메뉴 건너뛰기




Volumn 3, Issue 2, 2000, Pages 159-164

U-turns and regulatory RNAs

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY RNA; RNA;

EID: 0034025902     PISSN: 13695274     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1369-5274(00)00069-2     Document Type: Review
Times cited : (58)

References (47)
  • 1
    • 85041131924 scopus 로고
    • Antisense RNA control in bacteria, phages and plasmids
    • Wagner E.G.H., Simons R.W. Antisense RNA control in bacteria, phages and plasmids. Annu Rev Microbiol. 48:1994;713-742.
    • (1994) Annu Rev Microbiol , vol.48 , pp. 713-742
    • Wagner, E.G.H.1    Simons, R.W.2
  • 2
    • 0025274894 scopus 로고
    • Control of ColE1 plasmid replication. Intermediates in the binding of RNA I and RNA II
    • Tomizawa J.I. Control of ColE1 plasmid replication. Intermediates in the binding of RNA I and RNA II. J Mol Biol. 212:1990;683-694.
    • (1990) J Mol Biol , vol.212 , pp. 683-694
    • Tomizawa, J.I.1
  • 3
    • 0027932830 scopus 로고
    • Antisense RNA-mediated transcriptional attenuation occurs faster than stable antisense/target pairing: An in vitro study of plasmid IP501
    • Brantl S., Wagner E.G.H. Antisense RNA-mediated transcriptional attenuation occurs faster than stable antisense/target pairing: an in vitro study of plasmid IP501. EMBO J. 13:1994;3599-3607.
    • (1994) EMBO J , vol.13 , pp. 3599-3607
    • Brantl, S.1    Wagner, E.G.H.2
  • 4
    • 0028354130 scopus 로고
    • Mechanism of binding of the antisense and target RNAs involved in the regulation of the IncB plasmid replication
    • Siemering K.R., Praszkier J., Pittard A.J. Mechanism of binding of the antisense and target RNAs involved in the regulation of the IncB plasmid replication. J Bacteriol. 176:1994;2677-2688.
    • (1994) J Bacteriol , vol.176 , pp. 2677-2688
    • Siemering, K.R.1    Praszkier, J.2    Pittard, A.J.3
  • 6
    • 0033543654 scopus 로고    scopus 로고
    • Ribonuclease III processing of co-axially stacked RNA helices
    • Franch T., Thisted T., Gerdes K. Ribonuclease III processing of co-axially stacked RNA helices. J Biol Chem. 274:1999;26572-26578.
    • (1999) J Biol Chem , vol.274 , pp. 26572-26578
    • Franch, T.1    Thisted, T.2    Gerdes, K.3
  • 7
    • 0032424799 scopus 로고    scopus 로고
    • Kissing and RNA stability in antisense control of plasmid replication
    • Brantl S., Wagner E.G.H. Kissing and RNA stability in antisense control of plasmid replication. Trend Biochem. 23:1998;451-454.
    • (1998) Trend Biochem , vol.23 , pp. 451-454
    • Brantl, S.1    Wagner, E.G.H.2
  • 8
    • 0033579543 scopus 로고    scopus 로고
    • Antisense RNA regulation in prokaryotes: Rapid RNA-RNA interaction facilitated by a general U-turn loop structure
    • A comparative analysis of recognition loops of antisense RNA-regulated gene systems revealed the presence of a YUNR U-turn motif. Using hok/sok as a model system, mutational analysis and structure probing data support the presence of a U-turn structure that enhances the rate of Sok-antisense-binding to its target in the hok mRNA. A similar function as a rate enhancer was inferred for other antisense-RNA-regulated gene systems
    • Franch T., Petersen M., Wagner E.G.H., Jacobsen J.P., Gerdes K. Antisense RNA regulation in prokaryotes: rapid RNA-RNA interaction facilitated by a general U-turn loop structure. J Mol Biol. 294:1999;1115-1125. A comparative analysis of recognition loops of antisense RNA-regulated gene systems revealed the presence of a YUNR U-turn motif. Using hok/sok as a model system, mutational analysis and structure probing data support the presence of a U-turn structure that enhances the rate of Sok-antisense-binding to its target in the hok mRNA. A similar function as a rate enhancer was inferred for other antisense-RNA-regulated gene systems.
