메뉴 건너뛰기




Volumn 13, Issue 12, 2007, Pages 2213-2223

An Hfq-like protein in archaea: Crystal structure and functional characterization of the Sm protein from Methanococcus jannaschii

Author keywords

Hfq; Methanococcus jannaschii; RNA binding protein; Sm; sRNA; Translational regulation

Indexed keywords

BACTERIAL PROTEIN; HFQ PROTEIN; PROTEIN SM; UNCLASSIFIED DRUG;

EID: 36248940726     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.689007     Document Type: Article
Times cited : (65)

References (61)
  • 2
    • 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
  • 3
    • 0035964342 scopus 로고    scopus 로고
    • Electrostatics of nanosystems: Application to microtubules and the ribosome
    • Baker, N.A., Sept, D., Joseph, S., Holst, M.J., and McCammon, J.A. 2001. Electrostatics of nanosystems: Application to microtubules and the ribosome. Proc. Natl. Acad. Sci. 98: 10037-10041.
    • (2001) Proc. Natl. Acad. Sci , vol.98 , pp. 10037-10041
    • Baker, N.A.1    Sept, D.2    Joseph, S.3    Holst, M.J.4    McCammon, J.A.5
  • 4
    • 18344396487 scopus 로고    scopus 로고
    • Lsm proteins and RNA processing
    • Beggs, J. 2005. Lsm proteins and RNA processing. Biochem. Soc. Trans. 33: 433-438.
    • (2005) Biochem. Soc. Trans , vol.33 , pp. 433-438
    • Beggs, J.1
  • 5
    • 34247109118 scopus 로고    scopus 로고
    • Hfq structure, function and ligand binding
    • Brennan, R.G. and Link, T.M. 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
  • 6
    • 0037276123 scopus 로고    scopus 로고
    • Identification of the Hfq-binding site on DsrA RNA: Hfq binds without altering DsrA secondary structure
    • Brescia, C.C., Mikulecky, P.J., Feig, A.L., and Sledjeski, D.D. 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
  • 7
    • 0029889596 scopus 로고    scopus 로고
    • Efficient translation of the RpoS σ factor in Salmonella typhimurium requires host factor I, an RNA-binding protein encoded by the hfq gene
    • Brown, L. and Elliott, T. 1996. Efficient translation of the RpoS σ 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
  • 8
    • 0141445965 scopus 로고    scopus 로고
    • Degradation of targeted mRNAs in Escherichia coli: Regulation by a small antisense RNA
    • Carpousis, A.J. 2003. Degradation of targeted mRNAs in Escherichia coli: Regulation by a small antisense RNA. Genes & Dev. 17: 2351-2355.
    • (2003) Genes & Dev , vol.17 , pp. 2351-2355
    • Carpousis, A.J.1
  • 9
    • 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.G., and Mabbutt, B.C. 2001. Crystal structure of a heptameric Sm-like protein complex from archaea: Implications for the structure and evolution of snRNPs. J. Mol. Biol. 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.G.5    Mabbutt, B.C.6
  • 10
    • 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., and Beggs, J.D. 1995. Identification and characterization of Uss1p (Sdb23p): A novel U6 snRNA-associated protein with significant similarity to core proteins of small nuclear ribonucleoproteins. EMBO J. 14: 2066-2075.
    • (1995) EMBO J , vol.14 , pp. 2066-2075
    • Cooper, M.1    Johnston, L.H.2    Beggs, J.D.3
  • 11
    • 0019254853 scopus 로고
    • Interaction of Escherichia coli host factor protein with oligoriboadenylates
    • de Haseth, P.L. and Uhlenbeck, O.C. 1980. Interaction of Escherichia coli host factor protein with oligoriboadenylates. Biochemistry 19: 6138-6146.
    • (1980) Biochemistry , vol.19 , pp. 6138-6146
    • de Haseth, P.L.1    Uhlenbeck, O.C.2
  • 12
    • 36248957306 scopus 로고    scopus 로고
    • DeLano, W.L. 2002. The PyMOL molecular graphics system. http://www.pymol.org.
