메뉴 건너뛰기




Volumn 369, Issue 4, 2007, Pages 1070-1078

Structural Basis of DNA Recognition by the Alternative Sigma-factor, σ54

Author keywords

Protein DNA complex; RNA polymerase; RpoN box; Sigma 54; Transcription initiation

Indexed keywords

SIGMA FACTOR; SIGMA FACTOR RPON;

EID: 34248578701     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.04.019     Document Type: Article
Times cited : (35)

References (32)
  • 1
    • 0037123763 scopus 로고    scopus 로고
    • Views of transcription initiation
    • Young B.A., Gruber T.M., and Gross C.A. Views of transcription initiation. Cell 109 (2002) 417-420
    • (2002) Cell , vol.109 , pp. 417-420
    • Young, B.A.1    Gruber, T.M.2    Gross, C.A.3
  • 3
    • 0025361357 scopus 로고
    • A bacterial enhancer functions to tether a transcriptional activator near a promoter
    • Wedel A., Weiss D.S., Popham D., Droge P., and Kustu S. A bacterial enhancer functions to tether a transcriptional activator near a promoter. Science 248 (1990) 486-490
    • (1990) Science , vol.248 , pp. 486-490
    • Wedel, A.1    Weiss, D.S.2    Popham, D.3    Droge, P.4    Kustu, S.5
  • 4
    • 33846895023 scopus 로고    scopus 로고
    • Bacterial enhancer-binding proteins: unlocking sigma(54)-dependent gene transcription
    • Rappas M., Bose D., and Zhang X. Bacterial enhancer-binding proteins: unlocking sigma(54)-dependent gene transcription. Curr. Opin. Struct. Biol. 17 (2007) 110-116
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 110-116
    • Rappas, M.1    Bose, D.2    Zhang, X.3
  • 5
  • 6
    • 0033962752 scopus 로고    scopus 로고
    • Phosphorylation of the flagellar regulatory protein FlrC is necessary for Vibrio cholerae motility and enhanced colonization
    • Correa N.E., Lauriano C.M., McGee R., and Klose K.E. Phosphorylation of the flagellar regulatory protein FlrC is necessary for Vibrio cholerae motility and enhanced colonization. Mol. Microbiol. 35 (2000) 743-755
    • (2000) Mol. Microbiol. , vol.35 , pp. 743-755
    • Correa, N.E.1    Lauriano, C.M.2    McGee, R.3    Klose, K.E.4
  • 8
    • 27644559492 scopus 로고    scopus 로고
    • Conformational changes of Escherichia coli sigma54-RNA-polymerase upon closed-promoter complex formation
    • Ray P., Hall R.J., Finn R.D., Chen S., Patwardhan A., Buck M., and van Heel M. Conformational changes of Escherichia coli sigma54-RNA-polymerase upon closed-promoter complex formation. J. Mol. Biol. 354 (2005) 201-205
    • (2005) J. Mol. Biol. , vol.354 , pp. 201-205
    • Ray, P.1    Hall, R.J.2    Finn, R.D.3    Chen, S.4    Patwardhan, A.5    Buck, M.6    van Heel, M.7
  • 9
    • 33748625150 scopus 로고    scopus 로고
    • The structural basis for promoter -35 element recognition by the group IV sigma factors
    • Lane W.J., and Darst S.A. The structural basis for promoter -35 element recognition by the group IV sigma factors. PLoS. Biol. 4 (2006) e269
    • (2006) PLoS. Biol. , vol.4
    • Lane, W.J.1    Darst, S.A.2
  • 10
    • 1842766125 scopus 로고    scopus 로고
    • Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformation
    • Sorenson M.K., Ray S.S., and Darst S.A. Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformation. Mol. Cell 14 (2004) 127-138
    • (2004) Mol. Cell , vol.14 , pp. 127-138
    • Sorenson, M.K.1    Ray, S.S.2    Darst, S.A.3
  • 11
    • 0036203066 scopus 로고    scopus 로고
    • Structure of the bacterial RNA polymerase promoter specificity sigma subunit
    • Campbell E.A., Muzzin O., Chlenov M., Sun J.L., Olson C.A., Weinman O., et al. Structure of the bacterial RNA polymerase promoter specificity sigma subunit. Mol. Cell 9 (2002) 527-539
    • (2002) Mol. Cell , vol.9 , pp. 527-539
    • Campbell, E.A.1    Muzzin, O.2    Chlenov, M.3    Sun, J.L.4    Olson, C.A.5    Weinman, O.6
  • 12
    • 0033570908 scopus 로고    scopus 로고
    • Compilation and analysis of sigma(54)-dependent promoter sequences
