메뉴 건너뛰기




Volumn 39, Issue 10, 2011, Pages 4450-4463

Mapping interactions between the RNA chaperone FinO and its RNA targets

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL RNA; CHAPERONE; COMPLEMENTARY RNA; MESSENGER RNA; PROTEIN FINO; PROTEIN FINP; PROTEIN TRAJ; RIBONUCLEASE; SINGLE STRANDED RNA; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; OUTER MEMBRANE PROTEIN; PANCREATIC RIBONUCLEASE; RNA BINDING PROTEIN; TRAJ PROTEIN, BACTERIA;

EID: 79961174453     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkr025     Document Type: Article
Times cited : (35)

References (49)
  • 1
    • 0023021741 scopus 로고
    • The conjugation system of F, the fertility factor of Escherichia coli
    • Ippen-Ihler, K.A. and Minkley, E.G. Jr (1986) The conjugation system of F, the fertility factor of Escherichia coli. Annu. Rev. Genet., 20, 593-624.
    • (1986) Annu. Rev. Genet. , vol.20 , pp. 593-624
    • Ippen-Ihler, K.A.1    Minkley Jr., E.G.2
  • 2
    • 0028335140 scopus 로고
    • Analysis of the sequence and gene products of the transfer region of the F sex factor
    • Frost, L.S., Ippen-Ihler, K. and Skurray, R.A. (1994) Analysis of the sequence and gene products of the transfer region of the F sex factor. Microbiol. Rev., 58, 162-210.
    • (1994) Microbiol. Rev. , vol.58 , pp. 162-210
    • Frost, L.S.1    Ippen-Ihler, K.2    Skurray, R.A.3
  • 3
    • 0015466336 scopus 로고
    • The nature of the transfer inhibitor of several F-like plasmids
    • Finnegan, D. and Willetts, N. (1972) The nature of the transfer inhibitor of several F-like plasmids. Mol. Gen. Genet., 119, 57-66.
    • (1972) Mol. Gen. Genet. , vol.119 , pp. 57-66
    • Finnegan, D.1    Willetts, N.2
  • 4
    • 0015765630 scopus 로고
    • The site of action of the F transfer inhibitor
    • Finnegan, D. and Willetts, N. (1973) The site of action of the F transfer inhibitor. Mol. Gen. Genet., 127, 307-316.
    • (1973) Mol. Gen. Genet. , vol.127 , pp. 307-316
    • Finnegan, D.1    Willetts, N.2
  • 5
    • 0021112330 scopus 로고
    • Regulation of the F conjugation genes studied by hybridization and tra-lacZ fusion
    • Gaffney, D., Skurray, R. and Willetts, N. (1983) Regulation of the F conjugation genes studied by hybridization and tra-lacZ fusion. J. Mol. Biol., 168, 103-122.
    • (1983) J. Mol. Biol. , vol.168 , pp. 103-122
    • Gaffney, D.1    Skurray, R.2    Willetts, N.3
  • 6
    • 0017380834 scopus 로고
    • The transcriptional control of fertility in F like plasmids
    • Willetts, N. (1977) The transcriptional control of fertility in F-like plasmids. J. Mol. Biol., 112, 141-148. (Pubitemid 8096609)
    • (1977) Journal of Molecular Biology , vol.112 , Issue.1 , pp. 141-148
    • Willetts, N.1
  • 7
    • 30744437713 scopus 로고    scopus 로고
    • Characterization of the opposing roles of H-NS and TraJ in transcriptional regulation of the F-plasmid tra operon
    • DOI 10.1128/JB.188.2.507-514.2006
    • Will, W.R. and Frost, L.S. (2006) Characterization of the opposing roles of H-NS and TraJ in transcriptional regulation of the F-plasmid tra operon. J. Bacteriol., 188, 507-514. (Pubitemid 43100539)
    • (2006) Journal of Bacteriology , vol.188 , Issue.2 , pp. 507-514
    • Will, W.R.1    Frost, L.S.2
  • 8
    • 0033613914 scopus 로고    scopus 로고
    • Degradation of FinP antisense RNA from F-like plasmids: The RNA-binding protein, FinO, protects FinP from ribonuclease E
    • DOI 10.1006/jmbi.1998.2404
    • Jerome, L.J., Van Biesen, T. and Frost, L.S. (1999) Degradation of FinP antisense RNA from F-like plasmids: the RNA-binding protein, FinO, protects FinP from ribonuclease E. J. Mol. Biol., 285, 1457-1473. (Pubitemid 29060448)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.4 , pp. 1457-1473
    • Jerome, L.J.1    Van Biesen, T.2    Frost, L.S.3
  • 9
    • 0026483512 scopus 로고
    • FinOP repression of the F plasmid involves extension of the half-life of FinP antisense RNA by FinO
    • Lee, S.H., Frost, L.S. and Paranchych, W. (1992) FinOP repression of the F plasmid involves extension of the half-life of FinP antisense RNA by FinO. Mol. Gen. Genet., 235, 131-139.
