메뉴 건너뛰기




Volumn 37, Issue 17, 2009, Pages 5803-5809

Nano positioning system reveals the course of upstream and nontemplate DNA within the RNA polymerase ii elongation complex

Author keywords

[No Author keywords available]

Indexed keywords

DNA; RNA POLYMERASE II;

EID: 73049092277     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkp601     Document Type: Article
Times cited : (82)

References (40)
  • 1
    • 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. (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
  • 2
    • 14844290215 scopus 로고    scopus 로고
    • Structures of complete RNA polymerase II and its subcomplex Rpb4/7
    • Armache, K.-J., Mitterweger, S., Meinhart, A. and Cramer, P. (2005) Structures of complete RNA polymerase II and its subcomplex Rpb4/7. J. Biol. Chem., 280, 7131-7134.
    • (2005) J. Biol. Chem. , vol.280 , pp. 7131-7134
    • Armache, K.-J.1    Mitterweger, S.2    Meinhart, A.3    Cramer, P.4
  • 3
    • 0037832543 scopus 로고    scopus 로고
    • Complete RNA polymerase II at 4.1 Å resolution: implications for the initiation of transcription
    • Bushnell, D.A. and Kornberg, R.D. (2003) Complete RNA polymerase II at 4.1 Å resolution: implications for the initiation of transcription. Proc. Natl Acad. Sci. USA, 100, 6969-6972.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 6969-6972
    • Bushnell, D.A.1    Kornberg, R.D.2
  • 4
    • 0037495037 scopus 로고    scopus 로고
    • Architecture of the initiation-competent 12-subunit RNA polymerase II
    • Armache, K.-J., Kettenberger, H. and Cramer, P. (2003) Architecture of the initiation-competent 12-subunit RNA polymerase II. Proc. Natl Acad. Sci. USA, 100, 6964-6968.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 6964-6968
    • Armache, K.-J.1    Kettenberger, H.2    Cramer, P.3
  • 5
    • 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. (2001) Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 A resolution. Science, 292, 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
  • 6
    • 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. (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
  • 7
    • 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. (2004) Structural basis of transcription: separation of RNA from DNA by RNA polymerase II. Science, 303, 1014-1016.
    • (2004) Science , vol.303 , pp. 1014-1016
    • Westover, K.D.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 8
    • 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. (2004) Structural basis of transcription: nucleotide selection by rotation in the RNA polymerase II active center. Cell, 119, 481-489.
    • (2004) Cell , vol.119 , pp. 481-489
    • Westover, K.D.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 9
    • 49449102926 scopus 로고    scopus 로고
    • Structural basis of transcription inhibition by [alpha]-amanitin and implications for RNA polymerase II translocation
    • Brueckner, F. and 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
  • 10
    • 0029987587 scopus 로고    scopus 로고
    • Probing the interaction between two single molecules: fluorescence resonance energy transfer between a single donor and a single acceptor
    • Ha, T., Enderle, T., Ogletree, D.F., Chemla, D.S., Selvin, P.R. and Weiss, S. (1996) Probing the interaction between two single molecules: fluorescence resonance energy transfer between a single donor and a single acceptor. Proc. Natl Acad. Sci. USA, 93, 6264-6268.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 6264-6268
    • Ha, T.1    Enderle, T.2    Ogletree, D.F.3    Chemla, D.S.4    Selvin, P.R.5    Weiss, S.6
  • 11
    • 50649121477 scopus 로고    scopus 로고
