메뉴 건너뛰기




Volumn 77, Issue 1, 2009, Pages 202-208

Solution structure of the DNA binding domain of AraC protein

Author keywords

Gene regulation; NMR; Transcription factor

Indexed keywords

ARAC PROTEIN; DNA BINDING PROTEIN; MARA PROTEIN; ROB PROTEIN; UNCLASSIFIED DRUG;

EID: 70349313266     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22431     Document Type: Article
Times cited : (32)

References (46)
  • 2
    • 0036786814 scopus 로고    scopus 로고
    • Growing repertoire of AraC/XylS activators
    • Egan SM. Growing repertoire of AraC/XylS activators. J Bacteriol 2002;184:5529-5532.
    • (2002) J Bacteriol , vol.184 , pp. 5529-5532
    • Egan, S.M.1
  • 3
    • 0030964038 scopus 로고    scopus 로고
    • Structural basis for ligand-regulated oligomerization of AraC
    • DOI 10.1126/science.276.5311.421
    • Soisson S, MacDougall-Shackleton B, Schleif R, Wolberger C. Structural basis for ligand-regulated oligomerization of AraC. Science 1997;276:421-425. (Pubitemid 27180705)
    • (1997) Science , vol.276 , Issue.5311 , pp. 421-425
    • Soisson, S.M.1    MacDougall-Shackleton, B.2    Schleif, R.3    Wolberger, C.4
  • 4
    • 0027158918 scopus 로고
    • Functional domains of AraC protein
    • Bustos S, Schleif R. Functional domains of AraC protein. Proc Natl Acad Sci USA 1993;90:5638-5642.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 5638-5642
    • Bustos, S.1    Schleif, R.2
  • 5
  • 7
    • 0035815103 scopus 로고    scopus 로고
    • Mapping arm-DNA-binding domain interactions in AraC
    • DOI 10.1006/jmbi.2001.4531
    • Wu M, Schleif R. Mapping arm-DNA-binding domain interactions in AraC. J Mol Biol 2001;307:1001-1009. (Pubitemid 33029949)
    • (2001) Journal of Molecular Biology , vol.307 , Issue.4 , pp. 1001-1009
    • Wu, M.1    Schleif, R.2
  • 8
    • 0025202249 scopus 로고
    • DNA looping and unlooping by AraC protein
    • Lobel R, Schleif R. DNA looping and unlooping by AraC protein. Science 1990;250:528-532. (Pubitemid 120031777)
    • (1990) Science , vol.250 , Issue.4980 , pp. 528-532
    • Lobell, R.B.1    Schleif, R.F.2
  • 9
    • 0027463760 scopus 로고
    • Variation of half-site organization and DNA looping by AraC protein
    • Carra J, Schleif R. Variation of half-site organization and DNA looping by AraC protein. EMBO J 1993;12:35-44. (Pubitemid 23042380)
    • (1993) EMBO Journal , vol.12 , Issue.1 , pp. 35-44
    • Carra, J.H.1    Schleif, R.F.2
  • 10
    • 0032496390 scopus 로고    scopus 로고
    • Apo-AraC actively seeks to loop
    • Seabold R, Schleif R. Apo-AraC actively seeks to loop. J Mol Biol 1998;278:529-538.
    • (1998) J Mol Biol , vol.278 , pp. 529-538
    • Seabold, R.1    Schleif, R.2
  • 12
    • 0034564982 scopus 로고    scopus 로고
    • Regulation of the L-arabinose operon of Escherichia coli
    • DOI 10.1016/S0168-9525(00)02153-3, PII S0168952500021533
    • Schleif R. Regulation of the L-arabinose operon of Escherichia coli. Trends Genet 2000;16:559-565. (Pubitemid 30843834)
    • (2000) Trends in Genetics , vol.16 , Issue.12 , pp. 559-565
    • Schleif, R.1
  • 13
    • 0037337551 scopus 로고    scopus 로고
    • The AraC protein: A love-hate relationship
    • Schleif R. The AraC protein: a love-hate relationship. Bio Essays 2003;25:274-282.
    • (2003) Bio Essays , vol.25 , pp. 274-282
    • Schleif, R.1
  • 14
    • 0011064091 scopus 로고
    • The DNA loop model for ara repression: AraC protein occupies the proposed loop sites in vivo and repression-negative mutations lie in these same sites
    • Martin K, Huo L, Schleif R. The DNA loop model for ara repression: AraC protein occupies the proposed loop sites in vivo and repression-negative mutations lie in these same sites. Proc Nat Acad Sci USA 1986;83:3654-3658. (Pubitemid 16062343)
    • (1986) Proceedings of the National Academy of Sciences of the United States of America , vol.83 , Issue.11 , pp. 3654-3658
    • Martin, K.1    Huo, L.2    Schleif, R.F.3
  • 15
    • 0038687706 scopus 로고    scopus 로고
    • Binding of the Escherichia coli MelR protein to the melAB promoter: Orientation of MelR subunits and investigation of MelR-DNA contacts
    • Grainger DC, Belyaeva TA, Lee DJ, Hyde EI, Busby SJW. Binding of the Escherichia coli MelR protein to the melAB promoter: orientation of MelR subunits and investigation of MelR-DNA contacts. Mol Microbiol 2003;48:335-348.