    • (1992) Mol. Gen. Genet. , vol.235 , pp. 131-139
    • Lee, S.H.1    Frost, L.S.2    Paranchych, W.3
  • 10
    • 0028063103 scopus 로고
    • The FinO protein of IncF plasmids binds FinP antisense RNA and its target, traJ mRNA, and promotes duplex formation
    • DOI 10.1111/j.1365-2958.1994.tb02177.x
    • Van Biesen, T. and Frost, L.S. (1994) The FinO protein of IncF plasmids binds FinP antisense RNA and its target, traJ mRNA, and promotes duplex formation. Mol. Microbiol., 14, 427-436. (Pubitemid 24337323)
    • (1994) Molecular Microbiology , vol.14 , Issue.3 , pp. 427-436
    • Van Biesen, T.1    Frost, L.S.2
  • 11
    • 0033538022 scopus 로고    scopus 로고
    • In vitro analysis of the interaction between the FinO protein and FinP antisense RNA of F-like conjugative plasmids
    • Jerome, L.J. and Frost, L.S. (1999) In vitro analysis of the interaction between the FinO protein and FinP antisense RNA of F-like conjugative plasmids. J. Biol. Chem., 274, 10356-10362.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10356-10362
    • Jerome, L.J.1    Frost, L.S.2
  • 12
    • 0033936316 scopus 로고    scopus 로고
    • Crystal structure of the bacterial conjugation repressor FinO
    • DOI 10.1038/76790
    • Ghetu, A.F., Gubbins, M.J., Frost, L.S. and Glover, J.N. (2000) Crystal structure of the bacterial conjugation repressor finO. Nat. Struct. Biol., 7, 565-569. (Pubitemid 30445913)
    • (2000) Nature Structural Biology , vol.7 , Issue.7 , pp. 565-569
    • Ghetu, A.F.1    Gubbins, M.J.2    Frost, L.S.3    Glover, J.N.M.4
  • 13
    • 0344995233 scopus 로고    scopus 로고
    • The FinO repressor of bacterial conjugation contains two RNA binding regions
    • DOI 10.1021/bi9911482
    • Ghetu, A.F., Gubbins, M.J., Oikawa, K., Kay, C.M., Frost, L.S. and Glover, J.N. (1999) The FinO repressor of bacterial conjugation contains two RNA binding regions. Biochemistry, 38, 14036-14044. (Pubitemid 29504235)
    • (1999) Biochemistry , vol.38 , Issue.42 , pp. 14036-14044
    • Ghetu, A.F.1    Gubbins, M.J.2    Oikawa, K.3    Kay, C.M.4    Frost, L.S.5    Glover, J.N.M.6
  • 14
    • 0036269981 scopus 로고    scopus 로고
    • Probing FinO-FinP RNA interactions by site-directed protein-RNA crosslinking and gelFRET
    • DOI 10.1017/S1355838202026730
    • Ghetu, A.F., Arthur, D.C., Kerppola, T.K. and Glover, J.N. (2002) Probing FinO-FinP RNA interactions by site-directed protein-RNA crosslinking and gelFRET. RNA, 8, 816-823. (Pubitemid 34620457)
    • (2002) RNA , vol.8 , Issue.6 , pp. 816-823
    • Ghetu, A.F.1    Arthur, D.C.2    Kerppola, T.K.3    Glover, J.N.M.4
  • 15
    • 0347504844 scopus 로고    scopus 로고
    • FinO is an RNA chaperone that facilitates sense-antisense RNA interactions
    • DOI 10.1093/emboj/cdg607
    • Arthur, D.C., Ghetu, A.F., Gubbins, M.J., Edwards, R.A., Frost, L.S. and Glover, J.N. (2003) FinO is an RNA chaperone that facilitates sense-antisense RNA interactions. EMBO J., 22, 6346-6355. (Pubitemid 37522591)
    • (2003) EMBO Journal , vol.22 , Issue.23 , pp. 6346-6355
    • Arthur, D.C.1    Ghetu, A.F.2    Gubbins, M.J.3    Edwards, R.A.4    Frost, L.S.5    Glover, J.N.M.6
  • 16
    • 0031739441 scopus 로고    scopus 로고
