메뉴 건너뛰기




Volumn 192, Issue 6, 2010, Pages 1710-1718

The Sinorhizobium meliloti RNA chaperone Hfq mediates symbiosis of S. meliloti and alfalfa

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CHAPERONE PROTEIN HFQ; SUCCINOGLYCAN; UNCLASSIFIED DRUG;

EID: 77949373122     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01427-09     Document Type: Article
Times cited : (33)

References (70)
  • 1
    • 34247158257 scopus 로고    scopus 로고
    • Mechanism of RNA silencing by Hfq-binding small RNAs
    • Aiba, H. 2007. Mechanism of RNA silencing by Hfq-binding small RNAs. Curr. Opin. Microbiol. 10:134-139.
    • (2007) Curr. Opin. Microbiol , vol.10 , pp. 134-139
    • Aiba, H.1
  • 2
    • 33847363604 scopus 로고    scopus 로고
    • Spectroscopic observation of RNA chaperone activities of Hfq in posttranscriptional regulation by a small non-coding RNA
    • Arluison, V., S. Hohng, R. Roy, O. Pellegrini, P. Regnier, and T. Ha. 2007. Spectroscopic observation of RNA chaperone activities of Hfq in posttranscriptional regulation by a small non-coding RNA. Nucleic Acids Res. 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
  • 3
    • 17644407666 scopus 로고    scopus 로고
    • Alternative sigma factor interactions in Salmonella: Sigma and sigma promote antioxidant defences by enhancing sigma levels
    • Bang, I. S., J. G. Frye, M. McClelland, J. Velayudhan, and F. C. Fang. 2005. Alternative sigma factor interactions in Salmonella: sigma and sigma promote antioxidant defences by enhancing sigma levels. Mol. Microbiol. 56: 811-823.
    • (2005) Mol. Microbiol , vol.56 , pp. 811-823
    • Bang, I.S.1    Frye, J.G.2    McClelland, M.3    Velayudhan, J.4    Fang, F.C.5
  • 4
    • 77949383248 scopus 로고    scopus 로고
    • Barra-Bily, L., C. Fontenelle, G. Jan, M. Flechard, A. Trautwetter, S. P. Pandey, G. C. Walker, and C. Blanco. 2010. Proteomic alterations explain phenotypic changes in Sinorhizobium meliloti lacking the RNA chaperone Hfq. J. Bacteriol. 192:1719-1729.
    • Barra-Bily, L., C. Fontenelle, G. Jan, M. Flechard, A. Trautwetter, S. P. Pandey, G. C. Walker, and C. Blanco. 2010. Proteomic alterations explain phenotypic changes in Sinorhizobium meliloti lacking the RNA chaperone Hfq. J. Bacteriol. 192:1719-1729.
  • 5
    • 0029125099 scopus 로고
    • New gentamicinresistance and lacZ promoter-probe cassettes suitable for insertion mutagenesis and generation of transcriptional fusions
    • Becker, A., M. Schmidt, W. Jager, and A. Puhler. 1995. New gentamicinresistance and lacZ promoter-probe cassettes suitable for insertion mutagenesis and generation of transcriptional fusions. Gene 162:37-39.
    • (1995) Gene , vol.162 , pp. 37-39
    • Becker, A.1    Schmidt, M.2    Jager, W.3    Puhler, A.4
  • 6
    • 0000124479 scopus 로고
    • Rhizobium-meliloti genes encoding catabolism of trigonelline are induced under symbiotic conditions
    • Boivin, C., S. Camut, C. A. Malpica, G. Truchet, and C. Rosenberg. 1990. Rhizobium-meliloti genes encoding catabolism of trigonelline are induced under symbiotic conditions. Plant Cell 2:1157-1170.
    • (1990) Plant Cell , vol.2 , pp. 1157-1170
    • Boivin, C.1    Camut, S.2    Malpica, C.A.3    Truchet, G.4    Rosenberg, C.5
  • 7
    • 34247109118 scopus 로고    scopus 로고
    • Hfq structure, function and ligand binding
    • Brennan, R. G., and T. M. Link. 2007. Hfq structure, function and ligand binding. Curr. Opin. Microbiol. 10:125-133.
    • (2007) Curr. Opin. Microbiol , vol.10 , pp. 125-133
    • Brennan, R.G.1    Link, T.M.2
  • 8
    • 0037276123 scopus 로고    scopus 로고
    • Identification of the Hfq-binding site on DsrA RNA: Hfq binds without altering DsrA secondary structure
    • Brescia, C. C., P. J. Mikulecky, A. L. Feig, and D. D. Sledjeski. 2003. Identification of the Hfq-binding site on DsrA RNA: Hfq binds without altering DsrA secondary structure. RNA 9:33-43.
