메뉴 건너뛰기




Volumn 14, Issue 3, 2004, Pages 375-386

Involvement of transcription termination factor 2 in mitotic repression of transcription elongation

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; DNA DIRECTED RNA POLYMERASE; RNA POLYMERASE II; TRANSCRIPTION ELONGATION FACTOR; TRANSCRIPTION FACTOR; TRANSCRIPTION TERMINATION FACTOR 2; UNCLASSIFIED DRUG;

EID: 2342535795     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(04)00234-5     Document Type: Article
Times cited : (50)

References (27)
  • 1
    • 0029939231 scopus 로고    scopus 로고
    • The Mfd protein of Bacillus subtilis 168 is involved in both transcription-coupled DNA repair and DNA recombination
    • Ayora S., Rojo F., Ogasawara N., Nakai S., Alonso J.C. The Mfd protein of Bacillus subtilis 168 is involved in both transcription-coupled DNA repair and DNA recombination. J. Mol. Biol. 256:1996;301-318
    • (1996) J. Mol. Biol. , vol.256 , pp. 301-318
    • Ayora, S.1    Rojo, F.2    Ogasawara, N.3    Nakai, S.4    Alonso, J.C.5
  • 2
    • 0345531143 scopus 로고    scopus 로고
    • A DNA translocation motif in the bacterial transcription-repair coupling factor, Mfd
    • Chambers A.L., Smith A.J., Savery N.J. A DNA translocation motif in the bacterial transcription-repair coupling factor, Mfd. Nucleic Acids Res. 31:2003;6409-6418
    • (2003) Nucleic Acids Res. , vol.31 , pp. 6409-6418
    • Chambers, A.L.1    Smith, A.J.2    Savery, N.J.3
  • 3
    • 0026045991 scopus 로고
    • Chromosome tangling and breakage at anaphase result from mutations in lodestar, a Drosophila gene encoding a putative nucleoside triphosphate-binding protein
    • Girdham C.H., Glover D.M. Chromosome tangling and breakage at anaphase result from mutations in lodestar, a Drosophila gene encoding a putative nucleoside triphosphate-binding protein. Genes Dev. 5:1991;1786-1799
    • (1991) Genes Dev. , vol.5 , pp. 1786-1799
    • Girdham, C.H.1    Glover, D.M.2
  • 4
    • 0030980312 scopus 로고    scopus 로고
    • Mitotic repression of the transcriptional machinery
    • Gottesfeld J.M., Forbes D.J. Mitotic repression of the transcriptional machinery. Trends Biochem. Sci. 22:1997;197-202
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 197-202
    • Gottesfeld, J.M.1    Forbes, D.J.2
  • 5
    • 0033609947 scopus 로고    scopus 로고
    • Human transcription release factor 2 dissociates RNA polymerases I and II stalled at a cyclobutane thymine dimer
    • Hara R., Selby C.P., Liu M., Price D.H., Sancar A. Human transcription release factor 2 dissociates RNA polymerases I and II stalled at a cyclobutane thymine dimer. J. Biol. Chem. 274:1999;24779-24786
    • (1999) J. Biol. Chem. , vol.274 , pp. 24779-24786
    • Hara, R.1    Selby, C.P.2    Liu, M.3    Price, D.H.4    Sancar, A.5
  • 6
    • 0033279823 scopus 로고    scopus 로고
    • Regulation of nuclear localization: A key to a door
    • Kaffman A., O'Shea E.K. Regulation of nuclear localization. a key to a door Annu. Rev. Cell Dev. Biol. 15:1999;291-339
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 291-339
    • Kaffman, A.1    O'Shea, E.K.2
  • 7
    • 0032808150 scopus 로고    scopus 로고
    • Quantitation of RNA polymerase II and its transcription factors in an HeLa cell: Little soluble holoenzyme but significant amounts of polymerases attached to the nuclear substructure
    • Kimura H., Tao Y., Roeder R.G., Cook P.R. Quantitation of RNA polymerase II and its transcription factors in an HeLa cell. little soluble holoenzyme but significant amounts of polymerases attached to the nuclear substructure Mol. Cell. Biol. 19:1999;5383-5392
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5383-5392
    • Kimura, H.1    Tao, Y.2    Roeder, R.G.3    Cook, P.R.4
  • 9