    • Analysis of the major domains of the F fertility inhibition protein, FinO
    • DOI 10.1007/s004380050856
    • Sandercock, J.R. and Frost, L.S. (1998) Analysis of the major domains of the F fertility inhibition protein, FinO. Mol. Gen. Genet., 259, 622-629. (Pubitemid 28499406)
    • (1998) Molecular and General Genetics , vol.259 , Issue.6 , pp. 622-629
    • Sandercock, J.R.1    Frost, L.S.2
  • 17
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • DOI 10.1016/0378-1119(89)90358-2
    • Ho, S.N., Hunt, H.D., Horton, R.M., Pullen, J.K. and Pease, L.R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene, 77, 51-59. (Pubitemid 19125653)
    • (1989) Gene , vol.77 , Issue.1 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 18
    • 0034840624 scopus 로고    scopus 로고
    • RNA oligonucleotide synthesis via 5′-silyl- 2′-orthoester chemistry
    • DOI 10.1006/meth.2000.1132
    • Scaringe, S.A. (2001) RNA oligonucleotide synthesis via 50-silyl-20-orthoester chemistry. Methods, 23, 206-217. (Pubitemid 32848421)
    • (2001) Methods , vol.23 , Issue.3 , pp. 206-217
    • Scaringe, S.A.1
  • 19
    • 15244359271 scopus 로고    scopus 로고
    • Method for assigning double-stranded RNA structures
    • 372
    • Brown, T.S. and Bevilacqua, P.C. (2005) Method for assigning double-stranded RNA structures. Biotechniques, 38, 368, 370, 372.
    • (2005) Biotechniques , vol.38 , pp. 368-370
    • Brown, T.S.1    Bevilacqua, P.C.2
  • 21
    • 37149049312 scopus 로고    scopus 로고
    • X-ray solution scattering (SAXS) combined with crystallography and computation: Defining accurate macromolecular structures, conformations and assemblies in solution
    • DOI 10.1017/S0033583507004635, PII S0033583507004635
    • Putnam, C.D., Hammel, M., Hura, G.L. and Tainer, J.A. (2007) X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution. Q. Rev. Biophys., 40, 191-285. (Pubitemid 350261954)
    • (2007) Quarterly Reviews of Biophysics , vol.40 , Issue.3 , pp. 191-285
    • Putnam, C.D.1    Hammel, M.2    Hura, G.L.3    Tainer, J.A.4
  • 22
    • 34248359067 scopus 로고    scopus 로고
    • ATSAS 2.1 - Towards automated and web-supported small-angle scattering data analysis
    • DOI 10.1107/S0021889807002853, PII S0021889807002853
    • Petoukhov, M.V., Konarev, P.V., Kikhney, A.G. and Svergun, D.I. (2007) ATSAS 2.1-towards automated and web-supported small-angle scattering data analysis. J. Appl. Cryst., 40, s223-s228. (Pubitemid 46732692)
    • (2007) Journal of Applied Crystallography , vol.40 , Issue.SUPPL. 1
    • Petoukhov, M.V.1    Konarev, P.V.2    Kikhney, A.G.3    Svergun, D.I.4
  • 23
    • 0031552368 scopus 로고    scopus 로고
    • On the conformation of the anticodon loops of initiator and elongator methionine tRNAs
    • DOI 10.1006/jmbi.1996.0903
    • Schweisguth, D.C. and Moore, P.B. (1997) On the conformation of the anticodon loops of initiator and elongator methionine tRNAs. J. Mol. Biol., 267, 505-519. (Pubitemid 27170678)
    • (1997) Journal of Molecular Biology , vol.267 , Issue.3 , pp. 505-519
    • Schweisguth, D.C.1    Moore, P.B.2
  • 27
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A protein-protein docking approach based on biochemical or biophysical information