    • (2003) RNA , vol.9 , pp. 33-43
    • Brescia, C.C.1    Mikulecky, P.J.2    Feig, A.L.3    Sledjeski, D.D.4
  • 9
    • 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., and T. Elliott. 1996. 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. 178:3763-3770.
    • (1996) J. Bacteriol , vol.178 , pp. 3763-3770
    • Brown, L.1    Elliott, T.2
  • 10
    • 0028696589 scopus 로고
    • Genetic regulation of nitrogen fixation in Rhizobium meliloti
    • Cebolla, A., and A. J. Palomares. 1994. Genetic regulation of nitrogen fixation in Rhizobium meliloti. Microbiologia 10:371-384.
    • (1994) Microbiologia , vol.10 , pp. 371-384
    • Cebolla, A.1    Palomares, A.J.2
  • 11
    • 0031661531 scopus 로고    scopus 로고
    • Succinoglycan is required for initiation and elongation of infection threads during nodulation of alfalfa by Rhizobium meliloti
    • Cheng, H. P., and G. C. Walker. 1998. Succinoglycan is required for initiation and elongation of infection threads during nodulation of alfalfa by Rhizobium meliloti. J. Bacteriol. 180:5183-5191.
    • (1998) J. Bacteriol , vol.180 , pp. 5183-5191
    • Cheng, H.P.1    Walker, G.C.2
  • 12
    • 36148952518 scopus 로고    scopus 로고
    • Identification of differentially expressed small non-coding RNAs in the legume endosymbiont Sinorhizobium meliloti by comparative genomics
    • del Val, C., E. Rivas, O. Torres-Quesada, N. Toro, and J. I. Jimenez-Zurdo. 2007. Identification of differentially expressed small non-coding RNAs in the legume endosymbiont Sinorhizobium meliloti by comparative genomics. Mol. Microbiol. 66:1080-1091.
    • (2007) Mol. Microbiol , vol.66 , pp. 1080-1091
    • del Val, C.1    Rivas, E.2    Torres-Quesada, O.3    Toro, N.4    Jimenez-Zurdo, J.I.5
  • 13
    • 3142550776 scopus 로고    scopus 로고
    • Hfq is essential for Vibrio cholerae virulence and downregulates sigma expression
    • Ding, Y., B. M. Davis, and M. K. Waldor .2004. Hfq is essential for Vibrio cholerae virulence and downregulates sigma expression. Mol. Microbiol. 53:345-354.
    • (2004) Mol. Microbiol , vol.53 , pp. 345-354
    • Ding, Y.1    Davis, B.M.2    Waldor, M.K.3
  • 14
    • 0037044479 scopus 로고    scopus 로고
    • The Hfq-like protein NrfA of the phototrophic purple bacterium Rhodobacter capsulatus controls nitrogen fixation via regulation of nifA and anfA expression
    • Drepper, T., K. Raabe, D. Giaourakis, M. Gendrullis, B. Masepohl, and W. Klipp .2002. The Hfq-like protein NrfA of the phototrophic purple bacterium Rhodobacter capsulatus controls nitrogen fixation via regulation of nifA and anfA expression. FEMS Microbiol. Lett. 215:221-227.
    • (2002) FEMS Microbiol. Lett , vol.215 , pp. 221-227
    • Drepper, T.1    Raabe, K.2    Giaourakis, D.3    Gendrullis, M.4    Masepohl, B.5    Klipp, W.6
  • 15
    • 65449172051 scopus 로고    scopus 로고
    • The RNA chaperone Hfq is involved in stress response and virulence in Neisseria meningitidis and is a pleiotropic regulator of protein expression
    • Fantappiè, L., M. M. E. Metruccio, K. L. Seib, F. Oriente, E. Cartocci, F. Ferlicca, M. M. Giuliani, V. Scarlato, and I. Delany .2009. The RNA chaperone Hfq is involved in stress response and virulence in Neisseria meningitidis and is a pleiotropic regulator of protein expression. Infect. Immun. 77:1842-1853.
