메뉴 건너뛰기




Volumn 19, Issue 6, 2009, Pages 740-745

Structure-function analysis of RNA polymerases I and III

Author keywords

[No Author keywords available]

Indexed keywords

DNA DIRECTED RNA POLYMERASE; DNA DIRECTED RNA POLYMERASE III; TRANSCRIPTION FACTOR II; TRANSCRIPTION FACTOR IIS; UNCLASSIFIED DRUG;

EID: 70549090264     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2009.10.005     Document Type: Review
Times cited : (44)

References (52)
  • 2
    • 5444237797 scopus 로고    scopus 로고
    • What better measure than ribosome synthesis?
    • Rudra D., and Warner J.R. What better measure than ribosome synthesis?. Genes Dev 18 (2004) 2431-2436
    • (2004) Genes Dev , vol.18 , pp. 2431-2436
    • Rudra, D.1    Warner, J.R.2
  • 3
    • 66549126163 scopus 로고    scopus 로고
    • A movie of the RNA polymerase nucleotide addition cycle
    • Brueckner F., Ortiz J., and Cramer P. A movie of the RNA polymerase nucleotide addition cycle. Curr Opin Struct Biol 19 (2009) 294-299
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 294-299
    • Brueckner, F.1    Ortiz, J.2    Cramer, P.3
  • 4
    • 39049143397 scopus 로고    scopus 로고
    • Orthologs of the small RPB8 subunit of the eukaryotic RNA polymerases are conserved in hyperthermophilic Crenarchaeota and 'Korarchaeota'
    • Koonin E.V., Makarova K.S., and Elkins J.G. Orthologs of the small RPB8 subunit of the eukaryotic RNA polymerases are conserved in hyperthermophilic Crenarchaeota and 'Korarchaeota'. Biol Direct 2 (2007) 38
    • (2007) Biol Direct , vol.2 , pp. 38
    • Koonin, E.V.1    Makarova, K.S.2    Elkins, J.G.3
  • 5
    • 42649112370 scopus 로고    scopus 로고
    • Early evolution of eukaryotic DNA-dependent RNA polymerases
    • Kwapisz M., Beckouet F., and Thuriaux P. Early evolution of eukaryotic DNA-dependent RNA polymerases. Trends Genet 24 (2008) 211-215
    • (2008) Trends Genet , vol.24 , pp. 211-215
    • Kwapisz, M.1    Beckouet, F.2    Thuriaux, P.3
  • 6
    • 66249122044 scopus 로고    scopus 로고
    • Evolution of complex RNA polymerases: the complete archaeal RNA polymerase structure
    • The authors determine the crystal structure of the complete archaeal RNA polymerase from Sulfolobus shibatae at 3.35 Å resolution including Rpo8/G subunit and a newly identified component of the Sulfolobales order enzyme, Rpo13.
    • Korkhin Y., Unligil U.M., Littlefield O., Nelson P.J., Stuart D.I., Sigler P.B., Bell S.D., and Abrescia N.G. Evolution of complex RNA polymerases: the complete archaeal RNA polymerase structure. PLoS Biol 7 (2009) e102. The authors determine the crystal structure of the complete archaeal RNA polymerase from Sulfolobus shibatae at 3.35 Å resolution including Rpo8/G subunit and a newly identified component of the Sulfolobales order enzyme, Rpo13.
