus 로고
    • The Sm-like protein Hfq regulates polyadenylation dependent mRNA decay in Escherichia coli
    • Mohanty B.K., Maples V.F., Kushner S.R. The Sm-like protein Hfq regulates polyadenylation dependent mRNA decay in Escherichia coli. Mol. Microbiol. 2004, 54:905-920.
    • (2004) Mol. Microbiol. , vol.54 , pp. 905-920
    • Mohanty, B.K.1    Maples, V.F.2    Kushner, S.R.3
  • 38
    • 1542320707 scopus 로고    scopus 로고
    • Hfq, a new chaperoning role: binding to messenger RNA determines access for small RNA regulator
    • Geissmann T.A., Touati D. Hfq, a new chaperoning role: binding to messenger RNA determines access for small RNA regulator. EMBO J. 2004, 23:396-405.
    • (2004) EMBO J. , vol.23 , pp. 396-405
    • Geissmann, T.A.1    Touati, D.2
  • 39
    • 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. Functional replacement of the Escherichia coli hfq gene by the homologue of Pseudomonas aeruginosa. Microbiology 2002, 148:883-891.
    • (2002) Microbiology , vol.148 , pp. 883-891
    • Sonnleitner, E.1    Moll, I.2    Bläsi, U.3
  • 41
    • 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 C.M., Rolle K., Vogel J. 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. 2009, 6:266-275.
    • (2009) RNA Biol. , vol.6 , pp. 266-275
    • Sittka, A.1    Sharma, C.M.2    Rolle, K.3    Vogel, J.4
  • 44
    • 0345077411 scopus 로고
    • Promoters largely determine the efficiency of repressor action
    • Lanzer M., Bujard H. Promoters largely determine the efficiency of repressor action. Proc. Natl Acad. Sci. USA 1988, 85:8973-8977.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 8973-8977
    • Lanzer, M.1    Bujard, H.2
  • 45
    • 0031816179 scopus 로고    scopus 로고
    • The Escherichia coli relBE genes belong to a new toxin-antitoxin gene family
    • Gotfredsen M., Gerdes K. The Escherichia coli relBE genes belong to a new toxin-antitoxin gene family. Mol. Microbiol. 1998, 29:1065-1076.
    • (1998) Mol. Microbiol. , vol.29 , pp. 1065-1076
    • Gotfredsen, M.1    Gerdes, K.2
  • 46
    • 0017887815 scopus 로고
    • Regulation of the deo operon in Escherichia coli: the double negative control of the deo operon by the cytR and deoR repressors in a DNA directed in vitro system
    • Valentin-Hansen P., Svenningsen B.A., Munch-Petersen A., Hammer-Jespersen K. Regulation of the deo operon in Escherichia coli: the double negative control of the deo operon by the cytR and deoR repressors in a DNA directed in vitro system. Mol. Gen. Genet. 1978, 159:191-202.
    • (1978) Mol. Gen. Genet. , vol.159 , pp. 191-202
    • Valentin-Hansen, P.1    Svenningsen, B.A.2    Munch-Petersen, A.3    Hammer-Jespersen, K.4
  • 47
    • 0029889596 scopus 로고    scopus 로고
    • Efficient translation of the RpoS sigma factor in Salmonella typhimurium requires host factor I, an RNA-binding protein encoded by the hfq gene
    • Brown L., Elliott T. Efficient translation of the RpoS sigma factor in Salmonella typhimurium requires host factor I, an RNA-binding protein encoded by the hfq gene. J. Bacteriol. 1996, 178:3763-3770.
    • (1996) J. Bacteriol. , vol.178 , pp. 3763-3770
    • Brown, L.1    Elliott, T.2
  • 48
    • 0029897937 scopus 로고    scopus 로고
    • The RNA-binding protein HF-I, known as a host factor for phage Q beta RNA replication, is essential for rpoS translation in Escherichia coli
    • Muffler A., Fischer D., HenggeAronis R. The RNA-binding protein HF-I, known as a host factor for phage Q beta RNA replication, is essential for rpoS translation in Escherichia coli. Genes Dev. 1996, 10:1143-1151.
    • (1996) Genes Dev. , vol.10 , pp. 1143-1151
    • Muffler, A.1    Fischer, D.2    HenggeAronis, R.3
  • 49
    • 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 sigma(s) subunit of RNA polymerase in Escherichia coli
    • Muffler A., Traulsen D.D., Fischer D., Lange R., HenggeAronis 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 sigma(s) subunit of RNA polymerase in Escherichia coli. J. Bacteriol. 1997, 179:297-300.
    • (1997) J. Bacteriol. , vol.179 , pp. 297-300
    • Muffler, A.1    Traulsen, D.D.2    Fischer, D.3    Lange, R.4    HenggeAronis, R.5
  • 50
    • 0031015418 scopus 로고    scopus 로고
    • Mutations that increase expression of the rpoS gene and decrease its dependence on hfq function in Salmonella typhimurium
    • Brown L., Elliott T. Mutations that increase expression of the rpoS gene and decrease its dependence on hfq function in Salmonella typhimurium. J. Bacteriol. 1997, 179:656-662.
    • (1997) J. Bacteriol. , vol.179 , pp. 656-662
    • Brown, L.1    Elliott, T.2
  • 51
    • 0038187589 scopus 로고    scopus 로고
    • Small non-coding RNAs, co-ordinators of adaptation processes in Escherichia coli: the RpoS paradigm
    • Repoila F., Majdalani N., Gottesman S. Small non-coding RNAs, co-ordinators of adaptation processes in Escherichia coli: the RpoS paradigm. Mol. Microbiol. 2003, 48:855-861.