    • Barrios H., Valderrama B., and Morett E. Compilation and analysis of sigma(54)-dependent promoter sequences. Nucl. Acids Res. 27 (1999) 4305-4313
    • (1999) Nucl. Acids Res. , vol.27 , pp. 4305-4313
    • Barrios, H.1    Valderrama, B.2    Morett, E.3
  • 13
    • 0029029993 scopus 로고
    • Core RNA polymerase and promoter DNA interactions of purified domains of sigma N: bipartite functions
    • Cannon W., Missailidis S., Smith C., Cottier A., Austin S., Moore M., and Buck M. Core RNA polymerase and promoter DNA interactions of purified domains of sigma N: bipartite functions. J. Mol. Biol. 248 (1995) 781-803
    • (1995) J. Mol. Biol. , vol.248 , pp. 781-803
    • Cannon, W.1    Missailidis, S.2    Smith, C.3    Cottier, A.4    Austin, S.5    Moore, M.6    Buck, M.7
  • 14
    • 0043032654 scopus 로고    scopus 로고
    • Mapping sigma 54-RNA polymerase interactions at the -24 consensus promoter element
    • Burrows P.C., Severinov K., Ishihama A., Buck M., and Wigneshweraraj S.R. Mapping sigma 54-RNA polymerase interactions at the -24 consensus promoter element. J. Biol. Chem. 278 (2003) 29728-29743
    • (2003) J. Biol. Chem. , vol.278 , pp. 29728-29743
    • Burrows, P.C.1    Severinov, K.2    Ishihama, A.3    Buck, M.4    Wigneshweraraj, S.R.5
  • 15
    • 29244469944 scopus 로고    scopus 로고
    • The C-terminal RpoN domain of sigma54 forms an unpredicted helix-turn-helix motif similar to domains of sigma70
    • Doucleff M., Malak L.T., Pelton J.G., and Wemmer D. E. The C-terminal RpoN domain of sigma54 forms an unpredicted helix-turn-helix motif similar to domains of sigma70. J. Biol. Chem. 280 (2005) 41530-41536
    • (2005) J. Biol. Chem. , vol.280 , pp. 41530-41536
    • Doucleff, M.1    Malak, L.T.2    Pelton, J.G.3    Wemmer, D. E.4
  • 17
    • 0035937702 scopus 로고    scopus 로고
    • Roles for the C-terminal region of sigma 54 in transcriptional silencing and DNA binding
    • Wang L., and Gralla J.D. Roles for the C-terminal region of sigma 54 in transcriptional silencing and DNA binding. J. Biol. Chem. 276 (2001) 8979-8986
    • (2001) J. Biol. Chem. , vol.276 , pp. 8979-8986
    • Wang, L.1    Gralla, J.D.2
  • 18
    • 0030609996 scopus 로고    scopus 로고
    • Engrailed (Gln50-→Lys) homeodomain-DNA complex at 1.9 Å resolution: structural basis for enhanced affinity and altered specificity
    • Tucker-Kellogg L., Rould M.A., Chambers K.A., Ades S.E., Sauer R.T., and Pabo C.O. Engrailed (Gln50-→Lys) homeodomain-DNA complex at 1.9 Å resolution: structural basis for enhanced affinity and altered specificity. Structure 5 (1997) 1047-1054
    • (1997) Structure , vol.5 , pp. 1047-1054
    • Tucker-Kellogg, L.1    Rould, M.A.2    Chambers, K.A.3    Ades, S.E.4    Sauer, R.T.5    Pabo, C.O.6
  • 19
    • 0022997581 scopus 로고
    • Deletion loop mutagenesis of the nifL promoter from Klebsiella pneumoniae: role of the -26 to -12 region in promoter function
    • Khan H., Buck M., and Dixon R. Deletion loop mutagenesis of the nifL promoter from Klebsiella pneumoniae: role of the -26 to -12 region in promoter function. Gene 45 (1986) 281-288
    • (1986) Gene , vol.45 , pp. 281-288
    • Khan, H.1    Buck, M.2    Dixon, R.3
  • 21
    • 0037123602 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: an RNA polymerase holoenzyme-DNA complex
    • Murakami K.S., Masuda S., Campbell E.A., Muzzin O., and Darst S.A. Structural basis of transcription initiation: an RNA polymerase holoenzyme-DNA complex. Science 296 (2002) 1285-1290
    • (2002) Science , vol.296 , pp. 1285-1290
    • Murakami, K.S.1    Masuda, S.2    Campbell, E.A.3    Muzzin, O.4    Darst, S.A.5
  • 22
    • 0037474295 scopus 로고    scopus 로고
    • Multiple roles of the RNA polymerase beta subunit flap domain in sigma 54-dependent transcription