    • (2009) PLoS Biol , vol.7
    • Korkhin, Y.1    Unligil, U.M.2    Littlefield, O.3    Nelson, P.J.4    Stuart, D.I.5    Sigler, P.B.6    Bell, S.D.7    Abrescia, N.G.8
  • 7
    • 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
  • 8
    • 34248675797 scopus 로고    scopus 로고
    • Transcription factor TFIIIB and transcription by RNA polymerase III
    • Kassavetis G.A., and Geiduschek E.P. Transcription factor TFIIIB and transcription by RNA polymerase III. Biochem Soc Trans 34 (2006) 1082-1087
    • (2006) Biochem Soc Trans , vol.34 , pp. 1082-1087
    • Kassavetis, G.A.1    Geiduschek, E.P.2
  • 9
    • 33744966027 scopus 로고    scopus 로고
    • Reconstitution of the yeast RNA polymerase III transcription system with all recombinant factors
    • Ducrot C., Lefebvre O., Landrieux E., Guirouilh-Barbat J., Sentenac A., and Acker J. Reconstitution of the yeast RNA polymerase III transcription system with all recombinant factors. J Biol Chem 281 (2006) 11685-11692
    • (2006) J Biol Chem , vol.281 , pp. 11685-11692
    • Ducrot, C.1    Lefebvre, O.2    Landrieux, E.3    Guirouilh-Barbat, J.4    Sentenac, A.5    Acker, J.6
  • 10
    • 33750087881 scopus 로고    scopus 로고
    • Structure of the tau60/Delta tau91 subcomplex of yeast transcription factor IIIC: insights into preinitiation complex assembly
    • Mylona A., Fernandez-Tornero C., Legrand P., Haupt M., Sentenac A., Acker J., and Muller C.W. Structure of the tau60/Delta tau91 subcomplex of yeast transcription factor IIIC: insights into preinitiation complex assembly. Mol Cell 24 (2006) 221-232
    • (2006) Mol Cell , vol.24 , pp. 221-232
    • Mylona, A.1    Fernandez-Tornero, C.2    Legrand, P.3    Haupt, M.4    Sentenac, A.5    Acker, J.6    Muller, C.W.7
  • 11
    • 33947369108 scopus 로고    scopus 로고
    • Insights into transcription initiation and termination from the electron microscopy structure of yeast RNA polymerase III
    • The yeast Pol III envelope, determined at 17 Å resolution by cryo-electron microscopy and single-particle analysis, shows a hand-like shape typical of RNA polymerases and, compared with Pol II structure, prominent features attributed to Pol-III-specific subunits and a bulkier stalk.
    • Fernandez-Tornero C., Bottcher B., Riva M., Carles C., Steuerwald U., Ruigrok R.W., Sentenac A., Muller C.W., and Schoehn G. Insights into transcription initiation and termination from the electron microscopy structure of yeast RNA polymerase III. Mol Cell 25 (2007) 813-823. The yeast Pol III envelope, determined at 17 Å resolution by cryo-electron microscopy and single-particle analysis, shows a hand-like shape typical of RNA polymerases and, compared with Pol II structure, prominent features attributed to Pol-III-specific subunits and a bulkier stalk.
    • (2007) Mol Cell , vol.25 , pp. 813-823
    • Fernandez-Tornero, C.1    Bottcher, B.2    Riva, M.3    Carles, C.4    Steuerwald, U.5    Ruigrok, R.W.6    Sentenac, A.7    Muller, C.W.8    Schoehn, G.9
  • 12
    • 33745499068 scopus 로고    scopus 로고
    • Structural biology of RNA polymerase III: subcomplex C17/25 X-ray structure and 11 subunit enzyme model
    • This paper provides an 11 subunit model of yeast Pol III by combining a homology model of the 9 subunit core enzyme with a X-ray structure at 3.2 Å resolution of the stalk subcomplex Rpc17/25 revealing specific features of Pol III that can account for functional differences between nuclear RNA polymerases.
    • Jasiak A.J., Armache K.J., Martens B., Jansen R.P., and Cramer P. Structural biology of RNA polymerase III: subcomplex C17/25 X-ray structure and 11 subunit enzyme model. Mol Cell 23 (2006) 71-81. This paper provides an 11 subunit model of yeast Pol III by combining a homology model of the 9 subunit core enzyme with a X-ray structure at 3.2 Å resolution of the stalk subcomplex Rpc17/25 revealing specific features of Pol III that can account for functional differences between nuclear RNA polymerases.