    • DOI 10.1021/ja026939x
    • Dominguez, C., Boelens, R. and Bonvin, A.M. (2003) HADDOCK: a protein-protein docking approach based on biochemical or biophysical information. J. Am. Chem. Soc., 125, 1731-1737. (Pubitemid 36232568)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.7 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.J.J.3
  • 28
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • DOI 10.1107/S0021889895007047
    • Svergun, D.I., Barberato, C. and Koch, M.H.J. (1995) CRYSOL-a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr., 28, 768-773. (Pubitemid 3014671)
    • (1995) Journal of Applied Crystallography , vol.28 , Issue.6 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.3
  • 29
    • 33748663254 scopus 로고    scopus 로고
    • THESEUS: Maximum likelihood superpositioning and analysis of macromolecular structures
    • DOI 10.1093/bioinformatics/btl332
    • Theobald, D.L. and Wuttke, D.S. (2006) THESEUS: maximum likelihood superpositioning and analysis of macromolecular structures. Bioinformatics, 22, 2171-2172. (Pubitemid 44390914)
    • (2006) Bioinformatics , vol.22 , Issue.17 , pp. 2171-2172
    • Theobald, D.L.1    Wuttke, D.S.2
  • 31
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: An automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations
    • DOI 10.1093/nar/gkh381
    • Dolinsky, T.J., Nielsen, J.E., McCammon, J.A. and Baker, N.A. (2004) PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations. Nucleic Acids Res., 32, W665-W667. (Pubitemid 38997419)
    • (2004) Nucleic Acids Research , vol.32 , Issue.WEB SERVER ISS.
    • Dolinsky, T.J.1    Nielsen, J.E.2    McCammon, J.A.3    Baker, N.A.4
  • 33
    • 0027527532 scopus 로고
    • Structural and functional analyses of the FinP antisense RNA regulatory system of the F conjugative plasmid
    • DOI 10.1111/j.1365-2958.1993.tb00901.x
    • Van Biesen, T., Soderbom, F., Wagner, E.G. and Frost, L.S. (1993) Structural and functional analyses of the FinP antisense RNA regulatory system of the F conjugative plasmid. Mol. Microbiol., 10, 35-43. (Pubitemid 23311192)
    • (1993) Molecular Microbiology , vol.10 , Issue.1 , pp. 35-43
    • Van Biesen, T.1    Soderbom, F.2    Wagner, E.G.H.3    Frost, L.S.4
  • 34
    • 0025171946 scopus 로고
    • Purification and characterization of Escherichia coli RNase I. Comparisons with RNase M
    • Meador, J. III, Cannon, B., Cannistraro, V.J. and Kennell, D. (1990) Purification and characterization of Escherichia coli RNase I. Comparisons with RNase M. Eur. J. Biochem., 187, 549-553. (Pubitemid 20074917)
    • (1990) European Journal of Biochemistry , vol.187 , Issue.3 , pp. 549-553
    • Meador III, J.1    Cannon, B.2    Cannistraro, V.J.3    Kennell, D.4
  • 36
    • 77749311718 scopus 로고    scopus 로고
    • Bridging the solution divide: Comprehensive structural analyses of dynamic RNA, DNA, and protein assemblies by small-angle X-ray scattering
    • Rambo, R.P. and Tainer, J.A. (2010) Bridging the solution divide: comprehensive structural analyses of dynamic RNA, DNA, and protein assemblies by small-angle X-ray scattering. Curr. Opin. Struct. Biol., 20, 128-137.