    • (2009) Infect. Immun , vol.77 , pp. 1842-1853
    • Fantappiè, L.1    Metruccio, M.M.E.2    Seib, K.L.3    Oriente, F.4    Cartocci, E.5    Ferlicca, F.6    Giuliani, M.M.7    Scarlato, V.8    Delany, I.9
  • 16
    • 1842737601 scopus 로고    scopus 로고
    • Similarity to peroxisomal-membrane protein family reveals that Sinorhizobium and Brucella BacA affect lipid-A fatty acids
    • Ferguson, G. P., A. Datta, J. Baumgartner, R. M. Roop, R. W. Carlson, and G. C. Walker .2004. Similarity to peroxisomal-membrane protein family reveals that Sinorhizobium and Brucella BacA affect lipid-A fatty acids. Proc. Natl. Acad. Sci. U. S. A. 101:5012-5017.
    • (2004) Proc. Natl. Acad. Sci. U. S. A , vol.101 , pp. 5012-5017
    • Ferguson, G.P.1    Datta, A.2    Baumgartner, J.3    Roop, R.M.4    Carlson, R.W.5    Walker, G.C.6
  • 17
    • 0035958746 scopus 로고    scopus 로고
    • Galibert, F., T. M. Finan, S. R. Long, A. Puhler, P. Abola, F. Ampe, F. Barloy-Hubler, M. J. Barnett, A. Becker, P. Boistard, G. Bothe, M. Boutry, L. Bowser, J. Buhrmester, E. Cadieu, D. Capela, P. Chain, A. Cowie, R. W. Davis, S. Dreano, N. A. Federspiel, R. F. Fisher, S. Gloux, T. Godrie, A. Goffeau, B. Golding, J. Gouzy, M. Gurjal, I. Hernandez-Lucas, A. Hong, L. Huizar, R. W. Hyman, T. Jones, D. Kahn, M. L. Kahn, S. Kalman, D. H. Keating, E. Kiss, C. Komp, V. Lalaure, D. Masuy, C. Palm, M. C. Peck, T. M. Pohl, D. Portetelle, B. Purnelle, U. Ramsperger, R. Surzycki, P. Thebault, M. Vandenbol, F. J. Vorholter, S. Weidner, D. H. Wells, K. Wong, K. C. Yeh, and J. Batut .2001. The composite genome of the legume symbiont Sinorhizobium meliloti. Science 293:668-672.
    • Galibert, F., T. M. Finan, S. R. Long, A. Puhler, P. Abola, F. Ampe, F. Barloy-Hubler, M. J. Barnett, A. Becker, P. Boistard, G. Bothe, M. Boutry, L. Bowser, J. Buhrmester, E. Cadieu, D. Capela, P. Chain, A. Cowie, R. W. Davis, S. Dreano, N. A. Federspiel, R. F. Fisher, S. Gloux, T. Godrie, A. Goffeau, B. Golding, J. Gouzy, M. Gurjal, I. Hernandez-Lucas, A. Hong, L. Huizar, R. W. Hyman, T. Jones, D. Kahn, M. L. Kahn, S. Kalman, D. H. Keating, E. Kiss, C. Komp, V. Lalaure, D. Masuy, C. Palm, M. C. Peck, T. M. Pohl, D. Portetelle, B. Purnelle, U. Ramsperger, R. Surzycki, P. Thebault, M. Vandenbol, F. J. Vorholter, S. Weidner, D. H. Wells, K. Wong, K. C. Yeh, and J. Batut .2001. The composite genome of the legume symbiont Sinorhizobium meliloti. Science 293:668-672.
  • 18
    • 0343566460 scopus 로고    scopus 로고
    • Sinorhizobium meliloti nfe (nodulation formation efficiency) genes exhibit temporal and spatial expression patterns similar to those of genes involved in symbiotic nitrogen fixation
    • Garcia-Rodriguez, F. M., and N. Toro .2000. Sinorhizobium meliloti nfe (nodulation formation efficiency) genes exhibit temporal and spatial expression patterns similar to those of genes involved in symbiotic nitrogen fixation. Mol. Plant Microbe Interact. 13:583-591.
    • (2000) Mol. Plant Microbe Interact , vol.13 , pp. 583-591
    • Garcia-Rodriguez, F.M.1    Toro, N.2
  • 19
    • 1542320707 scopus 로고    scopus 로고
    • Hfq, a new chaperoning role: Binding to messenger RNA determines access for small RNA regulator
    • Geissmann, T. A., and D. Touati .2004. Hfq, a new chaperoning role: binding to messenger RNA determines access for small RNA regulator. EMBO J. 23:396-405.