    • (2006) Mol Cell , vol.23 , pp. 71-81
    • Jasiak, A.J.1    Armache, K.J.2    Martens, B.3    Jansen, R.P.4    Cramer, P.5
  • 13
    • 0026590733 scopus 로고
    • Effect of mutations in a zinc-binding domain of yeast RNA polymerase C (III) on enzyme function and subunit association
    • Werner M., Hermann-Le Denmat S., Treich I., Sentenac A., and Thuriaux P. Effect of mutations in a zinc-binding domain of yeast RNA polymerase C (III) on enzyme function and subunit association. Mol Cell Biol 12 (1992) 1087-1095
    • (1992) Mol Cell Biol , vol.12 , pp. 1087-1095
    • Werner, M.1    Hermann-Le Denmat, S.2    Treich, I.3    Sentenac, A.4    Thuriaux, P.5
  • 14
    • 35148816658 scopus 로고    scopus 로고
    • Structural biology of RNA polymerase III: mass spectrometry elucidates subcomplex architecture
    • Lorenzen K., Vannini A., Cramer P., and Heck A.J. Structural biology of RNA polymerase III: mass spectrometry elucidates subcomplex architecture. Structure 15 (2007) 1237-1245
    • (2007) Structure , vol.15 , pp. 1237-1245
    • Lorenzen, K.1    Vannini, A.2    Cramer, P.3    Heck, A.J.4
  • 16
    • 0030931573 scopus 로고    scopus 로고
    • Identification of an autonomously initiating RNA polymerase III holoenzyme containing a novel factor that is selectively inactivated during protein synthesis inhibition
    • Wang Z., Luo T., and Roeder R.G. Identification of an autonomously initiating RNA polymerase III holoenzyme containing a novel factor that is selectively inactivated during protein synthesis inhibition. Genes Dev 11 (1997) 2371-2382
    • (1997) Genes Dev , vol.11 , pp. 2371-2382
    • Wang, Z.1    Luo, T.2    Roeder, R.G.3
  • 17
    • 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. Mapping the location of TFIIB within the RNA polymerase II transcription preinitiation complex: a model for the structure of the PIC. Cell 119 (2004) 169-180
    • (2004) Cell , vol.119 , pp. 169-180
    • Chen, H.T.1    Hahn, S.2
  • 18
    • 1142274214 scopus 로고    scopus 로고
    • Structural basis of transcription: an RNA polymerase II-TFIIB cocrystal at 4.5 Angstroms
    • Bushnell D.A., Westover K.D., Davis R.E., and Kornberg R.D. Structural basis of transcription: an RNA polymerase II-TFIIB cocrystal at 4.5 Angstroms. Science 303 (2004) 983-988
    • (2004) Science , vol.303 , pp. 983-988
    • Bushnell, D.A.1    Westover, K.D.2    Davis, R.E.3    Kornberg, R.D.4
  • 19
    • 0037495037 scopus 로고    scopus 로고
    • Architecture of initiation-competent 12-subunit RNA polymerase II
    • The authors report a model of the complete Pol II by fitting structures of the core and Rpb4/7 to a 4.2 Å crystallographic electron density map.
    • Armache K.J., Kettenberger H., and Cramer P. Architecture of initiation-competent 12-subunit RNA polymerase II. Proc Natl Acad Sci USA 100 (2003) 6964-6968. The authors report a model of the complete Pol II by fitting structures of the core and Rpb4/7 to a 4.2 Å crystallographic electron density map.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6964-6968
    • Armache, K.J.1    Kettenberger, H.2    Cramer, P.3
  • 20
    • 0037832543 scopus 로고    scopus 로고
    • Complete, 12-subunit RNA polymerase II at 4.1-A resolution: implications for the initiation of transcription
    • The X-ray structure of complete Pol II from S. cerevisiae at 4.1 Å resolution including the Rpb4/7 heterodimer is described.
    • Bushnell D.A., and Kornberg R.D. Complete, 12-subunit RNA polymerase II at 4.1-A resolution: implications for the initiation of transcription. Proc Natl Acad Sci U S A 100 (2003) 6969-6973. The X-ray structure of complete Pol II from S. cerevisiae at 4.1 Å resolution including the Rpb4/7 heterodimer is described.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 6969-6973
    • Bushnell, D.A.1    Kornberg, R.D.2
  • 21
    • 12344306120 scopus 로고    scopus 로고
    • Rpc25, a conserved RNA polymerase III subunit, is critical for transcription initiation
    • Zaros C., and Thuriaux P. Rpc25, a conserved RNA polymerase III subunit, is critical for transcription initiation. Mol Microbiol 55 (2005) 104-114
    • (2005) Mol Microbiol , vol.55 , pp. 104-114
    • Zaros, C.1    Thuriaux, P.2
  • 23
    • 30444450804 scopus 로고    scopus 로고
    • A subcomplex of RNA polymerase III subunits is required for transcription termination and reinitiation
    • This paper shows the specific requirement for the Rpc37/53 subcomplex in Pol III termination and the role of Rpc11 subunit in recycling, independent of its role in RNA cleavage.