    • Wigneshweraraj S.R., Kuznedelov K., Severinov K., and Buck M. Multiple roles of the RNA polymerase beta subunit flap domain in sigma 54-dependent transcription. J. Biol. Chem. 278 (2003) 3455-3465
    • (2003) J. Biol. Chem. , vol.278 , pp. 3455-3465
    • Wigneshweraraj, S.R.1    Kuznedelov, K.2    Severinov, K.3    Buck, M.4
  • 24
    • 34249765651 scopus 로고
    • NMRView: a computer program for the visualization and analysis of NMR data
    • Johnson B.A., and Blevins B.A. NMRView: a computer program for the visualization and analysis of NMR data. J. Biomol. NMR 4 (1994) 603-614
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, B.A.2
  • 25
    • 0035072685 scopus 로고    scopus 로고
    • Improved NMR spectra of a protein-DNA complex through rational mutagenesis and the application of a sensitivity optimized isotope-filtered NOESY experiment
    • Iwahara J., Wojciak J.M., and Clubb R.T. Improved NMR spectra of a protein-DNA complex through rational mutagenesis and the application of a sensitivity optimized isotope-filtered NOESY experiment. J. Biomol. NMR 19 (2001) 231-241
    • (2001) J. Biomol. NMR , vol.19 , pp. 231-241
    • Iwahara, J.1    Wojciak, J.M.2    Clubb, R.T.3
  • 26
    • 33845555707 scopus 로고
    • Exchangeable proton NMR without base-line distorsion, using new strong-pulse sequences
    • Pierre P., and Gueron G. Exchangeable proton NMR without base-line distorsion, using new strong-pulse sequences. J. Am. Chem. Soc. 104 (1982) 7310-7311
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 7310-7311
    • Pierre, P.1    Gueron, G.2
  • 27
    • 0030808350 scopus 로고    scopus 로고
    • Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy: application to a bacteriophage lambda N-peptide/boxB RNA complex
    • Zwahlen C., Legault P., F., V. S. J., Greenblatt J., Konrat R., and Kay L.E. Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy: application to a bacteriophage lambda N-peptide/boxB RNA complex. J. Am. Chem. Soc. 119 (1997) 6711-6721
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 6711-6721
    • Zwahlen, C.1    Legault, P.2    Vincent, S.J.F.3    Greenblatt, J.4    Konrat, R.5    Kay, L.E.6
  • 28
    • 0028545648 scopus 로고
    • Measurement of HN-H alpha J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods
    • Kuboniwa H., Grzesiek S., Delaglio F., and Bax A. Measurement of HN-H alpha J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods. J. Biomol. NMR 4 (1994) 871-878
    • (1994) J. Biomol. NMR , vol.4 , pp. 871-878
    • Kuboniwa, H.1    Grzesiek, S.2    Delaglio, F.3    Bax, A.4
  • 29
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • Guntert P. Automated NMR structure calculation with CYANA. Methods Mol. Biol. 278 (2004) 353-378
    • (2004) Methods Mol. Biol. , vol.278 , pp. 353-378
    • Guntert, P.1
  • 31
    • 0036500804 scopus 로고    scopus 로고
    • The structure of the Dead ringer-DNA complex reveals how AT-rich interaction domains (ARIDs) recognize DNA
    • Iwahara J., Iwahara M., Daughdrill G.W., Ford J., and Clubb R.T. The structure of the Dead ringer-DNA complex reveals how AT-rich interaction domains (ARIDs) recognize DNA. EMBO J. 21 (2002) 1197-1209
    • (2002) EMBO J. , vol.21 , pp. 1197-1209
    • Iwahara, J.1    Iwahara, M.2    Daughdrill, G.W.3    Ford, J.4    Clubb, R.T.5
  • 32
    • 0034794444 scopus 로고    scopus 로고
    • Improving the accuracy of NMR structures of DNA by means of a database potential of mean force describing base-base positional interactions
    • Kuszewski J., Schwieters C., and Clore G.M. Improving the accuracy of NMR structures of DNA by means of a database potential of mean force describing base-base positional interactions. J. Am. Chem. Soc. 123 (2001) 3903-3918
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 3903-3918
    • Kuszewski, J.1    Schwieters, C.2    Clore, G.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.