    • (1999) J Mol Biol , vol.294 , pp. 1115-1125
    • Franch, T.1    Petersen, M.2    Wagner, E.G.H.3    Jacobsen, J.P.4    Gerdes, K.5
  • 9
    • 0017359465 scopus 로고
    • Elementary steps of base recognition and helix-coil transitions in nucleic acids
    • Pörschke D. Elementary steps of base recognition and helix-coil transitions in nucleic acids. Mol Biol Biochem Biophys. 24:1977;191-218.
    • (1977) Mol Biol Biochem Biophys , vol.24 , pp. 191-218
    • Pörschke, D.1
  • 12
    • 0017182937 scopus 로고
    • Structural domains of transfer RNA molecules
    • Quigley G.J., Rich A. Structural domains of transfer RNA molecules. Science. 194:1976;796-804.
    • (1976) Science , vol.194 , pp. 796-804
    • Quigley, G.J.1    Rich, A.2
  • 13
    • 0029998660 scopus 로고    scopus 로고
    • Structure of a hexanucleotide RNA hairpin loop conserved in ribosomal RNAs
    • Huang S., Wang Y.X., Draper D.E. Structure of a hexanucleotide RNA hairpin loop conserved in ribosomal RNAs. J Mol Biol. 258:1996;308-321.
    • (1996) J Mol Biol , vol.258 , pp. 308-321
    • Huang, S.1    Wang, Y.X.2    Draper, D.E.3
  • 14
    • 0028063567 scopus 로고
    • Three-dimensional structure of a hammerhead ribozyme
    • Pley H.W., Flaherty K.M., McKay D.B. Three-dimensional structure of a hammerhead ribozyme. Nature. 372:1994;68-74.
    • (1994) Nature , vol.372 , pp. 68-74
    • Pley, H.W.1    Flaherty, K.M.2    McKay, D.B.3
  • 15
    • 0031572279 scopus 로고    scopus 로고
    • The structure of an essential splicing element: Stem loop IIa from yeast U2 snRNA
    • Stallings S.C., Moore P.B. The structure of an essential splicing element: stem loop IIa from yeast U2 snRNA. Structure. 5:1997;1173-1185.
    • (1997) Structure , vol.5 , pp. 1173-1185
    • Stallings, S.C.1    Moore, P.B.2
  • 16
    • 0031761536 scopus 로고    scopus 로고
    • HIV-1 A-rich RNA loop mimics the tRNA anticodon structure
    • Puglisi E.V., Puglisi J.D. HIV-1 A-rich RNA loop mimics the tRNA anticodon structure. Nat Struct Biol. 5:1998;1033-1036.
    • (1998) Nat Struct Biol , vol.5 , pp. 1033-1036
    • Puglisi, E.V.1    Puglisi, J.D.2
  • 17
    • 0030692131 scopus 로고    scopus 로고
    • Identification of specific Rp-phosphate oxygens in the tRNA anticodon loop required for ribosomal P-site binding
    • Schnitzer W., von Ahsen U. Identification of specific Rp-phosphate oxygens in the tRNA anticodon loop required for ribosomal P-site binding. Proc Natl Acad Sci USA. 94:1997;12823-12828.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12823-12828
    • Schnitzer, W.1    Von Ahsen, U.2
  • 18
    • 0032922676 scopus 로고    scopus 로고
    • The uridine in "u-turn": Contributions to tRNA-ribosomal binding
    • The function of the invariant uracil ribonucleoside of the tRNA anticodon loop is investigated. The uracil contributes to U-turn stability of the anticodon loop by two non-Watson-Crick interactions and strong base-stacking effects. These properties promote the anticodon loop interaction with a ribosome/mRNA complex
    • Ashraf S.S., Ansari G., Guenther R., Sochacka E., Malkiewicz A., Agris P.F. The uridine in "U-turn": contributions to tRNA-ribosomal binding. RNA. 5:1999;503-511. The function of the invariant uracil ribonucleoside of the tRNA anticodon loop is investigated. The uracil contributes to U-turn stability of the anticodon loop by two non-Watson-Crick interactions and strong base-stacking effects. These properties promote the anticodon loop interaction with a ribosome/mRNA complex.
    • (1999) RNA , vol.5 , pp. 503-511
    • Ashraf, S.S.1    Ansari, G.2    Guenther, R.3    Sochacka, E.4    Malkiewicz, A.5    Agris, P.F.6
  • 19
    • 0025122169 scopus 로고
    • Electrical potential of transfer RNAs: Codon-anticodon recognition
    • Sharp K.A., Honig B., Harvey S.C. Electrical potential of transfer RNAs: codon-anticodon recognition. Biochemistry. 29:1990;340-346.