    • Landrieux E., Nazif A., Ducrot C., Acker J., Riva M., and Carles C. A subcomplex of RNA polymerase III subunits is required for transcription termination and reinitiation. EMBO J 25 (2005) 118-128. This paper shows the specific requirement for the Rpc37/53 subcomplex in Pol III termination and the role of Rpc11 subunit in recycling, independent of its role in RNA cleavage.
    • (2005) EMBO J , vol.25 , pp. 118-128
    • Landrieux, E.1    Nazif, A.2    Ducrot, C.3    Acker, J.4    Riva, M.5    Carles, C.6
  • 25
    • 37349041027 scopus 로고    scopus 로고
    • Functional architecture of RNA polymerase I
    • This paper substantially improves the structural data available so far for yeast Pol I, combining a 12 Å EM envelope structure with an atomic crystal structure of the Rpa14/Rpa43 stalk. It also documents the contribution of Rpa12 to the intrinsic transcript cleavage activity of Pol I and suggests that the Pol-I-specific subunits Rpa34 and Rpa49 may be functionally and structurally equivalent to the two main subunits of TFIIF, thus acting as a built-in elongation factor.
    • Kuhn C.D., Geiger S.R., Baumli S., Gartmann M., Gerber J., Jennebach S., Mielke T., Tschochner H., Beckmann R., and Cramer P. Functional architecture of RNA polymerase I. Cell 131 (2007) 1260-1272. This paper substantially improves the structural data available so far for yeast Pol I, combining a 12 Å EM envelope structure with an atomic crystal structure of the Rpa14/Rpa43 stalk. It also documents the contribution of Rpa12 to the intrinsic transcript cleavage activity of Pol I and suggests that the Pol-I-specific subunits Rpa34 and Rpa49 may be functionally and structurally equivalent to the two main subunits of TFIIF, thus acting as a built-in elongation factor.
    • (2007) Cell , vol.131 , pp. 1260-1272
    • Kuhn, C.D.1    Geiger, S.R.2    Baumli, S.3    Gartmann, M.4    Gerber, J.5    Jennebach, S.6    Mielke, T.7    Tschochner, H.8    Beckmann, R.9    Cramer, P.10
  • 26
    • 0031001382 scopus 로고    scopus 로고
    • A34.5, a nonessential component of yeast RNA polymerase I, cooperates with subunit A14 and DNA topoisomerase I to produce a functional rRNA synthesis machine
    • Gadal O., Mariotte-Labarre S., Chedin S., Quemeneur E., Carles C., Sentenac A., and Thuriaux P. A34.5, a nonessential component of yeast RNA polymerase I, cooperates with subunit A14 and DNA topoisomerase I to produce a functional rRNA synthesis machine. Mol Cell Biol 17 (1997) 1787-1795
    • (1997) Mol Cell Biol , vol.17 , pp. 1787-1795
    • Gadal, O.1    Mariotte-Labarre, S.2    Chedin, S.3    Quemeneur, E.4    Carles, C.5    Sentenac, A.6    Thuriaux, P.7
  • 27
    • 40749128530 scopus 로고    scopus 로고
    • Two RNA polymerase I subunits control the binding and release of Rrn3 during transcription
    • This paper presents genetic evidence showing that the Rpa49 subunit (and its Rpa34 partner) contributes to the early phase of elongation by favouring the release of the Rrn3 initiation factor during promoter escape, but also suggests that Rpa49 may directly affect the efficiency of Pol I recruitment at the rDNA promoter.
    • Beckouet F., Labarre-Mariotte S., Albert B., Imazawa Y., Werner M., Gadal O., Nogi Y., and Thuriaux P. Two RNA polymerase I subunits control the binding and release of Rrn3 during transcription. Mol Cell Biol 28 (2008) 1596-1605. This paper presents genetic evidence showing that the Rpa49 subunit (and its Rpa34 partner) contributes to the early phase of elongation by favouring the release of the Rrn3 initiation factor during promoter escape, but also suggests that Rpa49 may directly affect the efficiency of Pol I recruitment at the rDNA promoter.
