메뉴 건너뛰기




Volumn 30, Issue 1, 2016, Pages 117-131

P-TEFb regulation of transcription termination factor Xrn2 revealed by a chemical genetic screen for Cdk9 substrates

Author keywords

Chemical genetics; P TEFb; Protein phosphorylation; RNA polymerase II; Transcription termination; Xrn2

Indexed keywords

CYCLIN DEPENDENT KINASE 9; EXORIBONUCLEASE; POSITIVE TRANSCRIPTION ELONGATION FACTOR B; RNA; TRANSCRIPTION FACTOR; TRANSCRIPTION TERMINATION FACTOR XRN2; UNCLASSIFIED DRUG; CHROMATIN; PROTEIN BINDING; XRN2 PROTEIN, HUMAN;

EID: 84953381916     PISSN: 08909369     EISSN: 15495477     Source Type: Journal    
DOI: 10.1101/gad.269589.115     Document Type: Article
Times cited : (96)

References (64)
  • 1
    • 0034405427 scopus 로고    scopus 로고
    • Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry
    • Ajuh P, Kuster B, Panov K, Zomerdijk JC, Mann M, Lamond AI. 2000. Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry. EMBO J 19: 6569-6581.
    • (2000) EMBO J , vol.19 , pp. 6569-6581
    • Ajuh, P.1    Kuster, B.2    Panov, K.3    Zomerdijk, J.C.4    Mann, M.5    Lamond, A.I.6
  • 2
    • 0035415869 scopus 로고    scopus 로고
    • Chemical genetic approaches for the elucidation of signaling pathways
    • Alaimo PJ, Shogren-Knaak MA, Shokat KM. 2001. Chemical genetic approaches for the elucidation of signaling pathways. Curr Opin Chem Biol 5: 360-367.
    • (2001) Curr Opin Chem Biol , vol.5 , pp. 360-367
    • Alaimo, P.J.1    Shogren-Knaak, M.A.2    Shokat, K.M.3
  • 4
    • 70349558526 scopus 로고    scopus 로고
    • Identification of flavopiridol analogues that selectively inhibit positive transcription elongation factor (P-TEFb) and block HIV-1 replication
    • Ali A, Ghosh A, Nathans RS, Sharova N, O'Brien S, Cao H, Stevenson M, Rana TM. 2009. Identification of flavopiridol analogues that selectively inhibit positive transcription elongation factor (P-TEFb) and block HIV-1 replication. Chembiochem 10: 2072-2080.
    • (2009) Chembiochem , vol.10 , pp. 2072-2080
    • Ali, A.1    Ghosh, A.2    Nathans, R.S.3    Sharova, N.4    O'Brien, S.5    Cao, H.6    Stevenson, M.7    Rana, T.M.8
  • 8
    • 33846522525 scopus 로고    scopus 로고
    • The mixed-lineage leukemia fusion partner AF4 stimulates RNA polymerase II transcriptional elongation and mediates coordinated chromatin remodeling
    • Bitoun E, Oliver PL, Davies KE. 2007. The mixed-lineage leukemia fusion partner AF4 stimulates RNA polymerase II transcriptional elongation and mediates coordinated chromatin remodeling. Hum Mol Genet 16: 92-106.
    • (2007) Hum Mol Genet , vol.16 , pp. 92-106
    • Bitoun, E.1    Oliver, P.L.2    Davies, K.E.3
  • 9
    • 40349092941 scopus 로고    scopus 로고
    • Covalent capture of kinase-specific phosphopeptides reveals Cdk1-cyclin B substrates
    • Blethrow JD, Glavy JS, Morgan DO, Shokat KM. 2008. Covalent capture of kinase-specific phosphopeptides reveals Cdk1-cyclin B substrates. Proc Natl Acad Sci 105: 1442-1447.
    • (2008) Proc Natl Acad Sci , vol.105 , pp. 1442-1447
    • Blethrow, J.D.1    Glavy, J.S.2    Morgan, D.O.3    Shokat, K.M.4