    • (1990) Biochemistry , vol.29 , pp. 340-346
    • Sharp, K.A.1    Honig, B.2    Harvey, S.C.3
  • 20
    • 0032707625 scopus 로고    scopus 로고
    • Calculating the electrostatic properties of RNA provides new insights into molecular interactions and function
    • Chin K., Sharp K.A., Honig B., Pyle A.M. Calculating the electrostatic properties of RNA provides new insights into molecular interactions and function. Nat Struct Biol. 6:1999;1055-1061.
    • (1999) Nat Struct Biol , vol.6 , pp. 1055-1061
    • Chin, K.1    Sharp, K.A.2    Honig, B.3    Pyle, A.M.4
  • 22
    • 0032496274 scopus 로고    scopus 로고
    • Structural basis for binding of the plasmid ColIb-P9 antisense Inc RNA to its target RNA with the 5′-rUUGGCG-3′ motif in the loop sequene
    • A comprehensive mutational analyses of the binding of antisense IncI to its target in the repZ mRNA suggest that the rUU dinucleotide of the recognition loop in repZ is important for fast pairing to IncI. The authors propose that the six-nucleotide target loop forms a U-turn configuration. In the accompanying paper [47] they show that the U-turn loop structure is also important for intramolecular pseudoknot formation in the repZ mRNA
    • Asano K., Niimi T., Yokoyama S., Mizobuchi K. Structural basis for binding of the plasmid ColIb-P9 antisense Inc RNA to its target RNA with the 5′-rUUGGCG-3′ motif in the loop sequene. J Biol Chem. 273:1998;11826-11838. A comprehensive mutational analyses of the binding of antisense IncI to its target in the repZ mRNA suggest that the rUU dinucleotide of the recognition loop in repZ is important for fast pairing to IncI. The authors propose that the six-nucleotide target loop forms a U-turn configuration. In the accompanying paper [47] they show that the U-turn loop structure is also important for intramolecular pseudoknot formation in the repZ mRNA.
    • (1998) J Biol Chem , vol.273 , pp. 11826-11838
    • Asano, K.1    Niimi, T.2    Yokoyama, S.3    Mizobuchi, K.4
  • 23
    • 0025861307 scopus 로고
    • Complexes formed by complementary RNA stem-loop. their formation structures and interaction with ColE1 Rom protein
    • Eguchi Y., Tomizawa J.I. Complexes formed by complementary RNA stem-loop. their formation structures and interaction with ColE1 Rom protein. J Mol Biol. 220:1991;831-842.
    • (1991) J Mol Biol , vol.220 , pp. 831-842
    • Eguchi, Y.1    Tomizawa, J.I.2
  • 24
    • 0024844260 scopus 로고
    • Insertion sequence IS10 anti-sense pairing initiates by an interaction between the 5′ end of the target RNA and a loop in the anti-sense RNA
    • Kittle J.D., Simons R.W., Lee J., Kleckner N. Insertion sequence IS10 anti-sense pairing initiates by an interaction between the 5′ end of the target RNA and a loop in the anti-sense RNA. J Mol Biol. 210:1989;561-572.
    • (1989) J Mol Biol , vol.210 , pp. 561-572
    • Kittle, J.D.1    Simons, R.W.2    Lee, J.3    Kleckner, N.4
  • 26
    • 0031459386 scopus 로고    scopus 로고
    • A small, stable RNA induced by oxidative stress: Role as a pleiotropic regulator and antimutator
    • Altuvia S., Weinstein-Fischer D., Zhang A., Postow L., Storz G. A small, stable RNA induced by oxidative stress: role as a pleiotropic regulator and antimutator. Cell. 90:1997;43-53.
    • (1997) Cell , vol.90 , pp. 43-53
    • Altuvia, S.1    Weinstein-Fischer, D.2    Zhang, A.3    Postow, L.4    Storz, G.5
  • 27
    • 0029897937 scopus 로고    scopus 로고
    • The RNA-binding protein HF-1, known as a host factor for phage QB RNA replication, is essential for rpoS translation in Escherichia coli
    • Muffler A., Fischer D., Hengge-Aronis R. The RNA-binding protein HF-1, known as a host factor for phage QB RNA replication, is essential for rpoS translation in Escherichia coli. Genes Dev. 10:1996;1143-1151.