    • Advances in single-molecule fluorescence methods for molecular biology
    • Joo, C., Balci, H., Ishitsuka, Y., Buranachai, C. and Ha, T. (2008) Advances in single-molecule fluorescence methods for molecular biology. Annu. Rev. Biochem., 77, 51-76.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 51-76
    • Joo, C.1    Balci, H.2    Ishitsuka, Y.3    Buranachai, C.4    Ha, T.5
  • 14
    • 15444372003 scopus 로고    scopus 로고
    • Distance-restrained docking of rifampicin and rifamycin SV to RNA polymerase using systematic FRET measurements: developing benchmarks of model quality and reliability
    • Knight, J.L., Mekler, V., Mukhopadhyay, J., Ebright, R.H. and Levy, R.M. (2005) Distance-restrained docking of rifampicin and rifamycin SV to RNA polymerase using systematic FRET measurements: developing benchmarks of model quality and reliability. Biophys. J., 88, 925-938.
    • (2005) Biophys. J. , vol.88 , pp. 925-938
    • Knight, J.L.1    Mekler, V.2    Mukhopadhyay, J.3    Ebright, R.H.4    Levy, R.M.5
  • 15
    • 0742324525 scopus 로고    scopus 로고
    • DNA-binding orientation and domain conformation of the E. coli rep helicase monomer bound to a partial duplex junction: single-molecule studies of fluorescently labeled enzymes
    • Rasnik, I., Myong, S., Cheng, W., Lohman, T.M. and Ha, T. (2004) DNA-binding orientation and domain conformation of the E. coli rep helicase monomer bound to a partial duplex junction: single-molecule studies of fluorescently labeled enzymes. J. Mol. Biol., 336, 395-408.
    • (2004) J. Mol. Biol. , vol.336 , pp. 395-408
    • Rasnik, I.1    Myong, S.2    Cheng, W.3    Lohman, T.M.4    Ha, T.5
  • 18
    • 58549106435 scopus 로고    scopus 로고
    • Mapping RNA exit channel on transcribing RNA polymerase II by FRET analysis
    • Chen, C.Y., Chang, C.C., Yen, C.F., Chiu, M.T. and Chang, W.H. (2009) Mapping RNA exit channel on transcribing RNA polymerase II by FRET analysis. Proc. Natl Acad. Sci. USA, 106, 127-132.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 127-132
    • Chen, C.Y.1    Chang, C.C.2    Yen, C.F.3    Chiu, M.T.4    Chang, W.H.5
  • 19
    • 0032113494 scopus 로고    scopus 로고
    • Crutial role of the RNA:DNA hybrid in the processivity of transcription
    • Sidorenkov, I., Komissarova, N. and Kashlev, M. (1998) Crutial role of the RNA:DNA hybrid in the processivity of transcription. Mol. Cell, 2, 55-64.
    • (1998) Mol. Cell. , vol.2 , pp. 55-64
    • Sidorenkov, I.1    Komissarova, N.2    Kashlev, M.3
  • 20
    • 0034595503 scopus 로고    scopus 로고
    • Overextended RNA:DNA hybrid as a negative regulator of RNA polymerase II processivity
    • Kireeva, M.L., Komissarova, N. and Kashlev, M. (2000) Overextended RNA:DNA hybrid as a negative regulator of RNA polymerase II processivity. J. Mol. Biol., 299, 325-335.
    • (2000) J. Mol. Biol. , vol.299 , pp. 325-335
    • Kireeva, M.L.1    Komissarova, N.2    Kashlev, M.3
  • 21
    • 0034051171 scopus 로고    scopus 로고
    • The 8-nucleotide-long RNA:DNA hybrid is a primary stability determinant of the RNA polymerase II elongation complex
    • Kireeva, M.L., Komissarova, N., Waugh, D.S. and Kashlev, M. (2000) The 8-nucleotide-long RNA:DNA hybrid is a primary stability determinant of the RNA polymerase II elongation complex. J. Biol. Chem., 275, 6530-6536.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6530-6536
    • Kireeva, M.L.1    Komissarova, N.2    Waugh, D.S.3    Kashlev, M.4
  • 22
    • 0031058485 scopus 로고    scopus 로고
    • Nuclease cleavage of the upstream half of the nontemplate strand DNA in an Escherichia coli transcription elongation complex causes upstream translocation and transcriptional arrest