    • (2008) Mol Cell Biol , vol.28 , pp. 1596-1605
    • Beckouet, F.1    Labarre-Mariotte, S.2    Albert, B.3    Imazawa, Y.4    Werner, M.5    Gadal, O.6    Nogi, Y.7    Thuriaux, P.8
  • 28
    • 33745856637 scopus 로고    scopus 로고
    • RNA polymerase I-specific subunit CAST/hPAF49 has a role in the activation of transcription by upstream binding factor
    • Panov K.I., Panova T.B., Gadal O., Nishiyama K., Saito T., Russell J., and Zomerdijk J.C. RNA polymerase I-specific subunit CAST/hPAF49 has a role in the activation of transcription by upstream binding factor. Mol Cell Biol 26 (2006) 5436-5448
    • (2006) Mol Cell Biol , vol.26 , pp. 5436-5448
    • Panov, K.I.1    Panova, T.B.2    Gadal, O.3    Nishiyama, K.4    Saito, T.5    Russell, J.6    Zomerdijk, J.C.7
  • 29
    • 0034675857 scopus 로고    scopus 로고
    • The recruitment of RNA polymerase I on rDNA is mediated by the interaction of the A43 subunit with Rrn3
    • First direct evidence that Pol I needs to form a Pol I-Rrn3 complex in order to be recruited at the rDNA promoter, due to a direct contact between Rrn3 and Rpa43 that is the main component of the Pol I 'stalk'.
    • Peyroche G., Milkereit P., Bischler N., Tschochner H., Schultz P., Sentenac A., Carles C., and Riva M. The recruitment of RNA polymerase I on rDNA is mediated by the interaction of the A43 subunit with Rrn3. EMBO J 19 (2000) 5473-5482. First direct evidence that Pol I needs to form a Pol I-Rrn3 complex in order to be recruited at the rDNA promoter, due to a direct contact between Rrn3 and Rpa43 that is the main component of the Pol I 'stalk'.
    • (2000) EMBO J , vol.19 , pp. 5473-5482
    • Peyroche, G.1    Milkereit, P.2    Bischler, N.3    Tschochner, H.4    Schultz, P.5    Sentenac, A.6    Carles, C.7    Riva, M.8
  • 30
    • 33746631755 scopus 로고    scopus 로고
    • The transcriptional activity of RNA polymerase I is a key determinant for the level of all ribosome components
    • Using a yeast strain constitutively competent for Pol I recruitment at the rDNA promoter, the authors demonstrate that constitutive rDNA transcription correlates with an activation of the Pol II-dependent transcription of ribosomal protein genes. They also observe a de-regulation of Pol III, possibly limited to the synthesis of the 5S rRNA.
    • Laferté A., Favry E., Sentenac A., Riva M., Carles C., and Chédin S. The transcriptional activity of RNA polymerase I is a key determinant for the level of all ribosome components. Genes Dev 20 (2006) 2030-2040. Using a yeast strain constitutively competent for Pol I recruitment at the rDNA promoter, the authors demonstrate that constitutive rDNA transcription correlates with an activation of the Pol II-dependent transcription of ribosomal protein genes. They also observe a de-regulation of Pol III, possibly limited to the synthesis of the 5S rRNA.