    • (2003) Mol Microbiol , vol.48 , pp. 335-348
    • Grainger, D.C.1    Belyaeva, T.A.2    Lee, D.J.3    Hyde, E.I.4    Busby, S.J.W.5
  • 16
    • 0028173180 scopus 로고
    • DNA-dependent renaturation of an insoluble DNA binding protein
    • Egan S, Schleif R. DNA-dependent renaturation of an insoluble DNA binding protein. J Mol Biol 1994;243:821-829.
    • (1994) J Mol Biol , vol.243 , pp. 821-829
    • Egan, S.1    Schleif, R.2
  • 17
    • 42549109171 scopus 로고    scopus 로고
    • Roles of effectors in XylS-dependent transcription activation: Intramolecular domain derepression and DNA binding
    • DOI 10.1128/JB.01784-07
    • Domínguez-Cuevas P, Marín P, Busby S, Ramos JL, Marqués S. Roles of effectors in XylS-dependent transcription activation: intramolecular domain derepression and DNA binding. J Bacteriol 2008;190:3118-3128. (Pubitemid 351581406)
    • (2008) Journal of Bacteriology , vol.190 , Issue.9 , pp. 3118-3128
    • Dominguez-Cuevas, P.1    Marin, P.2    Busby, S.3    Ramos, J.L.4    Marques, S.5
  • 18
    • 3242891579 scopus 로고    scopus 로고
    • DNA-binding specificity of AdpA, a transcriptional activator in the A-factor regulatory cascade in Streptomyces griseus
    • DOI 10.1111/j.1365-2958.2004.04153.x
    • Yamazaki H, Tomono A, Ohnishi Y, Horinouchi S. DNA-binding specificity of AdpA, a transcriptional activator in the A-factor regulatory cascade in Streptomyces griseus. Mol Microbiol 2004;53:555-572. (Pubitemid 38998175)
    • (2004) Molecular Microbiology , vol.53 , Issue.2 , pp. 555-572
    • Yamazaki, H.1    Tomono, A.2    Ohnishi, Y.3    Horinouchi, S.4
  • 20
    • 0001759947 scopus 로고    scopus 로고
    • Crystal structure of the Escherichia coli Rob transcription factor in complex with DNA
    • DOI 10.1038/75213
    • Kwon HJ, Bennik MH, Demple B, Ellenberger T. Crystal structure of the Escherichia coli Rob transcription factor in complex with DNA. Nat Struct Biol 2000;7:424-430. (Pubitemid 30250008)
    • (2000) Nature Structural Biology , vol.7 , Issue.5 , pp. 424-430
    • Kwon, H.J.1    Bennik, M.H.J.2    Demple, B.3    Ellenberger, T.4
  • 21
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar RS, Record MT Jr. Coupling of local folding to site-specific binding of proteins to DNA. Science 1994;263:777-784.
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record Jr., M.T.2
  • 23
    • 0034992645 scopus 로고    scopus 로고
    • A method for efficient isotopic labeling of recombinant proteins
    • DOI 10.1023/A:1011254402785
    • Marley J, Lu M, Bracken C. A method for efficient isotopic labeling of recombinant proteins. J Biomol NMR 2001;20:71-75. (Pubitemid 32519656)
    • (2001) Journal of Biomolecular NMR , vol.20 , Issue.1 , pp. 71-75
    • Marley, J.1    Lu, M.2    Bracken, C.3
  • 24
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace CN, Vajdos F, Lee L, Grimsley G, Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Sci 1995;4:2411-2423.
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Lee, L.3    Grimsley, G.4    Gray, T.5
  • 25
    • 3042610198 scopus 로고    scopus 로고
    • Biochemical and physiological properties of the DNA binding domain of AraC protein
    • DOI 10.1016/j.jmb.2004.05.018, PII S0022283604005856
    • Timmes A, Rodgers ME, Schleif R. Biochemical and physiological properties of the DNA binding domain of AraC protein. J Mol Biol 2004;340:731-738. (Pubitemid 38829634)
    • (2004) Journal of Molecular Biology , vol.340 , Issue.4 , pp. 731-738
    • Timmes, A.1    Rodgers, M.2    Schleif, R.3
  • 28
    • 34249765651 scopus 로고
    • NMRView: A computer program for the visualization and analysis of NMR data
    • Johnson BA, Blevins RA. NMRView: a computer program for the visualization and analysis of NMR data. J Biomol NMR 1994;4:603-614.
    • (1994) J Biomol NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 30
    • 0036873589 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS
    • DOI 10.1023/A:1021614115432
    • Herrmann T, Güntert P, Wüthrich K. Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS. J Biomol NMR 2002;24:171-189. (Pubitemid 36113646)
    • (2002) Journal of Biomolecular NMR , vol.24 , Issue.3 , pp. 171-189
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 31