    • 0032476005 scopus 로고    scopus 로고
    • A human RNA polymerase II transcription termination factor is a SWI2/SNF2 family member
    • Liu M., Xie Z., Price D.H. A human RNA polymerase II transcription termination factor is a SWI2/SNF2 family member. J. Biol. Chem. 273:1998;25541-25544
    • (1998) J. Biol. Chem. , vol.273 , pp. 25541-25544
    • Liu, M.1    Xie, Z.2    Price, D.H.3
  • 10
    • 0037415719 scopus 로고    scopus 로고
    • A model for dsDNA translocation revealed by a structural motif common to RecG and Mfd proteins
    • Mahdi A.A., Briggs G.S., Sharples G.J., Wen Q., Lloyd R.G. A model for dsDNA translocation revealed by a structural motif common to RecG and Mfd proteins. EMBO J. 22:2003;724-734
    • (2003) EMBO J. , vol.22 , pp. 724-734
    • Mahdi, A.A.1    Briggs, G.S.2    Sharples, G.J.3    Wen, Q.4    Lloyd, R.G.5
  • 11
    • 0026725368 scopus 로고
    • Control of formation of two distinct classes of RNA polymerase II elongation complexes
    • Marshall N.F., Price D.H. Control of formation of two distinct classes of RNA polymerase II elongation complexes. Mol. Cell. Biol. 12:1992;2078-2090
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2078-2090
    • Marshall, N.F.1    Price, D.H.2
  • 12
    • 0029011873 scopus 로고
    • Purification of P-TEFb, a transcription factor required for the transition into productive elongation
    • Marshall N.F., Price D.H. Purification of P-TEFb, a transcription factor required for the transition into productive elongation. J. Biol. Chem. 270:1995;12335-12338
    • (1995) J. Biol. Chem. , vol.270 , pp. 12335-12338
    • Marshall, N.F.1    Price, D.H.2
  • 13
    • 0029959881 scopus 로고    scopus 로고
    • Control of RNA polymerase II elongation potential by a novel carboxyl-terminal domain kinase
    • Marshall N.F., Peng J., Xie Z., Price D.H. Control of RNA polymerase II elongation potential by a novel carboxyl-terminal domain kinase. J. Biol. Chem. 271:1996;27176-27183
    • (1996) J. Biol. Chem. , vol.271 , pp. 27176-27183
    • Marshall, N.F.1    Peng, J.2    Xie, Z.3    Price, D.H.4
  • 14
    • 0037077154 scopus 로고    scopus 로고
    • E. coli transcription repair coupling factor (Mfd protein) rescues arrested complexes by promoting forward translocation
    • Park J.S., Marr M.T., Roberts J.W. E. coli transcription repair coupling factor (Mfd protein) rescues arrested complexes by promoting forward translocation. Cell. 109:2002;757-767
    • (2002) Cell , vol.109 , pp. 757-767
    • Park, J.S.1    Marr, M.T.2    Roberts, J.W.3
  • 15
    • 0030813559 scopus 로고    scopus 로고
    • Mitotic repression of RNA polymerase II transcription is accompanied by release of transcription elongation complexes
    • Parsons G.G., Spencer C.A. Mitotic repression of RNA polymerase II transcription is accompanied by release of transcription elongation complexes. Mol. Cell. Biol. 17:1997;5791-5802
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5791-5802
    • Parsons, G.G.1    Spencer, C.A.2
  • 17
    • 0032031706 scopus 로고    scopus 로고
    • Identification of multiple cyclin subunits of human P-TEFb
    • b
    • Peng J., Zhu Y., Milton J.T., Price D.H. Identification of multiple cyclin subunits of human P-TEFb. Genes Dev. 12:1998;755-762. b
    • (1998) Genes Dev. , vol.12 , pp. 755-762
    • Peng, J.1    Zhu, Y.2    Milton, J.T.3    Price, D.H.4
  • 18
    • 0034111019 scopus 로고    scopus 로고
    • P-TEFb, a cyclin-dependent kinase controlling elongation by RNA polymerase II
    • Price D.H. P-TEFb, a cyclin-dependent kinase controlling elongation by RNA polymerase II. Mol. Cell. Biol. 20:2000;2629-2634
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2629-2634
    • Price, D.H.1
  • 19
    • 0029829364 scopus 로고    scopus 로고
