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Volumn 76, Issue 4, 2009, Pages 787-793

Crystal structure of NusG N-terminal (NGN) domain from Methanocaldococcus jannaschii and its interaction with rpoE″

Author keywords

Archaea; Docking; Homodimer; RNA polymerase; Transcription factor

Indexed keywords

BACTERIAL PROTEIN; HOMODIMER; PROTEIN NUSG; PROTEIN RPOE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 68149163147     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22465     Document Type: Article
Times cited : (10)

References (28)
  • 1
    • 0026726828 scopus 로고
    • NusG, a new Escherichia coli elongation factor involved in transcriptional antitermination by the N protein of phage lambda
    • Li J, Horwitz R, McCracken S, Greenblatt J. NusG, a new Escherichia coli elongation factor involved in transcriptional antitermination by the N protein of phage lambda. J Biol Chem 1992;267: 6012-6019.
    • (1992) J Biol Chem , vol.267 , pp. 6012-6019
    • Li, J.1    Horwitz, R.2    McCracken, S.3    Greenblatt, J.4
  • 2
    • 0026527997 scopus 로고
    • Requirement for E. coli NusG protein in factor-dependent transcription termination
    • Sullivan SL, Gottesman ME. Requirement for E. coli NusG protein in factor-dependent transcription termination. Cell 1992;68:989-994.
    • (1992) Cell , vol.68 , pp. 989-994
    • Sullivan, S.L.1    Gottesman, M.E.2
  • 3
    • 0027944318 scopus 로고
    • A quaternary transcription termination complex. Reciprocal stabilization by Rho factor and Nus G protein
    • Nehrke KW, Platt T. A quaternary transcription termination complex. Reciprocal stabilization by Rho factor and Nus G protein J Mol Biol 1994;243:830-839.
    • (1994) J Mol Biol , vol.243 , pp. 830-839
    • Nehrke, K.W.1    Platt, T.2
  • 4
    • 0028905513 scopus 로고
    • Escherichia coli NusG protein stimulates transcription elongation rates in vivo and in vitro
    • Burova E, Hung SC, Sagitov V, Stitt BL, Gottesman ME. Escherichia coli NusG protein stimulates transcription elongation rates in vivo and in vitro. J Bacteriol 1995;177:1388-1392.
    • (1995) J Bacteriol , vol.177 , pp. 1388-1392
    • Burova, E.1    Hung, S.C.2    Sagitov, V.3    Stitt, B.L.4    Gottesman, M.E.5
  • 5
    • 0036713442 scopus 로고    scopus 로고
    • Novel domains and orthologues of eukaryotic transcription elongation factors
    • Ponting CP. Novel domains and orthologues of eukaryotic transcription elongation factors. Nucleic Acids Res 2002;30:3643-3652.
    • (2002) Nucleic Acids Res , vol.30 , pp. 3643-3652
    • Ponting, C.P.1
  • 8
    • 0032534814 scopus 로고    scopus 로고
    • Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro
    • DOI 10.1093/emboj/17.24.7395
    • Wada T, Takagi T, Yamaguchi Y, Watanabe D, Handa H. Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro. EMBO J 1998;17:7395-7403. (Pubitemid 29002707)
    • (1998) EMBO Journal , vol.17 , Issue.24 , pp. 7395-7403
    • Wada, T.1    Takagi, T.2    Yamaguchi, Y.3    Watanabe, D.4    Handa, H.5
  • 9
    • 0033515521 scopus 로고    scopus 로고
    • NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation
    • Yamaguchi Y, Takagi T, Wada T, Yano K, Furuya A, Sugimoto S, Hasegawa J, Handa H. NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation. Cell 1999;97:41-51. (Pubitemid 29165888)
    • (1999) Cell , vol.97 , Issue.1 , pp. 41-51
    • Yamaguchi, Y.1    Takagi, T.2    Wada, T.3    Yano, K.4    Furuya, A.5    Sugimoto, S.6    Hasegawa, J.7    Handa, H.8
  • 10
    • 34547563511 scopus 로고    scopus 로고
    • Properties of RNA polymerase II elongation complexes before and after the P-TEFb-mediated transition into productive elongation
    • DOI 10.1074/jbc.M702936200
    • Cheng B, Price DH. Properties of RNA polymerase II elongation complexes before and after the P-TEFb-mediated transition into productive elongation. J Biol Chem 2007;282:21901-21912. (Pubitemid 47195731)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.30 , pp. 21901-21912
    • Cheng, B.1    Price, D.H.2
  • 13
    • 55249117324 scopus 로고    scopus 로고
    • Core structure of the yeast spt4-spt5 complex: A conserved module for regulation of transcription elongation
    • Guo M, Xu F, Yamada J, Egelhofer T, Gao Y, Hartzog GA, Teng M, Niu L. Core structure of the yeast spt4-spt5 complex: a conserved module for regulation of transcription elongation. Structure 2008; 16:1649-1658.
    • (2008) Structure , vol.16 , pp. 1649-1658
    • Guo, M.1    Xu, F.2    Yamada, J.3    Egelhofer, T.4    Gao, Y.5    Hartzog, G.A.6    Teng, M.7    Niu, L.8
  • 14
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. Processing of x-ray diffraction data collected in oscillation mode Methods Enzymol 1997;276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 16
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 1997;53(Part 3):240-255.