    • (2004) EMBO J , vol.23 , pp. 396-405
    • Geissmann, T.A.1    Touati, D.2
  • 20
    • 58549105954 scopus 로고    scopus 로고
    • Molecular determinants of a symbiotic chronic infection
    • Gibson, K. E., H. Kobayashi, and G. C. Walker .2008. Molecular determinants of a symbiotic chronic infection. Annu. Rev. Genet. 42:413-441.
    • (2008) Annu. Rev. Genet , vol.42 , pp. 413-441
    • Gibson, K.E.1    Kobayashi, H.2    Walker, G.C.3
  • 21
    • 0027291609 scopus 로고
    • A Rhizobium-meliloti homolog of the Escherichia-coli peptide antibiotic transport protein sbma is essential for bacteroid development
    • Glazebrook, J., A. Ichige, and G. C. Walker .1993. A Rhizobium-meliloti homolog of the Escherichia-coli peptide antibiotic transport protein sbma is essential for bacteroid development. Genes Dev. 7:1485-1497.
    • (1993) Genes Dev , vol.7 , pp. 1485-1497
    • Glazebrook, J.1    Ichige, A.2    Walker, G.C.3
  • 22
    • 34548637112 scopus 로고    scopus 로고
    • Disruption of nifA Gene influences multiple cellular processes in Sinorhizobium meliloti
    • Gong, Z., J. Zhu, G. Yu, and H. Zou .2007. Disruption of nifA Gene influences multiple cellular processes in Sinorhizobium meliloti. J. Genet. Genomics 34:783-789.
    • (2007) J. Genet. Genomics , vol.34 , pp. 783-789
    • Gong, Z.1    Zhu, J.2    Yu, G.3    Zou, H.4
  • 23
    • 20644462362 scopus 로고    scopus 로고
    • Micros for microbes: Non-coding regulatory RNAs in bacteria
    • Gottesman, S .2005. Micros for microbes: non-coding regulatory RNAs in bacteria. Trends Genet. 21:399-404.
    • (2005) Trends Genet , vol.21 , pp. 399-404
    • Gottesman, S.1
  • 24
    • 4344682527 scopus 로고    scopus 로고
    • The small RNA regulators of Escherichia coli: Roles and mechanisms
    • Gottesman, S .2004. The small RNA regulators of Escherichia coli: roles and mechanisms. Annu. Rev. Microbiol. 58:303-328.
    • (2004) Annu. Rev. Microbiol , vol.58 , pp. 303-328
    • Gottesman, S.1
  • 26
    • 33947361601 scopus 로고    scopus 로고
    • E-mediated envelope stress response and the sigma32-mediated cytoplasmic stress response in Escherichia coli
    • E-mediated envelope stress response and the sigma32-mediated cytoplasmic stress response in Escherichia coli. J. Bacteriol. 189: 1963-1973.
    • (2007) J. Bacteriol , vol.189 , pp. 1963-1973
    • Guisbert, E.1    Rhodius, V.A.2    Ahuja, N.3    Witkin, E.4    Gross, C.A.5
  • 27
    • 0034652188 scopus 로고    scopus 로고
    • Host factor Hfq of Escherichia coli stimulates elongation of poly(A) tails by poly(A) polymerase I
    • Hajnsdorf, E., and P. Regnier .2000. Host factor Hfq of Escherichia coli stimulates elongation of poly(A) tails by poly(A) polymerase I. Proc. Natl. Acad. Sci. U. S. A. 97:1501-1505.
    • (2000) Proc. Natl. Acad. Sci. U. S. A , vol.97 , pp. 1501-1505
    • Hajnsdorf, E.1    Regnier, P.2
  • 28
    • 0031020858 scopus 로고    scopus 로고
    • Genetic analysis of the Rhizobium meliloti bacA gene: Functional interchangeability with the Escherichia coli sbmA gene and phenotypes of mutants
    • Ichige, A., and G. C. Walker .1997. Genetic analysis of the Rhizobium meliloti bacA gene: functional interchangeability with the Escherichia coli sbmA gene and phenotypes of mutants. J. Bacteriol. 179:209-216.
    • (1997) J. Bacteriol , vol.179 , pp. 209-216
    • Ichige, A.1    Walker, G.C.2
  • 29
    • 0037370853 scopus 로고    scopus 로고
    • Expression of the bacterial catalase genes during Sinorhizobium meliloti-Medicago sativa symbiosis and their crucial role during the infection process
    • Jamet, A., S. Sigaud, G. Van de Sype, A. Puppo, and D. Herouart .2003. Expression of the bacterial catalase genes during Sinorhizobium meliloti-Medicago sativa symbiosis and their crucial role during the infection process. Mol. Plant Microbe Interact. 16:217-225.