    • (1996) Genes Dev , vol.10 , pp. 1143-1151
    • Muffler, A.1    Fischer, D.2    Hengge-Aronis, R.3
  • 29
    • 0025031657 scopus 로고
    • Identification and sequence analysis of the gene encoding the transcriptional activator of the formate hydrogenlyase system of Escherichia coli
    • Schlensog V., Böck A. Identification and sequence analysis of the gene encoding the transcriptional activator of the formate hydrogenlyase system of Escherichia coli. Mol Microbiol. 8:1990;1319-1327.
    • (1990) Mol Microbiol , vol.8 , pp. 1319-1327
    • Schlensog, V.1    Böck, A.2
  • 30
    • 0032531720 scopus 로고    scopus 로고
    • The Escherichia coli OxyS regulatory RNA represses fhlA translation by blocking ribosome binding
    • OxyS represses fhlA encoding a transcriptional activator of genes required for formation of the formate-hydrogenlyase complex. Seven nucleotides centred around the loop of the terminator hairpin of OxyS is complementary to the Shine & Dalgarno (SD) region of fhlA. Toeprinting and mutational analyses showed that OxyS precludes ribosome binding at the SD of fhlA
    • Altuvia S., Zhang A., Argaman L., Tiwari A., Storz G. The Escherichia coli OxyS regulatory RNA represses fhlA translation by blocking ribosome binding. EMBO J. 17:1998;6069-6075. OxyS represses fhlA encoding a transcriptional activator of genes required for formation of the formate-hydrogenlyase complex. Seven nucleotides centred around the loop of the terminator hairpin of OxyS is complementary to the Shine & Dalgarno (SD) region of fhlA. Toeprinting and mutational analyses showed that OxyS precludes ribosome binding at the SD of fhlA.
    • (1998) EMBO J , vol.17 , pp. 6069-6075
    • Altuvia, S.1    Zhang, A.2    Argaman, L.3    Tiwari, A.4    Storz, G.5
  • 31
    • 0003208241 scopus 로고    scopus 로고
    • Uptake and metabolism of iron and molybdenum
    • F.C. et al. Neidhardt. Washington, DC: ASM Press
    • Earhart C.F. Uptake and metabolism of iron and molybdenum. Neidhardt F.C.et al. Escherichia coli and Salmonella. 1996;1075-1090 ASM Press, Washington, DC.
    • (1996) Escherichia Coli and Salmonella , pp. 1075-1090
    • Earhart, C.F.1
  • 32
    • 0027411681 scopus 로고
    • Posttranscriptional repression of Escherichia coli OmpF protein in response to redox stress: Positive control of the micF antisense RNA by the soxRS locus
    • Chou J.H., Greenberg J.T., Demple B. Posttranscriptional repression of Escherichia coli OmpF protein in response to redox stress: positive control of the micF antisense RNA by the soxRS locus. J Bacteriol. 175:1993;1026-1031.
    • (1993) J Bacteriol , vol.175 , pp. 1026-1031
    • Chou, J.H.1    Greenberg, J.T.2    Demple, B.3
  • 33
    • 0000871346 scopus 로고
    • Regulation of capsule synthesis: Modification of the two component paradigm by an accessory unstable regulator
    • J.A. Hoch, & T.J. Silhavy. Washington, DC: ASM Press
    • Gottesman S. Regulation of capsule synthesis: modification of the two component paradigm by an accessory unstable regulator. Hoch J.A., Silhavy T.J. Two-Component Signal Transduction. 1995;253-262 ASM Press, Washington, DC.