  • 13
    • 79952362044 scopus 로고    scopus 로고
    • Structural and biochemical studies of the 5 ′→3′ exoribonuclease Xrn1
    • Chang JH, Xiang S, Xiang K, Manley JL, Tong L. 2011. Structural and biochemical studies of the 5 ′→3′ exoribonuclease Xrn1. Nat Struct Mol Biol 18: 270-276.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 270-276
    • Chang, J.H.1    Xiang, S.2    Xiang, K.3    Manley, J.L.4    Tong, L.5
  • 14
    • 0035943710 scopus 로고    scopus 로고
    • Flavopiridol inactivates P-TEFb and blocks most RNA polymerase II transcription in vivo
    • Chao SH, Price DH. 2001. Flavopiridol inactivates P-TEFb and blocks most RNA polymerase II transcription in vivo. J Biol Chem 276: 31793-31799.
    • (2001) J Biol Chem , vol.276 , pp. 31793-31799
    • Chao, S.H.1    Price, D.H.2
  • 16
    • 84861905610 scopus 로고    scopus 로고
    • Co-transcriptional degradation of aberrant pre-mRNA by Xrn2
    • Davidson L, Kerr A,West S. 2012. Co-transcriptional degradation of aberrant pre-mRNA by Xrn2. EMBO J 31: 2566-2578.
    • (2012) EMBO J , vol.31 , pp. 2566-2578
    • Davidson, L.1    Kerr, A.2    West, S.3
  • 17
    • 84893936668 scopus 로고    scopus 로고
    • 3′ end formation of premRNA and phosphorylation of Ser2 on the RNA polymerase II CTD are reciprocally coupled in human cells
    • Davidson L, Muniz L, West S. 2014. 3′ end formation of premRNA and phosphorylation of Ser2 on the RNA polymerase II CTD are reciprocally coupled in human cells. Genes Dev 28: 342-356.
    • (2014) Genes Dev , vol.28 , pp. 342-356
    • Davidson, L.1    Muniz, L.2    West, S.3
  • 18
    • 69249157270 scopus 로고    scopus 로고
    • Torpedo nuclease Rat1 is insufficient to terminate RNA polymerase II in vitro
    • Dengl S, Cramer P. 2009. Torpedo nuclease Rat1 is insufficient to terminate RNA polymerase II in vitro. J Biol Chem 284: 21270-21279.
    • (2009) J Biol Chem , vol.284 , pp. 21270-21279
    • Dengl, S.1    Cramer, P.2
  • 21
    • 84863032295 scopus 로고    scopus 로고
    • Glucocorticoid-dependent phosphorylation of the transcriptional coregulator GRIP1
    • Dobrovolna J, Chinenov Y, Kennedy MA, Liu B, Rogatsky I. 2012. Glucocorticoid-dependent phosphorylation of the transcriptional coregulator GRIP1. Mol Cell Biol 32: 730-739.
    • (2012) Mol Cell Biol , vol.32 , pp. 730-739
    • Dobrovolna, J.1    Chinenov, Y.2    Kennedy, M.A.3    Liu, B.4    Rogatsky, I.5
  • 22
    • 84946490100 scopus 로고    scopus 로고
    • SMADsandYAP compete to control elongation of β-catenin:LEF-1-recruited RNAPII during hESC differentiation
    • Estaras C, Benner C, Jones KA. 2015.SMADsandYAP compete to control elongation of β-catenin:LEF-1-recruited RNAPII during hESC differentiation. Mol Cell 58: 780-793.
    • (2015) Mol Cell , vol.58 , pp. 780-793
    • Estaras, C.1    Benner, C.2    Jones, K.A.3
  • 23
    • 29144481702 scopus 로고    scopus 로고
    • Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping
    • Fenger-Gron M, Fillman C, Norrild B, Lykke-Andersen J. 2005. Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping. Mol Cell 20: 905-915.