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • DOI 10.1016/S0022-2836(02)00241-3
    • Herrmann T, Güntert P, Wüthrich K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol 2002;319:209-227. (Pubitemid 34729497)
    • (2002) Journal of Molecular Biology , vol.319 , Issue.1 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 33
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • Güntert P. Automated NMR structure calculation with CYANA. Meth Mol Biol 2004;278:353-378.
    • (2004) Meth Mol Biol , vol.278 , pp. 353-378
    • Güntert, P.1
  • 34
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • DOI 10.1023/A:1008392405740
    • Cornilescu G, Delaglio F, Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR 1999;13:289-302. (Pubitemid 29143535)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.3 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 37
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • DOI 10.1016/0263-7855(96)00009-4
    • Koradi R, Billeter M, Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graphics 1996;14:51-55. (Pubitemid 26152976)
    • (1996) Journal of Molecular Graphics , vol.14 , Issue.1 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 39
    • 0028034697 scopus 로고
    • Reaching out. Locating and lengthening the interdomain linker in AraC protein
    • DOI 10.1006/jmbi.1994.1584
    • Eustance R, Bustos S, Schleif R. Reaching out: locating and lengthening the interdomain linker in AraC protein. J Mol Biol 1994;242:330-338. (Pubitemid 2134849)
    • (1994) Journal of Molecular Biology , vol.242 , Issue.4 , pp. 330-338
    • Eustance, R.J.1    Bustos, S.A.2    Schleif, R.F.3
  • 40
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: As domains continue to swap
    • DOI 10.1110/ps.0201402
    • Liu Y, Eisenberg D. 3D domain swapping: as domains continue to swap. Protein Sci 2002;11:1285-1298. (Pubitemid 34547201)
    • (2002) Protein Science , vol.11 , Issue.6 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 41
    • 33646376290 scopus 로고
    • Spin diffusion measurements: Spin echos in the presence of a time-dependent field gradient
    • Stejskal EO, Tanner JE. Spin diffusion measurements: spin echos in the presence of a time-dependent field gradient. J Chem Phys 42 1965;42:288-291.
    • (1965) J Chem Phys 42 , vol.42 , pp. 288-291
    • Stejskal, E.O.1    Tanner, J.E.2
  • 42
    • 44949277996 scopus 로고
    • A PFG experiment for accurate diffusion and flow studies in the presence of eddy currents
    • Gibbs SJ, Johnson CSJ. A PFG experiment for accurate diffusion and flow studies in the presence of eddy currents. J Magn Reson 1991;93:395-402.
    • (1991) J Magn Reson , vol.93 , pp. 395-402
    • Gibbs, S.J.1    Johnson, C.S.J.2
  • 43
    • 0030582731 scopus 로고    scopus 로고
    • How AraC interacts specifically with its target DNAs
    • DOI 10.1006/jmbi.1996.0668
    • Niland P, Huhne R, Müller-Hill B. How AraC interacts specifically with its target DNAs. J Mol Biol 1996;264:667-674. (Pubitemid 27013552)
    • (1996) Journal of Molecular Biology , vol.264 , Issue.4 , pp. 667-674
    • Niland, P.1    Huhne, R.2    Muller-Hill, B.3
  • 45
    • 0029863748 scopus 로고    scopus 로고
    • Transcriptional activation of promoters of the superoxide and multiple antibiotic resistance regulons by Rob, a binding protein of the Escherichia coli origin of chromosomal replication
    • Jair K, Yu X, Skarstad K, Thöny B, Fujita N, Ishihama A, Wolf R Jr. Transcriptional activation of promoters of the superoxide and multiple antibiotic resistance regulons by Rob, a binding protein of the Escherichia coli origin of chromosomal replication. J Bacteriol 1996;178:2507-2513. (Pubitemid 26134472)
    • (1996) Journal of Bacteriology , vol.178 , Issue.9 , pp. 2507-2513
    • Jair, K.-W.1    Yu, X.2    Skarstad, K.3    Thony, B.4    Fujita, N.5    Ishihama, A.6    Wolf Jr., R.E.7
  • 46
    • 0035895918 scopus 로고    scopus 로고
    • The C-terminal End of AraC Tightly Binds to the Rest of Its Domain
    • DOI 10.1074/jbc.M007956200
    • Harmer T, Schleif R. The C-terminal end of AraC tightly binds to the rest of its domain. J Biol Chem 2001;276:4886-4888. (Pubitemid 37371376)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.7 , pp. 4886-4888
    • Harmer, T.L.1    Schleif, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.