    • (1995) Two-Component Signal Transduction , pp. 253-262
    • Gottesman, S.1
  • 34
    • 0028957883 scopus 로고
    • A small RNA acts as an antisilencer of the H-NS-silenced rcsA gene of Escherichia coli
    • Sledjeski D., Gottesman S. A small RNA acts as an antisilencer of the H-NS-silenced rcsA gene of Escherichia coli. Proc Natl Acad Sci USA. 92:1995;2003-2007.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2003-2007
    • Sledjeski, D.1    Gottesman, S.2
  • 35
    • 0032514643 scopus 로고    scopus 로고
    • Riboregulation in Escherichia coli: DsrA RNA acts by RNA:RNA interactions at multiple loci
    • The small RNA, DsrA, exhibits partial sequence is complementary to the leader of rpoS mRNA and to a segment of the hns gene immediately downstream of the AUG start-codon. DsrA appears to interfere with translation initiation of hns, whereas the translation of rpoS is stimulated by DsrA. DsrA is complementary to an element in the rpoS mRNA that occludes the TIR and thus enhances rpoS translation by binding to this element
    • Lease R.A., Cusick M.E., Belfort M. Riboregulation in Escherichia coli: DsrA RNA acts by RNA:RNA interactions at multiple loci. Proc Natl Acad Sci USA. 95:1998;12456-12461. The small RNA, DsrA, exhibits partial sequence is complementary to the leader of rpoS mRNA and to a segment of the hns gene immediately downstream of the AUG start-codon. DsrA appears to interfere with translation initiation of hns, whereas the translation of rpoS is stimulated by DsrA. DsrA is complementary to an element in the rpoS mRNA that occludes the TIR and thus enhances rpoS translation by binding to this element.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12456-12461
    • Lease, R.A.1    Cusick, M.E.2    Belfort, M.3
  • 36
    • 0029113833 scopus 로고
    • Activation of alpha-toxin translation in Staphylococcus aureus by the trans-encoded antisense RNA, RNAIII
    • Morfeldt E., Taylor D., von Gabain A., Arvidson S. Activation of alpha-toxin translation in Staphylococcus aureus by the trans-encoded antisense RNA, RNAIII. EMBO J. 14:1995;4569-4577.
    • (1995) EMBO J , vol.14 , pp. 4569-4577
    • Morfeldt, E.1    Taylor, D.2    Von Gabain, A.3    Arvidson, S.4
  • 37
    • 0029739317 scopus 로고    scopus 로고
    • The small RNA, DsrA, is essential for the low temperature expression of RpoS during exponential growth in Escherichia coli
    • Sledjeski D., Gupta A., Gottesman S. The small RNA, DsrA, is essential for the low temperature expression of RpoS during exponential growth in Escherichia coli. EMBO J. 15:1996;3993-4000.
    • (1996) EMBO J , vol.15 , pp. 3993-4000
    • Sledjeski, D.1    Gupta, A.2    Gottesman, S.3
  • 38
    • 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
    • Previously, Gottesman and co-workers described that the effect of DsrA on rpoS was most pronounced at low temperatures where the secondary structure stability in rpoS mRNA is augmented. In this paper, mutational analysis of a base-pair in the rpoS secondary structure and the corresponding nucleotide in DsrA provide compelling evidence for the mechanism of DsrA stimulation of rpoS synthesis
    • Majdalani N., Cunning C., Sledjeski D., Elliot T., Gottesman S. 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. Previously, Gottesman and co-workers described that the effect of DsrA on rpoS was most pronounced at low temperatures where the secondary structure stability in rpoS mRNA is augmented. In this paper, mutational analysis of a base-pair in the rpoS secondary structure and the corresponding nucleotide in DsrA provide compelling evidence for the mechanism of DsrA stimulation of rpoS synthesis.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12462-12467
    • Majdalani, N.1    Cunning, C.2    Sledjeski, D.3    Elliot, T.4    Gottesman, S.5
  • 39
    • 0027171032 scopus 로고
    • Identification and molecular characterizationof csrA, a pleiotropic gene from Escherichia coli that affects glycogen biosynthesis, gluconeogenesis, cell size, and surface properties
    • Romeo T., Gong M., Liu M.Y., Brun-Zinkernagel A.M. Identification and molecular characterizationof csrA, a pleiotropic gene from Escherichia coli that affects glycogen biosynthesis, gluconeogenesis, cell size, and surface properties. J Bacteriol. 175:1993;4744-4755.
    • (1993) J Bacteriol , vol.175 , pp. 4744-4755
    • Romeo, T.1    Gong, M.2    Liu, M.Y.3    Brun-Zinkernagel, A.M.4
  • 40
    • 0030841920 scopus 로고    scopus 로고
    • The RNA molecule CsrB binds to the global regulatory protein CsrA and antagonizes its activity in Escherichia coli
    • Liu M.Y., Gui G., Wei B., Preston J.F., Oakford L., Geidroc D.P., Romeo T. The RNA molecule CsrB binds to the global regulatory protein CsrA and antagonizes its activity in Escherichia coli. J Biol Chem. 272:1997;17502-17510.
    • (1997) J Biol Chem , vol.272 , pp. 17502-17510
    • Liu, M.Y.1    Gui, G.2    Wei, B.3    Preston, J.F.4    Oakford, L.5    Geidroc, D.P.6    Romeo, T.7
  • 41
    • 0028891945 scopus 로고
    • Pleiotropic regulation of central carbohydrate metabolism in Escherichia coli via the gene csrA
    • Sabnis N.A., Yang H., Romeo T. Pleiotropic regulation of central carbohydrate metabolism in Escherichia coli via the gene csrA. J Biol Chem. 270:1995;29096-29104.
