메뉴 건너뛰기




Volumn 106, Issue 45, 2009, Pages 18942-18947

Allosteric control of catalysis by the F loop of RNA polymerase

Author keywords

Nucleotide addition; RNA cleavage; Streptolydigin; Temperature adaptation; Transcription

Indexed keywords

NUCLEOTIDE; RNA POLYMERASE; STREPTOLYDIGIN;

EID: 73149106601     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0905402106     Document Type: Article
Times cited : (37)

References (32)
  • 2
    • 10944232674 scopus 로고    scopus 로고
    • Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS
    • Kettenberger H, Armache KJ, Cramer P (2004) Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS. Mol Cell 16:955-965.
    • (2004) Mol Cell , vol.16 , pp. 955-965
    • Kettenberger, H.1    Armache, K.J.2    Cramer, P.3
  • 3
    • 34447513771 scopus 로고    scopus 로고
    • Structural basis for substrate loading in bacterial RNA polymerase
    • Vassylyev DG, et al. (2007) Structural basis for substrate loading in bacterial RNA polymerase. Nature 448:163-168.
    • (2007) Nature , vol.448 , pp. 163-168
    • Vassylyev, D.G.1
  • 4
    • 33751235874 scopus 로고    scopus 로고
    • Structural basis of transcription: Role of the trigger loop in substrate specificity and catalysis
    • Wang D, Bushnell DA, Westover KD, Kaplan CD, Kornberg RD (2006) Structural basis of transcription: Role of the trigger loop in substrate specificity and catalysis. Cell 127:941-954.
    • (2006) Cell , vol.127 , pp. 941-954
    • Wang, D.1    Bushnell, D.A.2    Westover, K.D.3    Kaplan, C.D.4    Kornberg, R.D.5
  • 5
    • 49449102926 scopus 로고    scopus 로고
    • Structural basis of transcription inhibition by alpha-amanitin and implications for RNA polymerase II translocation
    • Brueckner F, Cramer P (2008) Structural basis of transcription inhibition by alpha-amanitin and implications for RNA polymerase II translocation. Nat Struct Mol Biol 15:811-818.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 811-818
    • Brueckner, F.1    Cramer, P.2
  • 6
    • 0033578701 scopus 로고    scopus 로고
    • Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution
    • Zhang G, et al. (1999) Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution. Cell 98:811-824.
    • (1999) Cell , vol.98 , pp. 811-824
    • Zhang, G.1
  • 7
    • 0035827346 scopus 로고    scopus 로고
    • Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution
    • Cramer P, Bushnell DA, Kornberg RD (2001) Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution. Science 292:1863-1876.
    • (2001) Science , vol.292 , pp. 1863-1876
    • Cramer, P.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 8
    • 0037071844 scopus 로고    scopus 로고
    • Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 A resolution
    • Vassylyev DG, et al. (2002) Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 A resolution. Nature 417:712-719.
    • (2002) Nature , vol.417 , pp. 712-719
    • Vassylyev, D.G.1
  • 9
    • 34547204502 scopus 로고    scopus 로고
    • Acentral role of theRNApolymerase trigger loop in active-site rearrangement during transcriptional pausing
    • ToulokhonovI,ZhangJ, PalangatM,LandickR(2007)Acentral role of theRNApolymerase trigger loop in active-site rearrangement during transcriptional pausing. Mol Cell 27:406-419.
    • (2007) Mol Cell , vol.27 , pp. 406-419
    • Toulokhonov, I.1    Zhang, J.2    Palangat, M.3    Landick, R.4
  • 10
    • 12944324227 scopus 로고    scopus 로고
    • A ratchet mechanism of transcription elongation and its control
    • Bar-Nahum G, et al. (2005) A ratchet mechanism of transcription elongation and its control. Cell 120:183-193.
    • (2005) Cell , vol.120 , pp. 183-193
    • Bar-Nahum, G.1
  • 11
    • 0036753435 scopus 로고    scopus 로고
    • Swing-gate model of nucleotide entry into the RNA polymerase active center
