메뉴 건너뛰기




Volumn 14, Issue 1, 2004, Pages 4-9

The structural basis of the transition from initiation to elongation phases of transcription, as well as translocation and strand separation, by T7 RNA polymerase

Author keywords

DNA polymerase; DNAP; NTP; Nucleoside 5 triphosphate; PPi; Pyrophosphate; RNA polymerase; RNAP

Indexed keywords

DOUBLE STRANDED DNA; RNA POLYMERASE;

EID: 1342302799     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2004.01.006     Document Type: Review
Times cited : (52)

References (18)
  • 2
    • 0032584643 scopus 로고    scopus 로고
    • An integrated model of the transcription complex in elongation, termination, and editing
    • von Hippel P.H. An integrated model of the transcription complex in elongation, termination, and editing. Science. 281:1998;660-665.
    • (1998) Science , vol.281 , pp. 660-665
    • Von Hippel, P.H.1
  • 3
    • 0019319452 scopus 로고
    • Cycling of ribonucleic acid polymerase to produce oligonucleotides during initiation in vitro at the lac UV5 promoter
    • Carpousis A.J., Gralla J.D. Cycling of ribonucleic acid polymerase to produce oligonucleotides during initiation in vitro at the lac UV5 promoter. Biochemistry. 19:1980;3245-3253.
    • (1980) Biochemistry , vol.19 , pp. 3245-3253
    • Carpousis, A.J.1    Gralla, J.D.2
  • 4
    • 0023924749 scopus 로고
    • Processivity in early stages of transcription by T7 RNA polymerase
    • Martin C.T., Muller D.K., Coleman J.E. Processivity in early stages of transcription by T7 RNA polymerase. Biochemistry. 27:1988;3966-3974.
    • (1988) Biochemistry , vol.27 , pp. 3966-3974
    • Martin, C.T.1    Muller, D.K.2    Coleman, J.E.3
  • 5
    • 0033579380 scopus 로고    scopus 로고
    • Structure of a transcribing T7 RNA polymerase initiation complex
    • Cheetham G.M.T., Steitz T.A. Structure of a transcribing T7 RNA polymerase initiation complex. Science. 286:1999;2305-2309.
    • (1999) Science , vol.286 , pp. 2305-2309
    • Cheetham, G.M.T.1    Steitz, T.A.2
  • 6
    • 0037112082 scopus 로고    scopus 로고
    • Structural basis for the transition from initiation to elongation transcription in T7 RNA polymerase
    • This paper compares structures of the initiation complex [5] with that of the elongation complex, and provides the basis for understanding promoter clearance and the processivity of the elongation complex.
    • Yin Y.W., Steitz T.A. Structural basis for the transition from initiation to elongation transcription in T7 RNA polymerase. Science. 298:2002;1387-1395 This paper compares structures of the initiation complex [5] with that of the elongation complex, and provides the basis for understanding promoter clearance and the processivity of the elongation complex.
    • (2002) Science , vol.298 , pp. 1387-1395
    • Yin, Y.W.1    Steitz, T.A.2
  • 7
    • 0037038361 scopus 로고    scopus 로고
    • Structure of a T7 RNA polymerase elongation complex at 2.9 Å resolution
    • The structure of an elongation complex is presented and its relationship to the initiation complex [5] discussed.
    • Tahirov T.H., Temiakov D., Patlan A.M., McAllister W.T., Vassylyev D.G., Yokoyama S. Structure of a T7 RNA polymerase elongation complex at 2.9 Å resolution. Nature. 420:2002;43-50 The structure of an elongation complex is presented and its relationship to the initiation complex [5] discussed.
    • (2002) Nature , vol.420 , pp. 43-50
    • Tahirov, T.H.1    Temiakov, D.2    Patlan, A.M.3    McAllister, W.T.4    Vassylyev, D.G.5    Yokoyama, S.6
  • 8
    • 0014670824 scopus 로고
    • Azotobacter vinelandii ribonucleic acid polymerase. 8. Pyrophosphate exchange
    • Krakow J.S., Fronk E. Azotobacter vinelandii ribonucleic acid polymerase. 8. Pyrophosphate exchange. J. Biol. Chem. 244:1969;5988-5993.
    • (1969) J. Biol. Chem. , vol.244 , pp. 5988-5993
    • Krakow, J.S.1    Fronk, E.2
  • 9
    • 1342313235 scopus 로고    scopus 로고