    • (2003) Mol. Microbiol. , vol.48 , pp. 855-861
    • Repoila, F.1    Majdalani, N.2    Gottesman, S.3
  • 54
    • 20644462362 scopus 로고    scopus 로고
    • Micros for microbes: non-coding regulatory RNAs in bacteria
    • Gottesman S. Micros for microbes: non-coding regulatory RNAs in bacteria. Trends Genet. 2005, 21:399-404.
    • (2005) Trends Genet. , vol.21 , pp. 399-404
    • Gottesman, S.1
  • 55
    • 0141860088 scopus 로고    scopus 로고
    • Coupled degradation of a small regulatory RNA and its mRNA targets in Escherichia coli
    • Massé E., Escorcia F.E., Gottesman S. Coupled degradation of a small regulatory RNA and its mRNA targets in Escherichia coli. Genes Dev. 2003, 17:2374-2383.
    • (2003) Genes Dev. , vol.17 , pp. 2374-2383
    • Massé, E.1    Escorcia, F.E.2    Gottesman, S.3
  • 59
    • 34447542213 scopus 로고    scopus 로고
    • A small RNA downregulates LamB maltoporin in Salmonella
    • Bossi L., Figueroa-Bossi N. A small RNA downregulates LamB maltoporin in Salmonella. Mol. Microbiol. 2007, 65:799-810.
    • (2007) Mol. Microbiol. , vol.65 , pp. 799-810
    • Bossi, L.1    Figueroa-Bossi, N.2
  • 62
    • 33744950278 scopus 로고    scopus 로고
    • Down-regulation of porins by a small RNA bypasses the essentiality of the regulated intramembrane proteolysis protease RseP in Escherichia coli
    • Douchin V., Bohn C., Bouloc P. Down-regulation of porins by a small RNA bypasses the essentiality of the regulated intramembrane proteolysis protease RseP in Escherichia coli. J. Biol. Chem. 2006, 281:12253-12259.
    • (2006) J. Biol. Chem. , vol.281 , pp. 12253-12259
    • Douchin, V.1    Bohn, C.2    Bouloc, P.3
  • 64
    • 69749123311 scopus 로고    scopus 로고
    • Caught at its own game: regulatory small RNA inactivated by an inducible transcript mimicking its target
    • Figueroa-Bossi N., Valentini M., Malleret L., Fiorini F., Bossi L. Caught at its own game: regulatory small RNA inactivated by an inducible transcript mimicking its target. Genes Dev. 2009, 23:2004-2015.
    • (2009) Genes Dev. , vol.23 , pp. 2004-2015
    • Figueroa-Bossi, N.1    Valentini, M.2    Malleret, L.3    Fiorini, F.4    Bossi, L.5
  • 66
    • 70349946771 scopus 로고    scopus 로고
    • An RNA trap helps bacteria get the most out of chitosugars
    • Vogel J. An RNA trap helps bacteria get the most out of chitosugars. Mol. Microbiol. 2009, 73:737-741.
    • (2009) Mol. Microbiol. , vol.73 , pp. 737-741
    • Vogel, J.1
  • 67
    • 69749101520 scopus 로고    scopus 로고
    • Regulating the regulator: an RNA decoy acts as an OFF switch for the regulation of an sRNA
    • Mandin P., Gottesman S. Regulating the regulator: an RNA decoy acts as an OFF switch for the regulation of an sRNA. Genes Dev. 2009, 23:1981-1985.
    • (2009) Genes Dev. , vol.23 , pp. 1981-1985
    • Mandin, P.1    Gottesman, S.2
  • 68
    • 34247158257 scopus 로고    scopus 로고
    • Mechanism of RNA silencing by Hfq-binding small RNAs
    • Aiba H. Mechanism of RNA silencing by Hfq-binding small RNAs. Curr. Opin. Microbiol. 2007, 10:134-139.
    • (2007) Curr. Opin. Microbiol. , vol.10 , pp. 134-139
    • Aiba, H.1
  • 69
    • 77349101808 scopus 로고    scopus 로고
    • Translational regulation of gene expression by an anaerobically induced small non-coding RNA in Escherichia coli
    • Boysen A., Møller-Jensen J., Kallipolitis B., Valentin-Hansen P., Overgaard M. Translational regulation of gene expression by an anaerobically induced small non-coding RNA in Escherichia coli. J. Biol. Chem. 2010, 285:10690-10702.
    • (2010) J. Biol. Chem. , vol.285 , pp. 10690-10702
    • Boysen, A.1    Møller-Jensen, J.2    Kallipolitis, B.3    Valentin-Hansen, P.4    Overgaard, M.5
  • 70
    • 77349104885 scopus 로고    scopus 로고
    • Reprogramming of anaerobic metabolism by the FnrS small RNA
    • Durand S., Storz G. Reprogramming of anaerobic metabolism by the FnrS small RNA. Mol. Microbiol. 2010, 75:1215-1231.
    • (2010) Mol. Microbiol. , vol.75 , pp. 1215-1231
    • Durand, S.1    Storz, G.2
  • 72
    • 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. Cellular electron microscopy imaging reveals the localization of the Hfq protein close to the bacterial membrane. PLoS One 2009, 4:e8301.
    • (2009) PLoS One , vol.4
    • Diestra, E.1    Cayrol, B.2    Arluison, V.3    Risco, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.