    • Epshtein V, et al. (2002) Swing-gate model of nucleotide entry into the RNA polymerase active center. Mol Cell 10:623-634.
    • (2002) Mol Cell , vol.10 , pp. 623-634
    • Epshtein, V.1
  • 12
    • 44449103640 scopus 로고    scopus 로고
    • The RNA polymerase II trigger loop functions in substrate selection and is directly targeted by alpha-amanitin
    • Kaplan CD, Larsson KM, Kornberg RD (2008) The RNA polymerase II trigger loop functions in substrate selection and is directly targeted by alpha-amanitin. Mol Cell 30:547-556.
    • (2008) Mol Cell , vol.30 , pp. 547-556
    • Kaplan, C.D.1    Larsson, K.M.2    Kornberg, R.D.3
  • 14
    • 57249108333 scopus 로고    scopus 로고
    • Bridge helix and trigger loop perturbations generate superactive RNA polymerases
    • Tan L, Wiesler S, Trzaska D, Carney HC, Weinzierl RO (2008) Bridge helix and trigger loop perturbations generate superactive RNA polymerases. J Biol 7:40.
    • (2008) J Biol , vol.7 , pp. 40
    • Tan, L.1    Wiesler, S.2    Trzaska, D.3    Carney, H.C.4    Weinzierl, R.O.5
  • 15
    • 24044497229 scopus 로고    scopus 로고
    • Structural basis of transcription inhibition by antibiotic streptolydigin
    • Temiakov D, et al. (2005) Structural basis of transcription inhibition by antibiotic streptolydigin. Mol Cell 19:655-666.
    • (2005) Mol Cell , vol.19 , pp. 655-666
    • Temiakov, D.1
  • 16
    • 0037022279 scopus 로고    scopus 로고
    • Structural basis of transcription: Alphaamanitin-RNA polymerase II cocrystal at 2.8Aresolution
    • Bushnell DA, Cramer P, Kornberg RD (2002) Structural basis of transcription: alphaamanitin-RNA polymerase II cocrystal at 2.8Aresolution. Proc Natl Acad Sci USA 99:1218-1222.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1218-1222
    • Bushnell, D.A.1    Cramer, P.2    Kornberg, R.D.3
  • 17
    • 0037543997 scopus 로고    scopus 로고
    • Unified two-metal mechanism of RNA synthesis and degradation by RNA polymerase
    • Sosunov V, et al. (2003) Unified two-metal mechanism of RNA synthesis and degradation by RNA polymerase. EMBO J 22:2234-2244.
    • (2003) EMBO J , vol.22 , pp. 2234-2244
    • Sosunov, V.1
  • 18
    • 22844436748 scopus 로고    scopus 로고
    • The involvement of the aspartate triad of the active center in all catalytic activities of multisubunit RNA polymerase
    • Sosunov V, et al. (2005) The involvement of the aspartate triad of the active center in all catalytic activities of multisubunit RNA polymerase. Nucleic Acids Res 33:4202-4211.
    • (2005) Nucleic Acids Res , vol.33 , pp. 4202-4211
    • Sosunov, V.1
  • 19
    • 0034700292 scopus 로고    scopus 로고
    • Purification and initial characterization of RNA polymerase from Thermus thermophilus strain HB8
    • Xue Y, Hogan BP, Erie DA (2000) Purification and initial characterization of RNA polymerase from Thermus thermophilus strain HB8. Biochemistry 39:14356-14362.
    • (2000) Biochemistry , vol.39 , pp. 14356-14362
    • Xue, Y.1    Hogan, B.P.2    Erie, D.A.3
  • 20
    • 0035191283 scopus 로고    scopus 로고
    • Recombinant Thermus aquaticus RNA polymerase, a new tool for structure- based analysis of transcription
    • Minakhin L, Nechaev S, Campbell EA, Severinov K (2001) Recombinant Thermus aquaticus RNA polymerase, a new tool for structure- based analysis of transcription. J Bacteriol 183:71-76.
    • (2001) J Bacteriol , vol.183 , pp. 71-76
    • Minakhin, L.1    Nechaev, S.2    Campbell, E.A.3    Severinov, K.4
  • 22
    • 0034973280 scopus 로고    scopus 로고
    • Review: Protein function at thermal extremes: Balancing stability and flexibility
    • Fields PA (2001) Review: Protein function at thermal extremes: Balancing stability and flexibility. Comp Biochem Physiol A Mol Integr Physiol 129:417-431.