    • The structural mechanism of translocation and helicase activity in T7 RNA polymerase
    • in press
    • Yin YW, Steitz TA: The structural mechanism of translocation and helicase activity in T7 RNA polymerase. Cell 2004, in press.
    • (2004) Cell
    • Yin, Y.W.1    Steitz, T.A.2
  • 10
    • 0031046587 scopus 로고    scopus 로고
    • A mutant T7 RNA polymerase that is defective in RNA binding and blocked in the early stages of transcription
    • He B., Rong M., Durbin W.T., McAllister J. A mutant T7 RNA polymerase that is defective in RNA binding and blocked in the early stages of transcription. J. Mol. Biol. 265:1997;275-288.
    • (1997) J. Mol. Biol. , vol.265 , pp. 275-288
    • He, B.1    Rong, M.2    Durbin, W.T.3    McAllister, J.4
  • 11
    • 0027772958 scopus 로고
    • Sliding clamps of DNA polymerases
    • Kuriyan J., O'Donnell M. Sliding clamps of DNA polymerases. J. Mol. Biol. 234:1993;915-925.
    • (1993) J. Mol. Biol. , vol.234 , pp. 915-925
    • Kuriyan, J.1    O'Donnell, M.2
  • 12
    • 0035827332 scopus 로고    scopus 로고
    • Structural basis of transcription: An RNA polymerase II elongation complex at 3.3 Å resolution
    • The structure of yeast RNA polymerase II bound to an elongation phase substrate containing downstream duplex DNA and RNA paired with a template extension is described. A proposal for translocation is presented.
    • Gnatt A.L., Cramer P., Fu J., Bushnell D.A., Kornberg R.D. Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 Å resolution. Science. 292:2001;1876-1882 The structure of yeast RNA polymerase II bound to an elongation phase substrate containing downstream duplex DNA and RNA paired with a template extension is described. A proposal for translocation is presented.
    • (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
  • 13
    • 0035827346 scopus 로고    scopus 로고
    • Structural basis of transcription: RNA polymerase II at 2.8 Angstrom resolution
    • The structure of an elongation complex of yeast RNA polymerase II is presented.
    • Cramer P., Bushnell D.A., Kornberg R.D. Structural basis of transcription: RNA polymerase II at 2.8 Angstrom resolution. Science. 292:2001;1863-1876 The structure of an elongation complex of yeast RNA polymerase II is presented.
    • (2001) Science , vol.292 , pp. 1863-1876
    • Cramer, P.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 14
    • 0033578701 scopus 로고    scopus 로고
    • Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 Å resolution
    • Zhang G., Campbell E.A., Minakhin L., Richter C., Severinov K., Darst S.A. Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 Å 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
    • 0037123602 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: An RNA polymerase holoenzyme-DNA complex
    • Murakami K.S., Masuda S., Campbell E.A., Mussin O., 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    Mussin, O.4    Darst, S.A.5
  • 17
    • 0029817866 scopus 로고    scopus 로고
    • Crystal structures of human DNA polymerase beta complexed with DNA: Implications for catalytic mechanism, processivity and fidelity
    • Pelletier H., Sawaya M.R., Wolfie W., Wilson S.H., Kraut J. Crystal structures of human DNA polymerase beta complexed with DNA: implications for catalytic mechanism, processivity and fidelity. Biochemistry. 35:1996;12742-12761.
    • (1996) Biochemistry , vol.35 , pp. 12742-12761
    • Pelletier, H.1    Sawaya, M.R.2    Wolfie, W.3    Wilson, S.H.4    Kraut, J.5
  • 18
    • 0037388383 scopus 로고    scopus 로고
    • Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations
    • Johnson S.J., Taylor J.S., Beese L.S. Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations. Proc. Natl. Acad. Sci. U.S.A. 100:2003;3895-3900.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3895-3900
    • Johnson, S.J.1    Taylor, J.S.2    Beese, L.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.