메뉴 건너뛰기




Volumn 19, Issue 3, 2009, Pages 294-299

A movie of the RNA polymerase nucleotide addition cycle

Author keywords

[No Author keywords available]

Indexed keywords

DNA; MESSENGER RNA; NUCLEOSIDE TRIPHOSPHATE; NUCLEOTIDE; RNA; RNA POLYMERASE;

EID: 66549126163     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2009.04.005     Document Type: Review
Times cited : (73)

References (24)
  • 2
    • 0035827332 scopus 로고    scopus 로고
    • Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 A resolution
    • Gnatt A.L., Cramer P., Fu J., Bushnell D.A., and Kornberg R.D. Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 A resolution. Science 292 (2001) 1876-1882
    • (2001) Science , vol.292 , pp. 1876-1882
    • Gnatt, A.L.1    Cramer, P.2    Fu, J.3    Bushnell, D.A.4    Kornberg, R.D.5
  • 3
    • 10944232674 scopus 로고    scopus 로고
    • Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS
    • Kettenberger H., Armache K.-J., and Cramer P. Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS. Mol Cell 16 (2004) 955-965
    • (2004) Mol Cell , vol.16 , pp. 955-965
    • Kettenberger, H.1    Armache, K.-J.2    Cramer, P.3
  • 4
    • 1142310578 scopus 로고    scopus 로고
    • Structural basis of transcription: separation of RNA from DNA by RNA polymerase II
    • Westover K.D., Bushnell D.A., and Kornberg R.D. Structural basis of transcription: separation of RNA from DNA by RNA polymerase II. Science 303 (2004) 1014-1016
    • (2004) Science , vol.303 , pp. 1014-1016
    • Westover, K.D.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 5
    • 8344234112 scopus 로고    scopus 로고
    • Structural basis of transcription: nucleotide selection by rotation in the RNA polymerase II active center
    • Westover K.D., Bushnell D.A., and Kornberg R.D. Structural basis of transcription: nucleotide selection by rotation in the RNA polymerase II active center. Cell 119 (2004) 481-489
    • (2004) Cell , vol.119 , pp. 481-489
    • Westover, K.D.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 6
    • 33751235874 scopus 로고    scopus 로고
    • Structural basis of transcription: role of the trigger loop in substrate specificity and catalysis
    • The structure of a core yeast Pol II EC with bound NTP substrate provides a view of the insertion state and reveals a closed trigger loop that stacks against the substrate.
    • Wang D., Bushnell D.A., Westover K.D., Kaplan C.D., and Kornberg R.D. Structural basis of transcription: role of the trigger loop in substrate specificity and catalysis. Cell 127 (2006) 941-954. The structure of a core yeast Pol II EC with bound NTP substrate provides a view of the insertion state and reveals a closed trigger loop that stacks against the substrate.
    • (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
  • 8
    • 34447513771 scopus 로고    scopus 로고
    • Structural basis for substrate loading in bacterial RNA polymerase
    • Structures of the bacterial EC bound to NTP analogs are reported in the presence and in the absence of the antibiotic streptolydigin. In the absence of the antibiotic, NTP binds to the insertion site and the trigger loop is closed. In the presence of the antibiotic, NTP binds in an overlapping site of the pre-insertion state and the trigger loop is partially open. Together with biochemical data, the results support the two-step mechanism of substrate loading.
    • Vassylyev D.G., Vassylyeva M.N., Zhang J., Palangat M., Artsimovitch I., and Landick R. Structural basis for substrate loading in bacterial RNA polymerase. Nature 448 (2007) 163-168. Structures of the bacterial EC bound to NTP analogs are reported in the presence and in the absence of the antibiotic streptolydigin. In the absence of the antibiotic, NTP binds to the insertion site and the trigger loop is closed. In the presence of the antibiotic, NTP binds in an overlapping site of the pre-insertion state and the trigger loop is partially open. Together with biochemical data, the results support the two-step mechanism of substrate loading.
    • (2007) Nature , vol.448 , pp. 163-168
    • Vassylyev, D.G.1    Vassylyeva, M.N.2    Zhang, J.3    Palangat, M.4    Artsimovitch, I.5    Landick, R.6
  • 9
    • 0035827346 scopus 로고    scopus 로고
    • Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution
    • Cramer P., Bushnell D.A., and Kornberg R.D. Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution. Science 292 (2001) 1863-1876
    • (2001) Science , vol.292 , pp. 1863-1876
    • Cramer, P.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 10
    • 0032518374 scopus 로고    scopus 로고
    • A mechanism for all polymerases [news; comment]
    • Steitz T.A. A mechanism for all polymerases [news; comment]. Nature 391 (1998) 231-232
    • (1998) Nature , vol.391 , pp. 231-232
    • Steitz, T.A.1
  • 11
    • 0033578701 scopus 로고    scopus 로고
    • Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution
    • Zhang G., Campbell E.A., Minakhin L., Richter C., Severinov K., and Darst S.A. Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution. Cell 98 (1999) 811-824
    • (1999) Cell , vol.98 , pp. 811-824
    • Zhang, G.1    Campbell, E.A.2    Minakhin, L.3    Richter, C.4    Severinov, K.5    Darst, S.A.6
  • 15
    • 57249108333 scopus 로고    scopus 로고
    • Bridge helix and trigger loop perturbations generate superactive RNA polymerases
    • Tan L., Wiesler S., Trzaska D., Carney H.C., and Weinzierl R.O. Bridge helix and trigger loop perturbations generate superactive RNA polymerases. J Biol 7 (2008) 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
  • 17
    • 49449102926 scopus 로고    scopus 로고
    • Structural basis of transcription inhibition by alpha-amanitin and implications for RNA polymerase II translocation
    • Crystals are reported that apparently preserve the equilibrium of the pre-translocation and post-translocation states of the complete yeast Pol II EC. Soaking of the crystals with the mushroom toxin a-amanitin trapped the EC in a previously unobserved state that is intermediary between the pre-translocation and the post-translocation states. The next DNA template base is seen in a pretemplating position above the bridge helix. The central bridge helix is shifted and apparently stabilized by the trigger loop, which forms a wedge below the bridge helix.
    • Brueckner F., and Cramer P. Structural basis of transcription inhibition by alpha-amanitin and implications for RNA polymerase II translocation. Nat Struct Mol Biol 15 (2008) 811-818. Crystals are reported that apparently preserve the equilibrium of the pre-translocation and post-translocation states of the complete yeast Pol II EC. Soaking of the crystals with the mushroom toxin a-amanitin trapped the EC in a previously unobserved state that is intermediary between the pre-translocation and the post-translocation states. The next DNA template base is seen in a pretemplating position above the bridge helix. The central bridge helix is shifted and apparently stabilized by the trigger loop, which forms a wedge below the bridge helix.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 811-818
    • Brueckner, F.1    Cramer, P.2
  • 19
    • 1342313235 scopus 로고    scopus 로고
    • The structural mechanism of translocation and helicase activity in t7 RNA polymerase
    • Yin Y.W., and Steitz T.A. The structural mechanism of translocation and helicase activity in t7 RNA polymerase. Cell 116 (2004) 393-404
    • (2004) Cell , vol.116 , pp. 393-404
    • Yin, Y.W.1    Steitz, T.A.2
  • 20
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60 (2004) 2126-2132
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 21
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semiautomated software for high-resolution single-particle reconstructions
    • Ludtke S.J., Baldwin P.R., and Chiu W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J Struct Biol 128 (1999) 82-97
    • (1999) J Struct Biol , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 23
    • 12944320326 scopus 로고    scopus 로고
    • Machinations of a maxwellian demon
    • Sousa R. Machinations of a maxwellian demon. Cell 120 (2005) 155-156
    • (2005) Cell , vol.120 , pp. 155-156
    • Sousa, R.1
  • 24
    • 1642417611 scopus 로고    scopus 로고
    • Active-site dynamics in RNA polymerases
    • Landick R. Active-site dynamics in RNA polymerases. Cell 116 (2004) 351-353
    • (2004) Cell , vol.116 , pp. 351-353
    • Landick, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.