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 128-137
    • Rambo, R.P.1    Tainer, J.A.2
  • 37
    • 34248363563 scopus 로고    scopus 로고
    • Structural analysis of flexible proteins in solution by small angle X-ray scattering combined with crystallography
    • DOI 10.1016/j.jsb.2006.09.008, PII S1047847706002917, Structural Analysis of Supramolecular Assembles by Hybrid Methods
    • Tsutakawa, S.E., Hura, G.L., Frankel, K.A., Cooper, P.K. and Tainer, J.A. (2007) Structural analysis of flexible proteins in solution by small angle X-ray scattering combined with crystallography. J. Struct. Biol., 158, 214-223. (Pubitemid 46729661)
    • (2007) Journal of Structural Biology , vol.158 , Issue.2 , pp. 214-223
    • Tsutakawa, S.E.1    Hura, G.L.2    Frankel, K.A.3    Cooper, P.K.4    Tainer, J.A.5
  • 38
    • 1842419667 scopus 로고    scopus 로고
    • Structure of the La motif: A winged helix domain mediates RNA binding via a conserved aromatic patch
    • DOI 10.1038/sj.emboj.7600115
    • Dong, G., Chakshusmathi, G., Wolin, S.L. and Reinisch, K.M. (2004) Structure of the La motif: a winged helix domain mediates RNA binding via a conserved aromatic patch. EMBO J., 23, 1000-1007. (Pubitemid 38436865)
    • (2004) EMBO Journal , vol.23 , Issue.5 , pp. 1000-1007
    • Dong, G.1    Chakshusmathi, G.2    Wolin, S.L.3    Reinisch, K.M.4
  • 39
    • 2442679207 scopus 로고    scopus 로고
    • Structural basis for overhang-specific small interfering RNA recognition by the PAZ domain
    • DOI 10.1038/nature02519
    • Ma, J.B., Ye, K. and Patel, D.J. (2004) Structural basis for overhang-specific small interfering RNA recognition by the PAZ domain. Nature, 429, 318-322. (Pubitemid 38684819)
    • (2004) Nature , vol.429 , Issue.6989 , pp. 318-322
    • Ma, J.-B.1    Ye, K.2    Patel, D.J.3
  • 40
    • 19344362237 scopus 로고    scopus 로고
    • Structural insights into RNA quality control: The Ro autoantigen binds misfolded RNAs via its central cavity
    • DOI 10.1016/j.cell.2005.03.009, PII S0092867405002424
    • Stein, A.J., Fuchs, G., Fu, C., Wolin, S.L. and Reinisch, K.M. (2005) Structural insights into RNA quality control: the Ro autoantigen binds misfolded RNAs via its central cavity. Cell, 121, 529-539. (Pubitemid 40720007)
    • (2005) Cell , vol.121 , Issue.4 , pp. 529-539
    • Stein, A.J.1    Fuchs, G.2    Fu, C.3    Wolin, S.L.4    Reinisch, K.M.5
  • 41
    • 0025188665 scopus 로고
    • Renaturation of complementary DNA strands mediated by purified mammalian heterogeneous nuclear ribonucleoprotein A1 protein: Implications for a mechanism for rapid molecular assembly
    • Pontius, B.W. and Berg, P. (1990) Renaturation of complementary DNA strands mediated by purified mammalian heterogeneous nuclear ribonucleoprotein A1 protein: implications for a mechanism for rapid molecular assembly. Proc. Natl Acad. Sci. USA, 87, 8403-8407.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 8403-8407
    • Pontius, B.W.1    Berg, P.2
  • 42
    • 2242469712 scopus 로고    scopus 로고
    • Structure of the HIV-1 nucleocapsid protein bound to the SL3 ψ-RNA recognition element
    • DOI 10.1126/science.279.5349.384
    • De Guzman, R.N., Wu, Z.R., Stalling, C.C., Pappalardo, L., Borer, P.N. and Summers, M.F. (1998) Structure of the HIV-1 nucleocapsid protein bound to the SL3 psi-RNA recognition element. Science, 279, 384-388. (Pubitemid 28063374)
    • (1998) Science , vol.279 , Issue.5349 , pp. 384-388