    • (2002)
    • DeLano, W.L.1
  • 13
    • 1542320707 scopus 로고    scopus 로고
    • Hfq, a new chaperoning role: Binding to messenger RNA determines access for small RNA regulator
    • Geissmann, T.A. and Touati, D. 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
  • 14
    • 0031816179 scopus 로고    scopus 로고
    • The Escherichia coli relBE genes belong to a new toxin-antitoxin gene family
    • Gotfredsen, M. and Gerdes, K. 1998. The Escherichia coli relBE genes belong to a new toxin-antitoxin gene family. Mol. Microbiol. 29: 1065-1076.
    • (1998) Mol. Microbiol , vol.29 , pp. 1065-1076
    • Gotfredsen, M.1    Gerdes, K.2
  • 15
    • 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
  • 16
    • 0029054377 scopus 로고
    • snRNP Sm proteins share two evolutionarily conserved sequence motifs which are involved in Sm protein-protein interactions
    • Hermann, H., Fabrizio, P., Raker, V.A., Foulaki, K., Hornig, H., Brahms, K., and Lührmann, H. 1995. snRNP Sm proteins share two evolutionarily conserved sequence motifs which are involved in Sm protein-protein interactions. EMBO J. 14: 2076-2088.
    • (1995) EMBO J , vol.14 , pp. 2076-2088
    • Hermann, H.1    Fabrizio, P.2    Raker, V.A.3    Foulaki, K.4    Hornig, H.5    Brahms, K.6    Lührmann, H.7
  • 17
    • 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., Lührmann, R., Li, J., and Nagai, K. 1999. Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs. Cell 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    Lührmann, R.7    Li, J.8    Nagai, K.9
  • 18
    • 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., and Aiba, H. 2006. Base-pairing requirement for RNA silencing by a bacterial small RNA and acceleration of duplex formation by Hfq. Mol. Microbiol. 61: 1013-1022.
    • (2006) Mol. Microbiol , vol.61 , pp. 1013-1022
    • Kawamoto, H.1    Koide, Y.2    Morita, T.3    Aiba, H.4
  • 19
    • 23944455046 scopus 로고    scopus 로고
    • LSm proteins form heptameric rings that bind to RNA via repeating motifs
    • Khusial, P., Plaag, R., and Zieve, G.W. 2005. LSm proteins form heptameric rings that bind to RNA via repeating motifs. Trends Biochem. Sci. 30: 522-528.
    • (2005) Trends Biochem. Sci , vol.30 , pp. 522-528
    • Khusial, P.1    Plaag, R.2    Zieve, G.W.3
  • 20
    • 27544435570 scopus 로고    scopus 로고
    • Crystal structure of an archaeal Sm protein from Sulfolobus solfataricus
    • Kilic, T., Thore, S., and Suck, D. 2005. Crystal structure of an archaeal Sm protein from Sulfolobus solfataricus. Proteins 61: 689-693.
    • (2005) Proteins , vol.61 , pp. 689-693
    • Kilic, T.1    Thore, S.2    Suck, D.3
  • 21
    • 0345077411 scopus 로고
    • Promoters largely determine the efficiency of repressor action
    • Lanzer, M. and Bujard, H. 1988. Promoters largely determine the efficiency of repressor action. Proc. Natl. Acad. Sci. 85: 8973-8977.
    • (1988) Proc. Natl. Acad. Sci , vol.85 , pp. 8973-8977
    • Lanzer, M.1    Bujard, H.2
  • 22
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S., and Thornton, J.M. 1993. PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26: 283-291.
    • (1993) J. Appl. Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 23
    • 9244253711 scopus 로고    scopus 로고
    • Cycling of the Sm-like protein Hfq on the DsrA small regulatory RNA
    • 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.
    • (2004) J. Mol. Biol , vol.344 , pp. 1211-1223
    • Lease, R.A.1    Woodson, S.A.2
  • 24
    • 0037007078 scopus 로고    scopus 로고
    • A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli
    • Massé, E. and Gottesman, S. 2002. A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli. Proc. Natl. Acad. Sci. 99: 4620-4625.