    • (2003) Mol. Plant Microbe Interact , vol.16 , pp. 217-225
    • Jamet, A.1    Sigaud, S.2    Van de Sype, G.3    Puppo, A.4    Herouart, D.5
  • 31
    • 0031979601 scopus 로고    scopus 로고
    • Kaminski, P. A., and C. Elmerich .1998. The control of Azorhizobium caulinodans nifA expression by oxygen, ammonia and by the HF-I-like protein, NrfA. Mol. Microbiol. 28:603-613.
    • Kaminski, P. A., and C. Elmerich .1998. The control of Azorhizobium caulinodans nifA expression by oxygen, ammonia and by the HF-I-like protein, NrfA. Mol. Microbiol. 28:603-613.
  • 32
    • 0028793123 scopus 로고
    • 4 new derivatives of the broad-host-range cloning vector pbbr1mcs, carrying different antibiotic-resistance cassettes
    • Kovach, M. E., P. H. Elzer, D. S. Hill, G. T. Robertson, M. A. Farris, R. M. Roop, and K. M. Peterson .1995. 4 new derivatives of the broad-host-range cloning vector pbbr1mcs, carrying different antibiotic-resistance cassettes. Gene 166:175-176.
    • (1995) Gene , vol.166 , pp. 175-176
    • Kovach, M.E.1    Elzer, P.H.2    Hill, D.S.3    Robertson, G.T.4    Farris, M.A.5    Roop, R.M.6    Peterson, K.M.7
  • 33
    • 46449132381 scopus 로고    scopus 로고
    • Impact of the RNA chaperone Hfq on the fitness and virulence potential of uropathogenic Escherichia coli
    • Kulesus, R. R., K. Diaz-Perez, E. S. Slechta, D. S. Eto, and M. A. Mulvey. 2008. Impact of the RNA chaperone Hfq on the fitness and virulence potential of uropathogenic Escherichia coli. Infect. Immun. 76:3019-3026.
    • (2008) Infect. Immun , vol.76 , pp. 3019-3026
    • Kulesus, R.R.1    Diaz-Perez, K.2    Slechta, E.S.3    Eto, D.S.4    Mulvey, M.A.5
  • 34
    • 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
    • Le Derout, J., M. Folichon, F. Briani, G. Deho, P. Regnier, and E. Hajnsdorf. 2003. Hfq affects the length and the frequency of short oligo(A) tails at the 3′ end of Escherichia coli rpsO mRNAs. Nucleic Acids Res. 31:4017-4023.
    • (2003) Nucleic Acids Res , vol.31 , pp. 4017-4023
    • Le Derout, J.1    Folichon, M.2    Briani, F.3    Deho, G.4    Regnier, P.5    Hajnsdorf, E.6
  • 35
    • 0010269952 scopus 로고
    • Exopolysaccharidedeficient mutants of Rhizobium-meliloti that form ineffective nodules
    • Leigh, J. A., E. R. Signer, and G. C. Walker .1985. Exopolysaccharidedeficient mutants of Rhizobium-meliloti that form ineffective nodules. Proc. Natl. Acad. Sci. U. S. A. 82:6231-6235.
    • (1985) Proc. Natl. Acad. Sci. U. S. A , vol.82 , pp. 6231-6235
    • Leigh, J.A.1    Signer, E.R.2    Walker, G.C.3
  • 36
    • 0034737819 scopus 로고    scopus 로고
    • Similar requirements of a plant symbiont and a mammalian pathogen for prolonged intracellular survival
    • LeVier, K., R. W. Phillips, V. K. Grippe, R. M. Roop, and G. C. Walker .2000. Similar requirements of a plant symbiont and a mammalian pathogen for prolonged intracellular survival. Science 287:2492-2493.
    • (2000) Science , vol.287 , pp. 2492-2493
    • LeVier, K.1    Phillips, R.W.2    Grippe, V.K.3    Roop, R.M.4    Walker, G.C.5
  • 39
    • 62649148439 scopus 로고    scopus 로고
    • Essential role for the BacA protein in the uptake of a truncated eukaryotic peptide in Sinorhizobium meliloti
    • Marlow, V. L., A. F. Haag, H. Kobayashi, V. Fletcher, M. Scocchi, G. C. Walker, and G. P. Ferguson .2009. Essential role for the BacA protein in the uptake of a truncated eukaryotic peptide in Sinorhizobium meliloti. J. Bacteriol. 191:1519-1527.