    • (2005) Mol Cell , vol.20 , pp. 905-915
    • Fenger-Gron, M.1    Fillman, C.2    Norrild, B.3    Lykke-Andersen, J.4
  • 24
    • 84944887484 scopus 로고    scopus 로고
    • Effects of transcription elongation rate and Xrn2 exonuclease activity on RNA polymerase II termination suggest widespread kinetic competition
    • Fong N, Brannan K, Erickson B, Kim H, Cortazar MA, Sheridan RM, Nguyen T, Karp S, Bentley DL. 2015. Effects of transcription elongation rate and Xrn2 exonuclease activity on RNA polymerase II termination suggest widespread kinetic competition. Mol Cell 60: 256-267.
    • (2015) Mol Cell , vol.60 , pp. 256-267
    • Fong, N.1    Brannan, K.2    Erickson, B.3    Kim, H.4    Cortazar, M.A.5    Sheridan, R.M.6    Nguyen, T.7    Karp, S.8    Bentley, D.L.9
  • 25
    • 0346095303 scopus 로고    scopus 로고
    • Dynamics of human immunodeficiency virus transcription: P-TEFb phosphorylates RD and dissociates negative effectors from the transactivation response element
    • Fujinaga K, Irwin D, Huang Y, Taube R, Kurosu T, Peterlin BM. 2004. Dynamics of human immunodeficiency virus transcription: P-TEFb phosphorylates RD and dissociates negative effectors from the transactivation response element. Mol Cell Biol 24: 787-795.
    • (2004) Mol Cell Biol , vol.24 , pp. 787-795
    • Fujinaga, K.1    Irwin, D.2    Huang, Y.3    Taube, R.4    Kurosu, T.5    Peterlin, B.M.6
  • 27
    • 70350442978 scopus 로고    scopus 로고
    • TFIIH-associated Cdk7 kinase functions in phosphorylation of C-terminal domain Ser7 residues, promoter-proximal pausing, and termination by RNA polymerase II
    • Glover-Cutter K, Larochelle S, Erickson B, Zhang C, Shokat K, Fisher RP, Bentley DL. 2009. TFIIH-associated Cdk7 kinase functions in phosphorylation of C-terminal domain Ser7 residues, promoter-proximal pausing, and termination by RNA polymerase II. Mol Cell Biol 29: 5455-5464.
    • (2009) Mol Cell Biol , vol.29 , pp. 5455-5464
    • Glover-Cutter, K.1    Larochelle, S.2    Erickson, B.3    Zhang, C.4    Shokat, K.5    Fisher, R.P.6    Bentley, D.L.7
  • 28
    • 33644787084 scopus 로고    scopus 로고
    • Gene-specific requirement for P-TEFb activity and RNA polymerase II phosphorylation within the p53 transcriptional program
    • Gomes NP, Bjerke G, Llorente B, Szostek SA, Emerson BM, Espinosa JM. 2006. Gene-specific requirement for P-TEFb activity and RNA polymerase II phosphorylation within the p53 transcriptional program. Genes Dev 20: 601-612.
    • (2006) Genes Dev , vol.20 , pp. 601-612
    • Gomes, N.P.1    Bjerke, G.2    Llorente, B.3    Szostek, S.A.4    Emerson, B.M.5    Espinosa, J.M.6
  • 29
    • 84867160564 scopus 로고    scopus 로고
    • The RNA polymerase II CTD coordinates transcription and RNA processing
    • Hsin JP, Manley JL. 2012. The RNA polymerase II CTD coordinates transcription and RNA processing. Genes Dev 26: 2119-2137.
    • (2012) Genes Dev , vol.26 , pp. 2119-2137
    • Hsin, J.P.1    Manley, J.L.2
  • 30
    • 80555125095 scopus 로고    scopus 로고
    • RNAP II CTD phosphorylated on threonine-4 is required for histone mRNA 3′ end processing