    • Wang, D. and Landick, R. (1997) Nuclease cleavage of the upstream half of the nontemplate strand DNA in an Escherichia coli transcription elongation complex causes upstream translocation and transcriptional arrest. J. Biol. Chem., 272, 5989-5994.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5989-5994
    • Wang, D.1    Landick, R.2
  • 23
    • 0028066790 scopus 로고
    • Discontinuous mechanism of transcription elongation
    • Nudler, E., Goldfarb, A. and Kashlev, M. (1994) Discontinuous mechanism of transcription elongation. Science, 265, 793-796.
    • (1994) Science , vol.265 , pp. 793-796
    • Nudler, E.1    Goldfarb, A.2    Kashlev, M.3
  • 24
    • 38949110771 scopus 로고    scopus 로고
    • The elongation factor RfaH and the initiation factor s bind to the same site on the transcription elongation complex
    • Sevostyanova, A., Svetlov, V., Vassylyev, D.G. and Artsimovitch, I. (2008) The elongation factor RfaH and the initiation factor s bind to the same site on the transcription elongation complex. Proc. Natl Acad. Sci. USA, 105, 865-870.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 865-870
    • Sevostyanova, A.1    Svetlov, V.2    Vassylyev, D.G.3    Artsimovitch, I.4
  • 25
    • 34547683177 scopus 로고    scopus 로고
    • The positions of TFIIF and TFIIE in the RNA polymerase II transcription initiation complex
    • Chen, H.-T., Warfield, L. and Hahn, S. (2007) The positions of TFIIF and TFIIE in the RNA polymerase II transcription initiation complex. Nat. Struct. Mol. Biol., 8, 696-703.
    • (2007) Nat. Struct. Mol. Biol. , vol.8 , pp. 696-703
    • Chen, H.-T.1    Warfield, L.2    Hahn, S.3
  • 26
    • 0029737547 scopus 로고    scopus 로고
    • Fluorescence characteristics of 5-carboxytetramethylrhodamine linked covalently to the 5' end of oligonucleotides: multiple conformers of single-stranded and double-stranded dye-DNA complexes
    • Vamosi, G., Gohlke, C. and Clegg, R.M. (1996) Fluorescence characteristics of 5-carboxytetramethylrhodamine linked covalently to the 5' end of oligonucleotides: multiple conformers of single-stranded and double-stranded dye-DNA complexes. Biophys. J., 71, 972-994.
    • (1996) Biophys. J. , vol.71 , pp. 972-994
    • Vamosi, G.1    Gohlke, C.2    Clegg, R.M.3
  • 27
  • 29
    • 39149093390 scopus 로고    scopus 로고
    • Structure-function analysis of the RNA polymerase cleft loops elucidates initial transcription, DNA unwinding and RNA displacement
    • Naji, S., Bertero, M.G., Spitalny, P., Cramer, P. and Thomm, M. (2008) Structure-function analysis of the RNA polymerase cleft loops elucidates initial transcription, DNA unwinding and RNA displacement. Nucleic Acids Res., 36, 676-687.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 676-687
    • Naji, S.1    Bertero, M.G.2    Spitalny, P.3    Cramer, P.4    Thomm, M.5
  • 30
    • 0027244844 scopus 로고
    • Evidence of DNA bending in transcription complexes imaged by scanning force microscopy
    • Rees, W., Keller, R.W., Vesenka, J.P., Yang, G. and Bustamante, C. (1993) Evidence of DNA bending in transcription complexes imaged by scanning force microscopy. Science, 260, 1646-1649.
    • (1993) Science , vol.260 , pp. 1646-1649
    • Rees, W.1    Keller, R.W.2    Vesenka, J.P.3    Yang, G.4    Bustamante, C.5
  • 32
    • 0034625251 scopus 로고    scopus 로고
    • Structural organization of the RNA polymerase-promoter open complex
    • Naryshkin, N., Revyakin, A., Kim, Y., Mekler, V. and Ebright, R.H. (2000) Structural organization of the RNA polymerase-promoter open complex. Cell, 101, 601-611.
    • (2000) Cell , vol.101 , pp. 601-611
    • Naryshkin, N.1    Revyakin, A.2    Kim, Y.3    Mekler, V.4    Ebright, R.H.5
  • 33
    • 0034682813 scopus 로고    scopus 로고