    • (1997) Acta Crystallogr D Biol Crystallogr , vol.53 , Issue.PART 3 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 18
    • 0013461295 scopus 로고    scopus 로고
    • Macromolecular TLS refinement in REFMAC at moderate resolutions
    • Winn MD, Murshudov GN, Papiz MZ. Macromolecular TLS refinement in REFMAC at moderate resolutions. Methods Enzymol 2003; 374:300-321.
    • (2003) Methods Enzymol , vol.374 , pp. 300-321
    • Winn, M.D.1    Murshudov, G.N.2    Papiz, M.Z.3
  • 19
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM. PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 1993;26:283-291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 20
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • DOI 10.1093/bioinformatics/bti770
    • Arnold K, Bordoli L, Kopp J, Schwede T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 2006;22:195-201. (Pubitemid 43205406)
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 21
    • 0034193510 scopus 로고    scopus 로고
    • Protein docking using spherical polar fourier correlations
    • Ritchie DW, Kemp GJ. Protein docking using spherical polar fourier correlations. Proteins 2000;39:178-194.
    • (2000) Proteins , vol.39 , pp. 178-194
    • Ritchie, D.W.1    Kemp, G.J.2
  • 22
    • 0037009445 scopus 로고    scopus 로고
    • Crystal structures of transcription factor NusG in light of its nucleic acid- And protein-binding activities
    • DOI 10.1093/emboj/cdf455
    • Steiner T, Kaiser JT, Marinkovic S, Huber R, Wahl MC. Crystal structures of transcription factor NusG in light of its nucleic acidand protein-binding activities. EMBO J 2002;21:4641-4653. (Pubitemid 34984351)
    • (2002) EMBO Journal , vol.21 , Issue.17 , pp. 4641-4653
    • Steiner, T.1    Kaiser, J.T.2    Marinkovic, S.3    Huber, R.4    Wahl, M.C.5
  • 23
    • 0242515770 scopus 로고    scopus 로고
    • A spring-loaded state of NusG in its functional cycle is suggested by X-ray crystallography and supported by site-directed mutants
    • DOI 10.1021/bi0272508
    • Knowlton JR, Bubunenko M, Andrykovitch M, Guo W, Routzahn KM, Waugh DS, Court DL, Ji X. A spring-loaded state of NusG in its functional cycle is suggested by x-ray crystallography and supported by site-directed mutants. Biochemistry 2003;42:2275-2281. (Pubitemid 36255201)
    • (2003) Biochemistry , vol.42 , Issue.8 , pp. 2275-2281
    • Knowlton, J.R.1    Bubunenko, M.2    Andrykovitch, M.3    Guo, W.4    Routzahn, K.M.5    Waugh, D.S.6    Court, D.L.7    Ji, X.8
  • 24
    • 2642588196 scopus 로고    scopus 로고
    • Structural and sequence comparisons arising from the solution structure of the transcription elongation factor NusG from Thermus thermophilus
    • DOI 10.1002/prot.20054
    • Reay P, Yamasaki K, Terada T, Kuramitsu S, Shirouzu M, Yokoyama S. Structural and sequence comparisons arising from the solution structure of the transcription elongation factor NusG from Thermus thermophilus. Proteins 2004;56:40-51. (Pubitemid 38720837)
    • (2004) Proteins: Structure, Function and Genetics , vol.56 , Issue.1 , pp. 40-51
    • Reay, P.1    Yamasaki, K.2    Terada, T.3    Kuramitsu, S.4    Shirouzu, M.5    Yokoyama, S.6
  • 25
    • 20444410362 scopus 로고    scopus 로고
    • Identification of a structural element that is essential for two functions of transcription factor NusG
    • Richardson LV, Richardson JP. Identification of a structural element that is essential for two functions of transcription factor NusG. Biochim Biophys Acta 2005;1729:135-140.
    • (2005) Biochim Biophys Acta , vol.1729 , pp. 135-140
    • Richardson, L.V.1    Richardson, J.P.2
  • 26
    • 34147155174 scopus 로고    scopus 로고
    • Structural Basis for Converting a General Transcription Factor into an Operon-Specific Virulence Regulator
    • DOI 10.1016/j.molcel.2007.02.021, PII S1097276507001219
    • Belogurov GA, Vassylyeva MN, Svetlov V, Klyuyev S, Grishin NV, Vassylyev DG, Artsimovitch I. Structural basis for converting a general transcription factor into an operon-specific virulence regulator. Mol Cell 2007;26:117-129. (Pubitemid 46553793)
    • (2007) Molecular Cell , vol.26 , Issue.1 , pp. 117-129
    • Belogurov, G.A.1    Vassylyeva, M.N.2    Svetlov, V.3    Klyuyev, S.4    Grishin, N.V.5    Vassylyev, D.6    Artsimovitch, I.7
  • 28
    • 0032004953 scopus 로고    scopus 로고
    • Evidence that Spt4. Spt5, and Spt6 control transcription elongation by RNA polymerase II in Saccharomyces cerevisiae
    • Hartzog GA, Wada T, Handa H, Winston F. Evidence that Spt4. Spt5, and Spt6 control transcription elongation by RNA polymerase II in Saccharomyces cerevisiae. Genes Dev 1998;12:357-369.
    • (1998) Genes Dev , vol.12 , pp. 357-369
    • Hartzog, G.A.1    Wada, T.2    Handa, H.3    Winston, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.