    • De Guzman, R.N.1    Wu, Z.R.2    Stalling, C.C.3    Pappalardo, L.4    Borer, P.N.5    Summers, M.F.6
  • 43
    • 3442902456 scopus 로고    scopus 로고
    • The role of structural disorder in the function of RNA and protein chaperones
    • DOI 10.1096/fj.04-1584rev
    • Tompa, P. and Csermely, P. (2004) The role of structural disorder in the function of RNA and protein chaperones. FASEB J., 18, 1169-1175. (Pubitemid 39006878)
    • (2004) FASEB Journal , vol.18 , Issue.11 , pp. 1169-1175
    • Tompa, P.1    Csermely, P.2
  • 44
    • 4344682527 scopus 로고    scopus 로고
    • The small RNA regulators of Escherichia coli: Roles and mechanisms
    • DOI 10.1146/annurev.micro.58.030603.123841
    • Gottesman, S. (2004) The small RNA regulators of Escherichia coli: roles and mechanisms. Annu. Rev. Microbiol., 58, 303-328. (Pubitemid 39551989)
    • (2004) Annual Review of Microbiology , vol.58 , pp. 303-328
    • Gottesman, S.1
  • 45
    • 36249019206 scopus 로고    scopus 로고
    • Dissecting RNA chaperone activity
    • DOI 10.1261/rna.671807
    • Rajkowitsch, L. and Schroeder, R. (2007) Dissecting RNA chaperone activity. RNA, 13, 2053-2060. (Pubitemid 350127547)
    • (2007) RNA , vol.13 , Issue.12 , pp. 2053-2060
    • Rajkowitsch, L.1    Schroeder, R.2
  • 46
    • 0033057057 scopus 로고    scopus 로고
    • Protein ProQ influences osmotic activation of compatible solute transporter ProP in Escherichia coli K-12
    • Kunte, H.J., Crane, R.A., Culham, D.E., Richmond, D. and Wood, J.M. (1999) Protein ProQ influences osmotic activation of compatible solute transporter ProP in Escherichia coli K-12. J. Bacteriol., 181, 1537-1543. (Pubitemid 29110814)
    • (1999) Journal of Bacteriology , vol.181 , Issue.5 , pp. 1537-1543
    • Kunte, H.J.1    Crane, R.A.2    Culham, D.E.3    Richmond, D.4    Wood, J.M.5
  • 47
    • 0024614224 scopus 로고
    • Insertion proQ220::Tn5 alters regulation of proline porter II, a transporter of proline and glycine betaine in Escherichia coli
    • Milner, J.L. and Wood, J.M. (1989) Insertion proQ220::Tn5 alters regulation of proline porter II, a transporter of proline and glycine betaine in Escherichia coli. J. Bacteriol., 171, 947-951.
    • (1989) J. Bacteriol. , vol.171 , pp. 947-951
    • Milner, J.L.1    Wood, J.M.2
  • 48
    • 5444265451 scopus 로고    scopus 로고
    • Overexpression, purification, and characterization of ProQ, a posttranslational regulator for osmoregulatory transporter ProP of Escherichia coli
    • DOI 10.1021/bi048561g
    • Smith, M.N., Crane, R.A., Keates, R.A. and Wood, J.M. (2004) Overexpression, purification, and characterization of ProQ, a posttranslational regulator for osmoregulatory transporter ProP of Escherichia coli. Biochemistry, 43, 12979-12989. (Pubitemid 39362767)
    • (2004) Biochemistry , vol.43 , Issue.41 , pp. 12979-12989
    • Smith, M.N.1    Crane, R.A.2    Keates, R.A.B.3    Wood, J.M.4
  • 49
    • 33947405688 scopus 로고    scopus 로고
    • Structural and functional analysis of ProQ: An osmoregulatory protein of Escherichia coli
    • DOI 10.1021/bi6023786
    • Smith, M.N., Kwok, S.C., Hodges, R.S. and Wood, J.M. (2007) Structural and functional analysis of ProQ: an osmoregulatory protein of Escherichia coli. Biochemistry, 46, 3084-3095. (Pubitemid 46449132)
    • (2007) Biochemistry , vol.46 , Issue.11 , pp. 3084-3095
    • Smith, M.N.1    Kwok, S.C.2    Hodges, R.S.3    Wood, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.