    • Dissection of two hallmarks of the open promoter complex by mutation in an RNA polymerase core subunit
    • Nechaev, S., Chlenov, M. and Severinov, K. (2000) Dissection of two hallmarks of the open promoter complex by mutation in an RNA polymerase core subunit. J. Biol. Chem., 275, 25516-25522.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25516-25522
    • Nechaev, S.1    Chlenov, M.2    Severinov, K.3
  • 34
    • 0031456021 scopus 로고    scopus 로고
    • A mutant RNA polymerasethat forms unusual open promoter complexes
    • Severinov, K. and Darst, S.A. (1997) A mutant RNA polymerasethat forms unusual open promoter complexes. Proc. Natl Acad. Sci. USA, 94, 13481-13486.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 13481-13486
    • Severinov, K.1    Darst, S.A.2
  • 35
    • 0037086450 scopus 로고    scopus 로고
    • Structure-based analysis of RNA polymerase function: the largest subunit's rudder contributes critically to elongation complex stability and is not involved in the maintenance of RNA-DNA hybrid length
    • Kuznedelov, K., Korzheva, N., Mustaev, A. and Severinov, K. (2002) Structure-based analysis of RNA polymerase function: the largest subunit's rudder contributes critically to elongation complex stability and is not involved in the maintenance of RNA-DNA hybrid length. EMBO J., 21, 1369-1378.
    • (2002) EMBO J. , vol.21 , pp. 1369-1378
    • Kuznedelov, K.1    Korzheva, N.2    Mustaev, A.3    Severinov, K.4
  • 36
    • 33646188087 scopus 로고    scopus 로고
    • Mutations in the Saccharomyces cerevisiae RPB1 gene conferring hypersensitivity to 6-azauracil
    • Malagon, F., Kireeva, M.L., Shafer, B.K., Lubkowska, L., Kashlev, M. and Strathern, J.N. (2006) Mutations in the Saccharomyces cerevisiae RPB1 gene conferring hypersensitivity to 6-azauracil. Genetics, 172, 2201-2209.
    • (2006) Genetics , vol.172 , pp. 2201-2209
    • Malagon, F.1    Kireeva, M.L.2    Shafer, B.K.3    Lubkowska, L.4    Kashlev, M.5    Strathern, J.N.6
  • 37
    • 33746811857 scopus 로고    scopus 로고
    • The role of the lid element in transcription by E. coli RNA polymerase
    • Toulokhonov, I. and Landick, R. (2006) The role of the lid element in transcription by E. coli RNA polymerase. J. Mol. Biol., 361, 644-658.
    • (2006) J. Mol. Biol. , vol.361 , pp. 644-658
    • Toulokhonov, I.1    Landick, R.2
  • 38
    • 33746827367 scopus 로고    scopus 로고
    • The role of the largest RNA polymerase subunit lid element in preventing the formation of extended RNA-DNA hybrid
    • Naryshkina, T., Kuznedelov, K. and Severinov, K. (2006) The role of the largest RNA polymerase subunit lid element in preventing the formation of extended RNA-DNA hybrid. J. Mol. Biol., 361, 634-643.
    • (2006) J. Mol. Biol. , vol.361 , pp. 634-643
    • Naryshkina, T.1    Kuznedelov, K.2    Severinov, K.3
  • 39
    • 5444275331 scopus 로고    scopus 로고
    • Mapping the location of TFIIB within the RNA polymerase II transcription preinitiation complex: a model for the structure of the PIC
    • Chen, H.T. and Hahn, S. (2004) Mapping the location of TFIIB within the RNA polymerase II transcription preinitiation complex: a model for the structure of the PIC. Cell, 119, 169-180.
    • (2004) Cell , vol.119 , pp. 169-180
    • Chen, H.T.1    Hahn, S.2
  • 40
    • 30044431985 scopus 로고    scopus 로고
    • RNA emerging from the active site of RNA polymerase II interacts with the Rpb7 subunit
    • Ujvari, A. and Luse, D.S. (2006) RNA emerging from the active site of RNA polymerase II interacts with the Rpb7 subunit. Nat. Struct. Mol. Biol., 13, 4954.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 49-54
    • Ujvari, A.1    Luse, D.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.