    • (2006) Genes Dev , vol.20 , pp. 2030-2040
    • Laferté, A.1    Favry, E.2    Sentenac, A.3    Riva, M.4    Carles, C.5    Chédin, S.6
  • 31
    • 33646847147 scopus 로고    scopus 로고
    • The RNA polymerase I transcription machinery
    • Russell J., and Zomerdijk J.C. The RNA polymerase I transcription machinery. Biochem Soc Symp 73 (2006) 203-216
    • (2006) Biochem Soc Symp , vol.73 , pp. 203-216
    • Russell, J.1    Zomerdijk, J.C.2
  • 33
    • 43249097755 scopus 로고    scopus 로고
    • Actively transcribed rRNA genes in S. cerevisiae are organized in a specialized chromatin associated with the high-mobility group protein Hmo1 and are largely devoid of histone molecules
    • Merz K., Hondele M., Goetze H., Gmelch K., Stoeckl U., and Griesenbeck J. Actively transcribed rRNA genes in S. cerevisiae are organized in a specialized chromatin associated with the high-mobility group protein Hmo1 and are largely devoid of histone molecules. Genes Dev 22 (2008) 1190-1204
    • (2008) Genes Dev , vol.22 , pp. 1190-1204
    • Merz, K.1    Hondele, M.2    Goetze, H.3    Gmelch, K.4    Stoeckl, U.5    Griesenbeck, J.6
  • 34
    • 36048959205 scopus 로고    scopus 로고
    • Hmo1 is required for TOR-dependent regulation of ribosomal protein gene transcription
    • Berger A.B., Decourty L., Badis G., Nehrbass U., Jacquier A., and Gadal O. Hmo1 is required for TOR-dependent regulation of ribosomal protein gene transcription. Mol Cell Biol 27 (2007) 8015-8026
    • (2007) Mol Cell Biol , vol.27 , pp. 8015-8026
    • Berger, A.B.1    Decourty, L.2    Badis, G.3    Nehrbass, U.4    Jacquier, A.5    Gadal, O.6
  • 35
    • 33646242795 scopus 로고    scopus 로고
    • An HMG protein. Hmo1, associates with promoters of many ribosomal protein genes and throughout the rRNA gene locus in Saccharomyces cerevisiae
    • Hall D.B., Wade J.T., and Struhl K. An HMG protein. Hmo1, associates with promoters of many ribosomal protein genes and throughout the rRNA gene locus in Saccharomyces cerevisiae. Mol Cell Biol 26 (2006) 3672-3679
    • (2006) Mol Cell Biol , vol.26 , pp. 3672-3679
    • Hall, D.B.1    Wade, J.T.2    Struhl, K.3
  • 37
    • 34548238632 scopus 로고    scopus 로고
    • Active RNA polymerase I of Trypanosoma brucei harbors a novel subunit essential for transcription
    • Nguyen T.N., Schimanski B., and Gunzl A. Active RNA polymerase I of Trypanosoma brucei harbors a novel subunit essential for transcription. Mol Cell Biol 27 (2007) 6254-6263
    • (2007) Mol Cell Biol , vol.27 , pp. 6254-6263
    • Nguyen, T.N.1    Schimanski, B.2    Gunzl, A.3
  • 38
    • 61849090827 scopus 로고    scopus 로고
    • RNA pol II subunit RPB7 is required for RNA pol I-mediated transcription in Trypanosoma brucei
    • In trypanosomes and other kinetoplastids, Pol I transcribes several strongly expressed protein-encoding genes, in addition to its canonical rDNA template. This paper provides an interesting clue by suggesting that the Rpb7 component of the Pol II stalk is associated to the trypanosomal Pol I.
    • Penate X., Lopez-Farfan D., Landeira D., Wentland A., Vidal I., and Navarro M. RNA pol II subunit RPB7 is required for RNA pol I-mediated transcription in Trypanosoma brucei. EMBO Rep 10 (2009) 252-257. In trypanosomes and other kinetoplastids, Pol I transcribes several strongly expressed protein-encoding genes, in addition to its canonical rDNA template. This paper provides an interesting clue by suggesting that the Rpb7 component of the Pol II stalk is associated to the trypanosomal Pol I.