    • (2009) J. Bacteriol , vol.191 , pp. 1519-1527
    • Marlow, V.L.1    Haag, A.F.2    Kobayashi, H.3    Fletcher, V.4    Scocchi, M.5    Walker, G.C.6    Ferguson, G.P.7
  • 41
    • 14544288359 scopus 로고    scopus 로고
    • The Hfq homolog in Legionella pneumophila demonstrates regulation by LetA and RpoS and interacts with the global regulator CsrA
    • McNealy, T. L., V. Forsbach-Birk, C. W. Shi, and R. Marre .2005. The Hfq homolog in Legionella pneumophila demonstrates regulation by LetA and RpoS and interacts with the global regulator CsrA. J. Bacteriol. 187:1527-1532.
    • (2005) J. Bacteriol , vol.187 , pp. 1527-1532
    • McNealy, T.L.1    Forsbach-Birk, V.2    Shi, C.W.3    Marre, R.4
  • 44
    • 7044285063 scopus 로고    scopus 로고
    • The Sm-like protein Hfq regulates polyadenylation dependent mRNA decay in Escherichia coli
    • Mohanty, B. K., V. F. Maples, and S. R. Kushner .2004. The Sm-like protein Hfq regulates polyadenylation dependent mRNA decay in Escherichia coli. Mol. Microbiol. 54:905-920.
    • (2004) Mol. Microbiol , vol.54 , pp. 905-920
    • Mohanty, B.K.1    Maples, V.F.2    Kushner, S.R.3
  • 45
    • 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., D. D. Traulsen, D. Fischer, R. Lange, and R. HenggeAronis . 1997. 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. 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
  • 46
    • 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., A. Boggild, C. B. F. Andersen, G. Nielsen, A. Boysen, D. E. Brodersen, and P. Valentin-Hansen .2007. An Hfq-like protein in archaea: crystal structure and functional characterization of the Sm protein from Methanococcus jannaschii. RNA 13:2213-2223.
    • (2007) RNA , vol.13 , pp. 2213-2223
    • Nielsen, J.S.1    Boggild, A.2    Andersen, C.B.F.3    Nielsen, G.4    Boysen, A.5    Brodersen, D.E.6    Valentin-Hansen, P.7
  • 47
    • 0036791011 scopus 로고    scopus 로고
    • Paulsen, I. T., R. Seshadri, K. E. Nelson, J. A. Eisen, J. F. Heidelberg, T. D. Read, R. J. Dodson, L. Umayam, L. M. Brinkac, M. J. Beanan, S. C. Daugherty, R. T. Deboy, A. S. Durkin, J. F. Kolonay, R. Madupu, W. C. Nelson, B. Ayodeji, M. Kraul, J. Shetty, J. Malek, S. E. Van Aken, S. Riedmuller, H. Tettelin, S. R. Gill, O. White, S. L. Salzberg, D. L. Hoover, L. E. Lindler, S. M. Halling, S. M. Boyle, and C. M. Fraser .2002. The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts. Proc. Natl. Acad. Sci. U. S. A. 99:13148-13153.
    • Paulsen, I. T., R. Seshadri, K. E. Nelson, J. A. Eisen, J. F. Heidelberg, T. D. Read, R. J. Dodson, L. Umayam, L. M. Brinkac, M. J. Beanan, S. C. Daugherty, R. T. Deboy, A. S. Durkin, J. F. Kolonay, R. Madupu, W. C. Nelson, B. Ayodeji, M. Kraul, J. Shetty, J. Malek, S. E. Van Aken, S. Riedmuller, H. Tettelin, S. R. Gill, O. White, S. L. Salzberg, D. L. Hoover, L. E. Lindler, S. M. Halling, S. M. Boyle, and C. M. Fraser .2002. The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts. Proc. Natl. Acad. Sci. U. S. A. 99:13148-13153.
  • 48
    • 15444342896 scopus 로고
    • Osmoregulation by organisms exposed to saline stress: Physiological mechanisms and genetic manipulation
    • A. San Pietro ed, Plenum Publishing Corp, New York, NY
    • Rains, D. W., L. N. Csonka, D. Le Rudulier, T. P. Croughan, S. S. Yang, S. J. Stavarek, and R. C. Valentine .1982. Osmoregulation by organisms exposed to saline stress: physiological mechanisms and genetic manipulation, p. 238-302. In A. San Pietro (ed.), Biosaline research: a look to the future. Plenum Publishing Corp., New York, NY.