    • (2001) Comp Biochem Physiol A Mol Integr Physiol , vol.129 , pp. 417-431
    • Fields, P.A.1
  • 23
    • 33646177461 scopus 로고    scopus 로고
    • Recombinant Thermus aquaticus RNA polymerase for structural studies
    • Kuznedelov K, et al. (2006) Recombinant Thermus aquaticus RNA polymerase for structural studies. J Mol Biol 359:110-121.
    • (2006) J Mol Biol , vol.359 , pp. 110-121
    • Kuznedelov, K.1
  • 24
    • 0034725870 scopus 로고    scopus 로고
    • A structural model of transcription elongation
    • Korzheva N, et al. (2000) A structural model of transcription elongation. Science 289:619-625.
    • (2000) Science , vol.289 , pp. 619-625
    • Korzheva, N.1
  • 25
    • 0346243938 scopus 로고    scopus 로고
    • Transcript cleavage factorsGreAandGreB act as transient catalytic components of RNA polymerase
    • Laptenko O, Lee J, Lomakin I, Borukhov S (2003) Transcript cleavage factorsGreAandGreB act as transient catalytic components of RNA polymerase. EMBO J 22:6322-6334.
    • (2003) EMBO J , vol.22 , pp. 6322-6334
    • Laptenko, O.1    Lee, J.2    Lomakin, I.3    Borukhov, S.4
  • 26
    • 0347994909 scopus 로고    scopus 로고
    • Donation of catalytic residues toRNApolymerase active center by transcription factor Gre
    • Sosunova E, et al. (2003) Donation of catalytic residues toRNApolymerase active center by transcription factor Gre. Proc Natl Acad Sci USA 100:15469-15474.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 15469-15474
    • Sosunova, E.1
  • 27
    • 0043244877 scopus 로고    scopus 로고
    • Structure and function of the transcription elongation factor GreB bound to bacterial RNA polymerase
    • Opalka N, et al. (2003) Structure and function of the transcription elongation factor GreB bound to bacterial RNA polymerase. Cell 114:335-345.
    • (2003) Cell , vol.114 , pp. 335-345
    • Opalka, N.1
  • 28
    • 35748963229 scopus 로고    scopus 로고
    • The carboxy-terminal coiled-coil of the RNA polymerase beta′-subunit is the main binding site for Gre factors
    • Vassylyeva MN, et al. (2007) The carboxy-terminal coiled-coil of the RNA polymerase beta′-subunit is the main binding site for Gre factors. EMBO Rep 8:1038-1043.
    • (2007) EMBO Rep , vol.8 , pp. 1038-1043
    • Vassylyeva, M.N.1
  • 29
    • 33746634704 scopus 로고    scopus 로고
    • Transcript-assisted transcriptional proofreading
    • Zenkin N, Yuzenkova Y, Severinov K (2006) Transcript-assisted transcriptional proofreading. Science 313:518-520.
    • (2006) Science , vol.313 , pp. 518-520
    • Zenkin, N.1    Yuzenkova, Y.2    Severinov, K.3
  • 30
    • 44449094019 scopus 로고    scopus 로고
    • Transient reversal ofRNApolymerase II active site closing controls fidelity of transcription elongation
    • Kireeva ML, et al. (2008) Transient reversal ofRNApolymerase II active site closing controls fidelity of transcription elongation. Mol Cell 30:557-566.
    • (2008) Mol Cell , vol.30 , pp. 557-566
    • Kireeva, M.L.1
  • 31
    • 0142147268 scopus 로고    scopus 로고
    • A new class of bacterial RNA polymerase inhibitor affects nucleotide addition
    • Artsimovitch I, Chu C, Lynch AS, Landick R (2003) A new class of bacterial RNA polymerase inhibitor affects nucleotide addition. Science 302:650-654.
    • (2003) Science , vol.302 , pp. 650-654
    • Artsimovitch, I.1    Chu, C.2    Lynch, A.S.3    Landick, R.4
  • 32
    • 66349138227 scopus 로고    scopus 로고
    • Structural basis of transcription: BacktrackedRNApolymerase II at 3.4 angstrom resolution
    • WangD, et al. (2009) Structural basis of transcription: BacktrackedRNApolymerase II at 3.4 angstrom resolution. Science 324:1203-1206.
    • (2009) Science , vol.324 , pp. 1203-1206
    • WangD1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.