    • (2002) Proc. Natl. Acad. Sci , vol.99 , pp. 4620-4625
    • Massé, E.1    Gottesman, S.2
  • 25
    • 0141860088 scopus 로고    scopus 로고
    • Coupled degradation of a small regulatory RNA and its mRNA targets in Escherichia coli
    • Massé, E., Escorcia, F.E., and Gottesman, S. 2003. Coupled degradation of a small regulatory RNA and its mRNA targets in Escherichia coli. Genes & Dev. 17: 2374-2383.
    • (2003) Genes & Dev , vol.17 , pp. 2374-2383
    • Massé, E.1    Escorcia, F.E.2    Gottesman, S.3
  • 29
    • 0036645490 scopus 로고    scopus 로고
    • Spot 42 RNA mediates discoordinate expression of the E. coli galactose operon
    • Møller, T., Franch, T., Udesen, C., Gerdes, K., and Valentin-Hansen, P. 2002b. Spot 42 RNA mediates discoordinate expression of the E. coli galactose operon. Genes & Dev. 16: 1696-1706.
    • (2002) Genes & Dev , vol.16 , pp. 1696-1706
    • Møller, T.1    Franch, T.2    Udesen, C.3    Gerdes, K.4    Valentin-Hansen, P.5
  • 30
    • 24944507588 scopus 로고    scopus 로고
    • RNase E-based ribonucleoprotein complexes: Mechanical basis of mRNA destabilization mediated by bacterial noncoding RNAs
    • Morita, T., Maki, K., and Aiba, H. 2005. RNase E-based ribonucleoprotein complexes: Mechanical basis of mRNA destabilization mediated by bacterial noncoding RNAs. Genes & Dev. 19: 2176-2186.
    • (2005) Genes & Dev , vol.19 , pp. 2176-2186
    • Morita, T.1    Maki, K.2    Aiba, H.3
  • 31
    • 0029897937 scopus 로고    scopus 로고
    • The RNA-binding protein HF-I, known as a host factor for phage Q β RNA replication, is essential for rpoS translation in Escherichia coli
    • Muffler, A., Fischer, D., and Hengge Aronis, R. 1996. The RNA-binding protein HF-I, known as a host factor for phage Q β RNA replication, is essential for rpoS translation in Escherichia coli. Genes & Dev. 10: 1143-1151.
    • (1996) Genes & Dev , vol.10 , pp. 1143-1151
    • Muffler, A.1    Fischer, D.2    Hengge Aronis, R.3
  • 33
    • 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., and Eisenberg, D.S. 2001. The crystal structure of a heptameric archaeal Sm protein: Implications for the eukaryotic snRNP core. Proc. Natl. Acad. Sci. 98: 5532-5537.
    • (2001) Proc. Natl. Acad. Sci , vol.98 , pp. 5532-5537
    • Mura, C.1    Cascio, D.2    Sawaya, M.R.3    Eisenberg, D.S.4
  • 34
    • 0037378351 scopus 로고    scopus 로고
    • The oligomerization and ligand-binding properties of Sm-like archaeal proteins (SmAPs)
    • Mura, C., Kozhukhovsky, A., Gingery, M., Phillips, M., and Eisenberg, D. 2003. The oligomerization and ligand-binding properties of Sm-like archaeal proteins (SmAPs). Protein Sci. 12: 832-847.
    • (2003) Protein Sci , vol.12 , pp. 832-847
    • Mura, C.1    Kozhukhovsky, A.2    Gingery, M.3    Phillips, M.4    Eisenberg, D.5
  • 35
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G.N., Vagin, A.A., and Dodson, E.J. 1997. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D53: 240-255.
    • (1997) Acta Crystallogr , vol.D53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 37
    • 0034031110 scopus 로고    scopus 로고
    • Post-transcriptional control by global regulators of gene expression in bacteria
    • Nogueira, T. and Springer, M. 2000. Post-transcriptional control by global regulators of gene expression in bacteria. Curr. Opin. Microbiol. 3: 154-158.