    • (1982) Biosaline research: A look to the future , pp. 238-302
    • Rains, D.W.1    Csonka, L.N.2    Le Rudulier, D.3    Croughan, T.P.4    Yang, S.S.5    Stavarek, S.J.6    Valentine, R.C.7
  • 49
    • 0032702842 scopus 로고    scopus 로고
    • The Brucella abortus host factor I (HF-I) protein contributes to stress resistance during stationary phase and is a major determinant of virulence in mice
    • Robertson, G. T., and R. M. Roop .1999. The Brucella abortus host factor I (HF-I) protein contributes to stress resistance during stationary phase and is a major determinant of virulence in mice. Mol. Microbiol. 34:690-700.
    • (1999) Mol. Microbiol , vol.34 , pp. 690-700
    • Robertson, G.T.1    Roop, R.M.2
  • 50
    • 33646345371 scopus 로고    scopus 로고
    • Evaluation of the dynamic structure of DsrA RNA from E-coli and its functional consequences
    • Rolle, K., M. Zywicki, E. Wyszko, M. Z. Barciszewska, and J. Barciszewski. 2006. Evaluation of the dynamic structure of DsrA RNA from E-coli and its functional consequences. J. Biochem. 139:431-438.
    • (2006) J. Biochem , vol.139 , pp. 431-438
    • Rolle, K.1    Zywicki, M.2    Wyszko, E.3    Barciszewska, M.Z.4    Barciszewski, J.5
  • 51
    • 0037146719 scopus 로고    scopus 로고
    • Seeking a niche: Putative contributions of the hfq and bacA gene products to the successful adaptation of the brucellae to their intracellular home
    • Roop, R. M., II, G. T. Robertson, G. P. Ferguson, L. E. Milford, M. E. Winkler, and G. C. Walker .2002. Seeking a niche: putative contributions of the hfq and bacA gene products to the successful adaptation of the brucellae to their intracellular home. Vet. Microbiol. 90:349-363.
    • (2002) Vet. Microbiol , vol.90 , pp. 349-363
    • Roop II, R.M.1    Robertson, G.T.2    Ferguson, G.P.3    Milford, L.E.4    Winkler, M.E.5    Walker, G.C.6
  • 54
    • 0028289983 scopus 로고
    • Small mobilizable multipurpose cloning vectors derived from the Escherichia-coli plasmids PK18 AND PK19-selection of defined deletions in the chromosome of corynebacterium-glutamicum
    • Schafer, A., A. Tauch, W. Jager, J. Kalinowski, G. Thierbach, and A. Puhler. 1994. Small mobilizable multipurpose cloning vectors derived from the Escherichia-coli plasmids PK18 AND PK19-selection of defined deletions in the chromosome of corynebacterium-glutamicum. Gene 145:69-73.
    • (1994) Gene , vol.145 , pp. 69-73
    • Schafer, A.1    Tauch, A.2    Jager, W.3    Kalinowski, J.4    Thierbach, G.5    Puhler, A.6
  • 55
    • 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., R. F. Pearson, T. Moller, P. Valentin-Hansen, and R. G. Brennan .2002. Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: a bacterial Sm-like protein. EMBO J. 21:3546-3556.
    • (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
  • 56
    • 33749177569 scopus 로고    scopus 로고
    • Induction of expression of hfq by DksA is essential for Shigella flexneri virulence
    • Sharma, A. K., and S. M. Payne .2006. Induction of expression of hfq by DksA is essential for Shigella flexneri virulence. Mol. Microbiol. 62:469-479.
    • (2006) Mol. Microbiol , vol.62 , pp. 469-479
    • Sharma, A.K.1    Payne, S.M.2
  • 57
    • 0022559895 scopus 로고
    • Plasmid vectors for the genetic-analysis and manipulation of rhizobia and other gram-negative bacteria
    • Simon, R., M. O'Connell, M. Labes, and A. Puhler .1986. Plasmid vectors for the genetic-analysis and manipulation of rhizobia and other gram-negative bacteria. Methods Enzymol. 118:640-659.
    • (1986) Methods Enzymol , vol.118 , pp. 640-659
    • Simon, R.1    O'Connell, M.2    Labes, M.3    Puhler, A.4
  • 58
    • 50849105413 scopus 로고    scopus 로고
    • Sittka, A., S. Lucchini, K. Papenfort, C. M. Sharma, K. Rolle, T. T. Binnewies, J. C. Hinton, and J. Vogel .2008. Deep sequencing analysis of small noncoding RNA and mRNA targets of the global post-transcriptional regulator, Hfq. PLoS Genet. 4:e1000163.