    • Mitotic regulation of TFIID: Inhibition of activator-dependent transcription and changes in subcellular localization
    • Segil N., Guermah M., Hoffmann A., Roeder R.G., Heintz N. Mitotic regulation of TFIID. inhibition of activator-dependent transcription and changes in subcellular localization Genes Dev. 10:1996;2389-2400
    • (1996) Genes Dev. , vol.10 , pp. 2389-2400
    • Segil, N.1    Guermah, M.2    Hoffmann, A.3    Roeder, R.G.4    Heintz, N.5
  • 20
    • 0026006495 scopus 로고
    • Progression of the cell cycle through mitosis leads to abortion of nascent transcripts
    • Shermoen A.W., O'Farrell P.H. Progression of the cell cycle through mitosis leads to abortion of nascent transcripts. Cell. 67:1991;303-310
    • (1991) Cell , vol.67 , pp. 303-310
    • Shermoen, A.W.1    O'Farrell, P.H.2
  • 21
    • 0037102566 scopus 로고    scopus 로고
    • CDK-9/cyclin T (P-TEFb) is required in two postinitiation pathways for transcription in the C. elegans embryo
    • Shim E.Y., Walker A.K., Shi Y., Blackwell T.K. CDK-9/cyclin T (P-TEFb) is required in two postinitiation pathways for transcription in the C. elegans embryo. Genes Dev. 16:2002;2135-2146
    • (2002) Genes Dev. , vol.16 , pp. 2135-2146
    • Shim, E.Y.1    Walker, A.K.2    Shi, Y.3    Blackwell, T.K.4
  • 22
    • 0034631951 scopus 로고    scopus 로고
    • Mitotic transcription repression in vivo in the absence of nucleosomal chromatin condensation
    • Spencer C.A., Kruhlak M.J., Jenkins H.L., Sun X.J., Bazett-Jones D.P. Mitotic transcription repression in vivo in the absence of nucleosomal chromatin condensation. J. Cell Biol. 150:2000;13-26
    • (2000) J. Cell Biol. , vol.150 , pp. 13-26
    • Spencer, C.A.1    Kruhlak, M.J.2    Jenkins, H.L.3    Sun, X.J.4    Bazett-Jones, D.P.5
  • 23
    • 0000335917 scopus 로고
    • Nucleic acid synthesis in relation to the cell division cycle
    • Taylor J. Nucleic acid synthesis in relation to the cell division cycle. Ann. NY Acad. Sci. 90:1960;409-421
    • (1960) Ann. NY Acad. Sci. , vol.90 , pp. 409-421
    • Taylor, J.1
  • 24
    • 0037716599 scopus 로고    scopus 로고
    • Role of E. coli transcription-repair coupling factor Mfd in Nun-mediated transcription termination
    • Washburn R.S., Wang Y., Gottesman M.E. Role of E. coli transcription-repair coupling factor Mfd in Nun-mediated transcription termination. J. Mol. Biol. 329:2003;655-662
    • (2003) J. Mol. Biol. , vol.329 , pp. 655-662
    • Washburn, R.S.1    Wang, Y.2    Gottesman, M.E.3
  • 25
    • 15844396178 scopus 로고    scopus 로고
    • Purification of an RNA polymerase II transcript release factor from Drosophila
    • Xie Z., Price D.H. Purification of an RNA polymerase II transcript release factor from Drosophila. J. Biol. Chem. 271:1996;11043-11046
    • (1996) J. Biol. Chem. , vol.271 , pp. 11043-11046
    • Xie, Z.1    Price, D.H.2
  • 26
    • 0031438709 scopus 로고    scopus 로고
    • Drosophila factor 2, an RNA polymerase II transcript release factor, has DNA-dependent ATPase activity
    • Xie Z., Price D. Drosophila factor 2, an RNA polymerase II transcript release factor, has DNA-dependent ATPase activity. J. Biol. Chem. 272:1997;31902-31907
    • (1997) J. Biol. Chem. , vol.272 , pp. 31902-31907
    • Xie, Z.1    Price, D.2
  • 27
    • 0032488913 scopus 로고    scopus 로고
    • Unusual nucleic acid binding properties of factor 2, an RNA polymerase II transcript release factor
    • Xie Z., Price D.H. Unusual nucleic acid binding properties of factor 2, an RNA polymerase II transcript release factor. J. Biol. Chem. 273:1998;3771-3777
    • (1998) J. Biol. Chem. , vol.273 , pp. 3771-3777
    • Xie, Z.1    Price, D.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.