    • (2009) EMBO Rep , vol.10 , pp. 252-257
    • Penate, X.1    Lopez-Farfan, D.2    Landeira, D.3    Wentland, A.4    Vidal, I.5    Navarro, M.6
  • 39
    • 0037073048 scopus 로고    scopus 로고
    • Promoting elongation with transcript cleavage stimulatory factors
    • Fish R.N., and Kane C.M. Promoting elongation with transcript cleavage stimulatory factors. Biochim Biophys Acta 1577 (2002) 287-307
    • (2002) Biochim Biophys Acta , vol.1577 , pp. 287-307
    • Fish, R.N.1    Kane, C.M.2
  • 40
    • 9144246231 scopus 로고    scopus 로고
    • Members of the SAGA and Mediator complexes are partners of the transcription elongation factor TFIIS
    • Wery M., Shematorova E., Van Driessche B., Vandenhaute J., Thuriaux P., and Van Mullem V. Members of the SAGA and Mediator complexes are partners of the transcription elongation factor TFIIS. EMBO J 23 (2004) 4232-4242
    • (2004) EMBO J , vol.23 , pp. 4232-4242
    • Wery, M.1    Shematorova, E.2    Van Driessche, B.3    Vandenhaute, J.4    Thuriaux, P.5    Van Mullem, V.6
  • 41
    • 1942421800 scopus 로고    scopus 로고
    • Genetic interactions of DST1 in Saccharomyces cerevisiae suggest a role of TFIIS in the initiation-elongation transition
    • Malagon F., Tong A.H., Shafer B.K., and Strathern J.N. Genetic interactions of DST1 in Saccharomyces cerevisiae suggest a role of TFIIS in the initiation-elongation transition. Genetics 166 (2004) 1215-1227
    • (2004) Genetics , vol.166 , pp. 1215-1227
    • Malagon, F.1    Tong, A.H.2    Shafer, B.K.3    Strathern, J.N.4
  • 42
    • 15044358405 scopus 로고    scopus 로고
    • Evidence that the elongation factor TFIIS plays a role in transcription initiation at GAL1 in Saccharomyces cerevisiae
    • Prather D.M., Larschan E., and Winston F. Evidence that the elongation factor TFIIS plays a role in transcription initiation at GAL1 in Saccharomyces cerevisiae. Mol Cell Biol 25 (2005) 2650-2659
    • (2005) Mol Cell Biol , vol.25 , pp. 2650-2659
    • Prather, D.M.1    Larschan, E.2    Winston, F.3
  • 43
    • 36049035016 scopus 로고    scopus 로고
    • The transcription elongation factor TFIIS is a component of RNA polymerase II preinitiation complexes
    • Kim B., Nesvizhskii A.I., Rani P.G., Hahn S., Aebersold R., and Ranish J.A. The transcription elongation factor TFIIS is a component of RNA polymerase II preinitiation complexes. Proc Natl Acad Sci U S A 104 (2007) 16068-16073
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 16068-16073
    • Kim, B.1    Nesvizhskii, A.I.2    Rani, P.G.3    Hahn, S.4    Aebersold, R.5    Ranish, J.A.6
  • 44
    • 36049014424 scopus 로고    scopus 로고
    • TFIIS elongation factor and Mediator act in conjunction during transcription initiation in vivo
    • Guglielmi B., Soutourina J., Esnault C., and Werner M. TFIIS elongation factor and Mediator act in conjunction during transcription initiation in vivo. Proc Natl Acad Sci U S A 104 (2007) 16062-16067
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 16062-16067
    • Guglielmi, B.1    Soutourina, J.2    Esnault, C.3    Werner, M.4
  • 45
    • 0043244876 scopus 로고    scopus 로고
    • Architecture of the RNA polymerase II-TFIIS complex and implications for mRNA cleavage
    • A crystal structure model of the Pol II-TFIIS complex at 3.8 Å resolution shows that TFIIS central domain extends from the polymerase surface via a pore and brings the C-terminal conserved SADE motif very close to the Pol II active site to stimulate the intrinsic transcript cleavage activity of the enzyme.
    • Kettenberger H., Armache K.J., and Cramer P. Architecture of the RNA polymerase II-TFIIS complex and implications for mRNA cleavage. Cell 114 (2003) 347-357. A crystal structure model of the Pol II-TFIIS complex at 3.8 Å resolution shows that TFIIS central domain extends from the polymerase surface via a pore and brings the C-terminal conserved SADE motif very close to the Pol II active site to stimulate the intrinsic transcript cleavage activity of the enzyme.
    • (2003) Cell , vol.114 , pp. 347-357
    • Kettenberger, H.1    Armache, K.J.2    Cramer, P.3
  • 46
    • 47549116548 scopus 로고    scopus 로고
    • Genome-wide location analysis reveals a role for TFIIS in RNA polymerase III transcription
    • On the basis of genome-wide location analysis, this paper reveals a previously unsuspected role of TFIIS, one of the well-characterized Pol II transcription elongation factor, in Pol III transcription and provides strong in vivo and in vitro evidence in favour of a role for TFIIS as a general Pol III transcription factor.
    • Ghavi-Helm Y., Michaut M., Acker J., Aude J., Thuriaux P., Werner M., and Soutourina J. Genome-wide location analysis reveals a role for TFIIS in RNA polymerase III transcription. Genes Dev 22 (2008) 1934-1947. On the basis of genome-wide location analysis, this paper reveals a previously unsuspected role of TFIIS, one of the well-characterized Pol II transcription elongation factor, in Pol III transcription and provides strong in vivo and in vitro evidence in favour of a role for TFIIS as a general Pol III transcription factor.