    • Sittka, A., S. Lucchini, K. Papenfort, C. M. Sharma, K. Rolle, T. T. Binnewies, J. C. Hinton, and J. Vogel .2008. Deep sequencing analysis of small noncoding RNA and mRNA targets of the global post-transcriptional regulator, Hfq. PLoS Genet. 4:e1000163.
  • 59
    • 33845713571 scopus 로고    scopus 로고
    • The RNA chaperone Hfq is essential for the virulence of Salmonella typhimurium
    • Sittka, A., V. Pfeiffer, K. Tedin, and J. Vogel .2007. The RNA chaperone Hfq is essential for the virulence of Salmonella typhimurium. Mol. Microbiol. 63:193-217.
    • (2007) Mol. Microbiol , vol.63 , pp. 193-217
    • Sittka, A.1    Pfeiffer, V.2    Tedin, K.3    Vogel, J.4
  • 61
    • 1842453716 scopus 로고    scopus 로고
    • Controlling mRNA stability and translation with small, noncoding RNAs
    • Storz, G., J. A. Opdyke, and A. X. Zhang .2004. Controlling mRNA stability and translation with small, noncoding RNAs. Curr. Opin. Microbiol. 7:140-144.
    • (2004) Curr. Opin. Microbiol , vol.7 , pp. 140-144
    • Storz, G.1    Opdyke, J.A.2    Zhang, A.X.3
  • 62
    • 0037709369 scopus 로고    scopus 로고
    • Sukhodolets, M. V., and S. Garges .2003. Interaction of Escherichia coli RNA polymerase with the ribosomal protein S1 and the Sm-like ATPase Hfq. Biochemistry 42:8022-8034.
    • Sukhodolets, M. V., and S. Garges .2003. Interaction of Escherichia coli RNA polymerase with the ribosomal protein S1 and the Sm-like ATPase Hfq. Biochemistry 42:8022-8034.
  • 63
    • 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 R. M. Wartell .2006. Escherichia coli Hfq binds A18 and DsrA domain II with similar 2:1 Hfq6/RNA stoichiometry using different surface sites. Biochemistry 45:4875-4887.
    • (2006) Biochemistry , vol.45 , pp. 4875-4887
    • Sun, X.1    Wartell, R.M.2
  • 64
    • 0036714801 scopus 로고    scopus 로고
    • Predicted structure and phyletic distribution of the RNA-binding protein Hfq
    • Sun, X., I. Zhulin, and R. M. Wartell .2002. Predicted structure and phyletic distribution of the RNA-binding protein Hfq. Nucleic Acids Res. 30:3662-3671.
    • (2002) Nucleic Acids Res , vol.30 , pp. 3662-3671
    • Sun, X.1    Zhulin, I.2    Wartell, R.M.3
  • 65
    • 0028243445 scopus 로고
    • Characterization of broadly pleiotropic phenotypes caused by an hfq insertion mutation in Escherichia-coli-K-12
    • Tsui, H. C. T., H. C. E. Leung, and M. E. Winkler .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
  • 66
    • 39149122829 scopus 로고    scopus 로고
    • Identification of chromosomal alpha-proteobacterial small RNAs by comparative genome analysis and detection in Sinorhizobium meliloti strain 1021
    • Ulve, V. M., E. W. Sevin, A. Cheron, and F. Barloy-Hubler .2007. Identification of chromosomal alpha-proteobacterial small RNAs by comparative genome analysis and detection in Sinorhizobium meliloti strain 1021. BMC Genomics 8:467.
    • (2007) BMC Genomics , vol.8 , pp. 467
    • Ulve, V.M.1    Sevin, E.W.2    Cheron, A.3    Barloy-Hubler, F.4
  • 67
    • 1642565815 scopus 로고    scopus 로고
    • The bacterial Smlike protein Hfq: A key player in RNA transactions
    • Valentin-Hansen, P., M. Eriksen, and C. Udesen .2004. The bacterial Smlike protein Hfq: a key player in RNA transactions. Mol. Microbiol. 51:1525-1533.
    • (2004) Mol. Microbiol , vol.51 , pp. 1525-1533
    • Valentin-Hansen, P.1    Eriksen, M.2    Udesen, C.3
  • 69
  • 70
    • 60149089144 scopus 로고    scopus 로고
    • Regulatory RNAs in bacteria
    • Waters, L. S., and G. Storz .2009. Regulatory RNAs in bacteria. Cell 136: 615-628.
    • (2009) Cell , vol.136 , pp. 615-628
    • Waters, L.S.1    Storz, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.