    • (2000) Curr. Opin. Microbiol , vol.3 , pp. 154-158
    • Nogueira, T.1    Springer, M.2
  • 38
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276: 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 39
    • 0034729584 scopus 로고    scopus 로고
    • RNA degradation: Sm-like proteins wRING the neck of mRNA
    • doi: 10.1016/S0960-9822(00)00552-2
    • Pannone, B.K. and Wolin, S.L. 2000. RNA degradation: Sm-like proteins wRING the neck of mRNA. Curr. Biol. 10: R478-R481. doi: 10.1016/S0960-9822(00)00552-2.
    • (2000) Curr. Biol , vol.10
    • Pannone, B.K.1    Wolin, S.L.2
  • 40
  • 41
    • 0038187589 scopus 로고    scopus 로고
    • Small noncoding RNAs, coordinators of adaptation processes in Escherichia coli: The RpoS paradigm
    • Repoila, F., Majdalani, N., and Gottesman, S. 2003. Small noncoding RNAs, coordinators of adaptation processes in Escherichia coli: The RpoS paradigm. Mol. Microbiol. 48: 855-861.
    • (2003) Mol. Microbiol , vol.48 , pp. 855-861
    • Repoila, F.1    Majdalani, N.2    Gottesman, S.3
  • 42
    • 0242380623 scopus 로고    scopus 로고
    • Sm-like proteins in Eubacteria: The crystal structure of the Hfq protein from Escherichia coli
    • doi: 10.1093/nar/gkg480
    • Sauter, C., Basquin, J., and Suck, D. 2003. Sm-like proteins in Eubacteria: The crystal structure of the Hfq protein from Escherichia coli. Nucleic Acids Res. 31: 4091-4098. doi: 10.1093/nar/gkg480.
    • (2003) Nucleic Acids Res , vol.31 , pp. 4091-4098
    • Sauter, C.1    Basquin, J.2    Suck, D.3
  • 43
    • 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., 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.
    • (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
  • 44
    • 0017227834 scopus 로고
    • Site-specific interaction of Qβ host factor and ribosomal protein S1 with Qβ and R17 bacteriophage RNAs
    • Senear, A.W. and Steitz, J.A. 1976. Site-specific interaction of Qβ host factor and ribosomal protein S1 with Qβ and R17 bacteriophage RNAs. J. Biol. Chem. 251: 1902-1912.
    • (1976) J. Biol. Chem , vol.251 , pp. 1902-1912
    • Senear, A.W.1    Steitz, J.A.2
  • 45
    • 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. 1995. 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. 14: 2089-2098.
    • (1995) EMBO J , vol.14 , pp. 2089-2098
    • Séraphin, B.1
  • 46
    • 0036129690 scopus 로고    scopus 로고
    • Functional replacement of the Escherichia coli hfq gene by the homologue of Pseudomonas aeruginosa
    • Sonnleitner, E., Moll, I., and Bläsi, U. 2002. Functional replacement of the Escherichia coli hfq gene by the homologue of Pseudomonas aeruginosa. Microbiol. 148: 883-891.
    • (2002) Microbiol , vol.148 , pp. 883-891
    • Sonnleitner, E.1    Moll, I.2    Bläsi, U.3
  • 48
    • 1842453716 scopus 로고    scopus 로고
    • Controlling mRNA stability and translation with small, noncoding RNAs
    • Storz, G., Opdyke, J.A., and Zhang, A.X. 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
  • 49
    • 33645939935 scopus 로고    scopus 로고
    • 6/RNA stoichiometry using different surface sites
    • 6/RNA stoichiometry using different surface sites. Biochemistry 45: 4875-4887.
    • (2006) Biochemistry , vol.45 , pp. 4875-4887
    • Sun, X.1    Wartell, R.M.2
  • 50
    • 0036714801 scopus 로고    scopus 로고
    • Predicted structure and phyletic distribution of the RNA-binding protein Hfq
    • doi: 10.1093/nar/gkf508
    • Sun, X.G., Zhulin, I., and Wartell, R.M. 2002. Predicted structure and phyletic distribution of the RNA-binding protein Hfq. Nucleic Acids Res. 30: 3662-3671. doi: 10.1093/nar/gkf508.