    • (1995) J Biol Chem , vol.270 , pp. 29096-29104
    • Sabnis, N.A.1    Yang, H.2    Romeo, T.3
  • 42
    • 0031697252 scopus 로고    scopus 로고
    • Global regulation by the small RNA-binding protein CsrA and the non-coding RNA molecule CsrB
    • This review describes the effects of CsrA/CsrB on the carbohydrate metabolism, cell surface, motility and adherence properties of E. coli. Furthermore, the importance of the homologous system RsmA/RsmB in plant pathogenesis in E. corotovora is described
    • Romeo T. Global regulation by the small RNA-binding protein CsrA and the non-coding RNA molecule CsrB. Mol Microbiol. 29:1998;1321-1330. This review describes the effects of CsrA/CsrB on the carbohydrate metabolism, cell surface, motility and adherence properties of E. coli. Furthermore, the importance of the homologous system RsmA/RsmB in plant pathogenesis in E. corotovora is described.
    • (1998) Mol Microbiol , vol.29 , pp. 1321-1330
    • Romeo, T.1
  • 43
    • 0029072697 scopus 로고
    • The product of the pleiotrophic Escherichia coli gene csrA regulates glycogen biosynthesis via its effect on mRNA stability
    • Liu M.Y., Yang H., Romeo T. The product of the pleiotrophic Escherichia coli gene csrA regulates glycogen biosynthesis via its effect on mRNA stability. J Bacteriol. 177:1995;2663-2672.
    • (1995) J Bacteriol , vol.177 , pp. 2663-2672
    • Liu, M.Y.1    Yang, H.2    Romeo, T.3
  • 44
    • 0030856586 scopus 로고    scopus 로고
    • The global regulator CsrA of Escherichia coli is a specific mRNA-binding protein
    • Liu M.Y., Romeo T. The global regulator CsrA of Escherichia coli is a specific mRNA-binding protein. J Bacteriol. 179:1997;4639-4642.
    • (1997) J Bacteriol , vol.179 , pp. 4639-4642
    • Liu, M.Y.1    Romeo, T.2
  • 45
    • 0029083083 scopus 로고
    • Identification of a global repressor gene, rsmA, of Erwinia carotovora subsp. carotovora that controls extracellular enzymes, N-(3-oxohexanoyl)-L-homoserine lactone, and pathogenicity in soft rotting Erwinia spp
    • Cui Y., Chatterjee A., Liu Y., Dumenyo C.K., Chatterjee A.K. Identification of a global repressor gene, rsmA, of Erwinia carotovora subsp. carotovora that controls extracellular enzymes, N-(3-oxohexanoyl)-L-homoserine lactone, and pathogenicity in soft rotting Erwinia spp. J Bacteriol. 177:1995;5108-5115.
    • (1995) J Bacteriol , vol.177 , pp. 5108-5115
    • Cui, Y.1    Chatterjee, A.2    Liu, Y.3    Dumenyo, C.K.4    Chatterjee, A.K.5
  • 46
    • 7344251897 scopus 로고    scopus 로고
    • Characterization of a novel RNA regulator of Erwinia carotovora ssp carotovora that controls production of extracellular enzymes and secondary metabolites
    • Liu Y., Cui C., Mukherjee A., Ma W.L., Chatterjee A.K. Characterization of a novel RNA regulator of Erwinia carotovora ssp carotovora that controls production of extracellular enzymes and secondary metabolites. Mol Microbiol. 29:1998;219-234.
    • (1998) Mol Microbiol , vol.29 , pp. 219-234
    • Liu, Y.1    Cui, C.2    Mukherjee, A.3    Ma, W.L.4    Chatterjee, A.K.5
  • 47
    • 0032496155 scopus 로고    scopus 로고
    • An RNA pseudoknot as the molecular switch for translation of the repZ gene encoding the replication initiator of Inclalpha plasmid ColIb-P9
    • Asano K., Mizobuchi K. An RNA pseudoknot as the molecular switch for translation of the repZ gene encoding the replication initiator of Inclalpha plasmid ColIb-P9. J Biol Chem. 273:1998;11815-11825.
    • (1998) J Biol Chem , vol.273 , pp. 11815-11825
    • Asano, K.1    Mizobuchi, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.