Gros plan sur l’ARN polymérase II

Marie-France Langelier; Vincent Trinh; Benoit Coulombe

doi:10.1051/medsci/2002182210

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Volume 18 / Numéro 2 (Février 2002)

Med Sci (Paris), 18 2 (2002) 210-216

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Numéro		Med Sci (Paris) Volume 18, Numéro 2, Février 2002


Page(s)		210 - 216
Section		M/S Revues : Mini-Synthèses
DOI		https://doi.org/10.1051/medsci/2002182210
Publié en ligne		15 février 2002

Orphanides G, Lagrange T, Reinberg D. The general transcription factors of RNA polymerase II. Genes Dev 1996; 10 : 2657–83. [Google Scholar]
Douziech M, Coin F, Chipoulet JM, et al. Mechanism of promoter melting by the xeroderma pigmentosum complementation group B helicase of transcription factor IIH revealed by protein-DNA photocross-linking. Mol Cel Biol 2000; 20 : 8168–77. [Google Scholar]
Holstege FC, Fiedler U, Timmers HT. Three transitions in the RNA polymerase II transcription complex during initiation. EMBO J 1997; 16 : 7468–80. [Google Scholar]
Conaway JW, Shilatifard A, Dvir A, Conaway RC. Control of elongation by RNA polymerase II. Trends Biochem Sci 2000; 25 : 375–80. [Google Scholar]
Coulombe B, Burton ZF. DNA bending and wrapping around RNA polymerase: a «revolutionary» model describing transcriptional mechanisms. Microbiol Mol Biol Rev 1999; 63 : 457–78. [Google Scholar]
Awrey DE, Weilbaecher RG, Hemming SA, Orlicky SM, Kane CM, Edwards AM. Transcription elongation through DNA arrest sites. J Biol Chem 1997; 272 : 14747–54. [Google Scholar]
Maillet I, Buhler JM, Sentenac A, Labarre J. Rpb4p is necessary for RNA polymerase II activity at high temperature. J Biol Chem 1999; 274 : 22586–90. [Google Scholar]
Cramer P, Bushnell DA, Kornberg RD. Structural basis of transcription: RNA polymerase II at 2.8 A resolution. Science 2001; 292 : 1863–76. [Google Scholar]
Gnatt AL, Cramer P, Fu J, Bushnell DA, Kornberg RD. Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 A resolution. Science 2001; 292 : 1876–82. [Google Scholar]
Poglitsch CL, Meredith GD, Gnatt A, et al. Electron crystal structure of an RNA polymerase II transcription elongation complex. Cell 1999; 98 : 791–8. [Google Scholar]
Fu J, Gnatt AL, Bushnell DA, et al. Yeast RNA polymerase II at 5 A resolution. Cell 1999; 98 : 799–810. [Google Scholar]
Cramer P, Bushnell DA, Fu J, et al. Architecture of RNA polymerase II and implications for the transcription mechanism. Science 2000; 288 : 640–9. [Google Scholar]
Nudler E, Mustaev A, Lukhtanov E, Goldfarb A. The RNA-DNA hybrid maintains the register of transcription by preventing backtracking of RNA polymerase. Cell 1997; 89 : 33–41. [Google Scholar]
Zhang G, Campbell EA, Minakhin L, Richter C, Severinov K, Darst SA. Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution. Cell 1999; 98 : 811–24. [Google Scholar]
Cho EJ, Takagi T, Moore CR, Buratowski S. mRNA cap-ping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxy-terminal domain. Genes Dev 1997; 11 : 3319–26. [Google Scholar]
McCracken S, Fong N, Rosonina E, et al. 5’-Capping enzymes are targeted to pre-mRNA by binding to the phosphorylated carboxy-terminal domain of RNA polymerase II. Genes Dev 1997; 11 : 3306–18. [Google Scholar]

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[1] Orphanides G, Lagrange T, Reinberg D. The general transcription factors of RNA polymerase II. Genes Dev 1996; 10 : 2657–83. [Google Scholar]

[2] Douziech M, Coin F, Chipoulet JM, et al. Mechanism of promoter melting by the xeroderma pigmentosum complementation group B helicase of transcription factor IIH revealed by protein-DNA photocross-linking. Mol Cel Biol 2000; 20 : 8168–77. [Google Scholar]

[3] Holstege FC, Fiedler U, Timmers HT. Three transitions in the RNA polymerase II transcription complex during initiation. EMBO J 1997; 16 : 7468–80. [Google Scholar]

[4] Conaway JW, Shilatifard A, Dvir A, Conaway RC. Control of elongation by RNA polymerase II. Trends Biochem Sci 2000; 25 : 375–80. [Google Scholar]

[5] Coulombe B, Burton ZF. DNA bending and wrapping around RNA polymerase: a «revolutionary» model describing transcriptional mechanisms. Microbiol Mol Biol Rev 1999; 63 : 457–78. [Google Scholar]

[6] Awrey DE, Weilbaecher RG, Hemming SA, Orlicky SM, Kane CM, Edwards AM. Transcription elongation through DNA arrest sites. J Biol Chem 1997; 272 : 14747–54. [Google Scholar]

[7] Maillet I, Buhler JM, Sentenac A, Labarre J. Rpb4p is necessary for RNA polymerase II activity at high temperature. J Biol Chem 1999; 274 : 22586–90. [Google Scholar]

[8] Cramer P, Bushnell DA, Kornberg RD. Structural basis of transcription: RNA polymerase II at 2.8 A resolution. Science 2001; 292 : 1863–76. [Google Scholar]

[9] Gnatt AL, Cramer P, Fu J, Bushnell DA, Kornberg RD. Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 A resolution. Science 2001; 292 : 1876–82. [Google Scholar]

[10] Poglitsch CL, Meredith GD, Gnatt A, et al. Electron crystal structure of an RNA polymerase II transcription elongation complex. Cell 1999; 98 : 791–8. [Google Scholar]

[11] Fu J, Gnatt AL, Bushnell DA, et al. Yeast RNA polymerase II at 5 A resolution. Cell 1999; 98 : 799–810. [Google Scholar]

[12] Cramer P, Bushnell DA, Fu J, et al. Architecture of RNA polymerase II and implications for the transcription mechanism. Science 2000; 288 : 640–9. [Google Scholar]

[13] Nudler E, Mustaev A, Lukhtanov E, Goldfarb A. The RNA-DNA hybrid maintains the register of transcription by preventing backtracking of RNA polymerase. Cell 1997; 89 : 33–41. [Google Scholar]

[14] Zhang G, Campbell EA, Minakhin L, Richter C, Severinov K, Darst SA. Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution. Cell 1999; 98 : 811–24. [Google Scholar]

[15] Cho EJ, Takagi T, Moore CR, Buratowski S. mRNA cap-ping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxy-terminal domain. Genes Dev 1997; 11 : 3319–26. [Google Scholar]

[16] McCracken S, Fong N, Rosonina E, et al. 5’-Capping enzymes are targeted to pre-mRNA by binding to the phosphorylated carboxy-terminal domain of RNA polymerase II. Genes Dev 1997; 11 : 3306–18. [Google Scholar]