    • (2008) Genes Dev , vol.22 , pp. 1934-1947
    • Ghavi-Helm, Y.1    Michaut, M.2    Acker, J.3    Aude, J.4    Thuriaux, P.5    Werner, M.6    Soutourina, J.7
  • 47
    • 0032535546 scopus 로고    scopus 로고
    • The RNA cleavage activity of RNA polymerase III is mediated by an essential TFIIS-like subunit and is important for transcription termination
    • Chedin S., Riva M., Schultz P., Sentenac A., and Carles C. The RNA cleavage activity of RNA polymerase III is mediated by an essential TFIIS-like subunit and is important for transcription termination. Genes Dev 12 (1998) 3857-3871
    • (1998) Genes Dev , vol.12 , pp. 3857-3871
    • Chedin, S.1    Riva, M.2    Schultz, P.3    Sentenac, A.4    Carles, C.5
  • 49
    • 0036227539 scopus 로고    scopus 로고
    • Rpa12p, a conserved RNA polymerase I subunit with two functional domains
    • Van Mullem V., Landrieux E., Vandenhaute J., and Thuriaux P. Rpa12p, a conserved RNA polymerase I subunit with two functional domains. Mol Microbiol 43 (2002) 1105-1113
    • (2002) Mol Microbiol , vol.43 , pp. 1105-1113
    • Van Mullem, V.1    Landrieux, E.2    Vandenhaute, J.3    Thuriaux, P.4
  • 50
    • 0030987775 scopus 로고    scopus 로고
    • Transcription elongation through DNA arrest sites. A multistep process involving both RNA polymerase II subunit RPB9 and TFIIS
    • Awrey D.E., Weilbaecher R.G., Hemming S.A., Orlicky S.M., Kane C.M., and Edwards A.M. Transcription elongation through DNA arrest sites. A multistep process involving both RNA polymerase II subunit RPB9 and TFIIS. J Biol Chem 272 (1997) 14747-14754
    • (1997) J Biol Chem , vol.272 , pp. 14747-14754
    • Awrey, D.E.1    Weilbaecher, R.G.2    Hemming, S.A.3    Orlicky, S.M.4    Kane, C.M.5    Edwards, A.M.6
  • 51
    • 0034724854 scopus 로고    scopus 로고
    • Transcription factor S, a cleavage induction factor of the archaeal RNA polymerase
    • Hausner W., Lange U., and Musfeldt M. Transcription factor S, a cleavage induction factor of the archaeal RNA polymerase. J Biol Chem 275 (2000) 12393-12399
    • (2000) J Biol Chem , vol.275 , pp. 12393-12399
    • Hausner, W.1    Lange, U.2    Musfeldt, M.3
  • 52
    • 33748053333 scopus 로고    scopus 로고
    • RNA polymerase II elongation factors Spt4p and Spt5p play roles in transcription elongation by RNA polymerase I and rRNA processing
    • This paper establishes that rDNA transcription depends on Spt4 and Spt5, two elongation factors initially identified by their association with Pol II. Intriguingly, Spt4 and Spt5 are also homologous to archaeal proteins and was thus probably inherited from the last ancestor shared by Archaea and Eukaryotes.
    • Schneider D.A., French S.L., Osheim Y.N., Bailey A.O., Vu L., Dodd J., Yates J.R., Beyer A.L., and Nomura M. RNA polymerase II elongation factors Spt4p and Spt5p play roles in transcription elongation by RNA polymerase I and rRNA processing. Proc Natl Acad Sci USA (2006). This paper establishes that rDNA transcription depends on Spt4 and Spt5, two elongation factors initially identified by their association with Pol II. Intriguingly, Spt4 and Spt5 are also homologous to archaeal proteins and was thus probably inherited from the last ancestor shared by Archaea and Eukaryotes.
    • (2006) Proc Natl Acad Sci USA
    • Schneider, D.A.1    French, S.L.2    Osheim, Y.N.3    Bailey, A.O.4    Vu, L.5    Dodd, J.6    Yates, J.R.7    Beyer, A.L.8    Nomura, M.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.