    • (2002) Nucleic Acids Res , vol.30 , pp. 3662-3671
    • Sun, X.G.1    Zhulin, I.2    Wartell, R.M.3
  • 51
    • 0347383761 scopus 로고    scopus 로고
    • SOLVE and RESOLVE: Automated structure solution and density modification
    • Terwilliger, T.C. 2003. SOLVE and RESOLVE: Automated structure solution and density modification. Methods Enzymol. 374: 22-36.
    • (2003) Methods Enzymol , vol.374 , pp. 22-36
    • Terwilliger, T.C.1
  • 52
    • 0037428440 scopus 로고    scopus 로고
    • Crystal structures of the Pyrococcus abyssi Sm core and its complex with RNA
    • Thore, S., Mayer, C., Sauter, C., Weeks, S., and Suck, D. 2003. Crystal structures of the Pyrococcus abyssi Sm core and its complex with RNA. J. Biol. Chem. 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
  • 53
    • 0035341325 scopus 로고    scopus 로고
    • RNA binding in an Sm core domain: X-ray structure and functional analysis of an archaeal Sm protein complex
    • Törö, I., Thore, S., Mayer, C., Basquin, J., Séraphin, B., and Suck, D. 2001. RNA binding in an Sm core domain: X-ray structure and functional analysis of an archaeal Sm protein complex. EMBO J. 20: 2293-2303.
    • (2001) EMBO J , vol.20 , pp. 2293-2303
    • Törö, I.1    Thore, S.2    Mayer, C.3    Basquin, J.4    Séraphin, B.5    Suck, D.6
  • 54
    • 0036290884 scopus 로고    scopus 로고
    • Archaeal Sm proteins form heptameric and hexameric complexes: Crystal structures of the Sm1 and Sm2 proteins from the hyperthermophile Archaeoglobus fulgidus
    • Törö, I., Basquin, J., Teo-Dreher, H., and Suck, D. 2002. Archaeal Sm proteins form heptameric and hexameric complexes: Crystal structures of the Sm1 and Sm2 proteins from the hyperthermophile Archaeoglobus fulgidus. J. Mol. Biol. 320: 129-142.
    • (2002) J. Mol. Biol , vol.320 , pp. 129-142
    • Törö, I.1    Basquin, J.2    Teo-Dreher, H.3    Suck, D.4
  • 55
    • 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
  • 57
    • 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-Pedersen, A., and Hammer-Jespersen, K. 1978. 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. 159: 191-202.
    • (1978) Mol. Gen. Genet , vol.159 , pp. 191-202
    • Valentin-Hansen, P.1    Svenningsen, B.A.2    Munch-Pedersen, A.3    Hammer-Jespersen, K.4
  • 58
    • 1642565815 scopus 로고    scopus 로고
    • The bacterial Sm-like protein Hfq: A key player in RNA transactions
    • Valentin-Hansen, P., Eriksen, M., and Udesen, C. 2004. The bacterial Sm-like 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
  • 59
    • 28544442127 scopus 로고    scopus 로고
    • Eukaryotic Lsm proteins: Lessons from bacteria
    • Wilusz, C.J. and Wilusz, J. 2005. Eukaryotic Lsm proteins: Lessons from bacteria. Nat. Struct. Mol. Biol. 12: 1031-1036.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 1031-1036
    • Wilusz, C.J.1    Wilusz, J.2
  • 60
    • 0025300402 scopus 로고
    • Towards a natural system of organisms: Proposal for the domains Archaea, Bacteria, and Eucarya
    • Woese, C.R., Kandler, O., and Wheelis, M.L. 1990. Towards a natural system of organisms: Proposal for the domains Archaea, Bacteria, and Eucarya. Proc. Natl. Acad. Sci. 87: 4576-4579.
    • (1990) Proc. Natl. Acad. Sci , vol.87 , pp. 4576-4579
    • Woese, C.R.1    Kandler, O.2    Wheelis, M.L.3
  • 61
    • 0036163624 scopus 로고    scopus 로고
    • The Sm-like Hfq protein increases OxyS RNA interaction with target mRNAs
    • Zhang, A.X., 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: 1-22.
    • (2002) Mol. Cell , vol.9 , pp. 1-22
    • Zhang, A.X.1    Wassarman, K.M.2    Ortega, J.3    Steven, A.C.4    Storz, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.