    • Hsin JP, Sheth A, Manley JL. 2011. RNAP II CTD phosphorylated on threonine-4 is required for histone mRNA 3′ end processing. Science 334: 683-686.
    • (2011) Science , vol.334 , pp. 683-686
    • Hsin, J.P.1    Sheth, A.2    Manley, J.L.3
  • 31
    • 23744514308 scopus 로고    scopus 로고
    • The bromodomain protein Brd4 is a positive regulatory component of P-TEFb and stimulates RNA polymerase II-dependent transcription
    • Jang MK, Mochizuki K, Zhou M, Jeong HS, Brady JN, Ozato K. 2005. The bromodomain protein Brd4 is a positive regulatory component of P-TEFb and stimulates RNA polymerase II-dependent transcription. Mol Cell 19: 523-534.
    • (2005) Mol Cell , vol.19 , pp. 523-534
    • Jang, M.K.1    Mochizuki, K.2    Zhou, M.3    Jeong, H.S.4    Brady, J.N.5    Ozato, K.6
  • 32
    • 34447321025 scopus 로고    scopus 로고
    • Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme
    • Jeronimo C, Forget D, Bouchard A, Li Q, Chua G, Poitras C, Therien C, Bergeron D, Bourassa S, Greenblatt J, et al. 2007. Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme. Mol Cell 27: 262-274.
    • (2007) Mol Cell , vol.27 , pp. 262-274
    • Jeronimo, C.1    Forget, D.2    Bouchard, A.3    Li, Q.4    Chua, G.5    Poitras, C.6    Therien, C.7    Bergeron, D.8    Bourassa, S.9    Greenblatt, J.10
  • 33
    • 79951969817 scopus 로고    scopus 로고
    • Coupled 5′ nucleotide recognition and processivity in Xrn1-mediated mRNA decay
    • Jinek M, Coyle SM, Doudna JA. 2011. Coupled 5′ nucleotide recognition and processivity in Xrn1-mediated mRNA decay. Mol Cell 41: 600-608.
    • (2011) Mol Cell , vol.41 , pp. 600-608
    • Jinek, M.1    Coyle, S.M.2    Doudna, J.A.3
  • 34
    • 0035853736 scopus 로고    scopus 로고
    • Positive transcription elongation factor B phosphorylates hSPT5 and RNA polymerase II carboxyl-terminal domain independently of cyclin-dependent kinase-activating kinase
    • Kim JB, Sharp PA. 2001. Positive transcription elongation factor B phosphorylates hSPT5 and RNA polymerase II carboxyl-terminal domain independently of cyclin-dependent kinase-activating kinase. J Biol Chem 276: 12317-12323.
    • (2001) J Biol Chem , vol.276 , pp. 12317-12323
    • Kim, J.B.1    Sharp, P.A.2
  • 35
    • 1542290655 scopus 로고    scopus 로고
    • Transitions in RNA polymerase II elongation complexes at the 3′ ends of genes
    • Kim M, Ahn SH, Krogan NJ, Greenblatt JF, Buratowski S. 2004a. Transitions in RNA polymerase II elongation complexes at the 3′ ends of genes. EMBO J 23: 354-364.
    • (2004) EMBO J , vol.23 , pp. 354-364
    • Kim, M.1    Ahn, S.H.2    Krogan, N.J.3    Greenblatt, J.F.4    Buratowski, S.5
  • 37
    • 0029891101 scopus 로고    scopus 로고
    • The structure and function of proteins involved in mammalian pre-mRNA splicing
    • Kramer A. 1996. The structure and function of proteins involved in mammalian pre-mRNA splicing. Annu Rev Biochem 65: 367-409.
    • (1996) Annu Rev Biochem , vol.65 , pp. 367-409
    • Kramer, A.1
  • 38
    • 84929161687 scopus 로고    scopus 로고
    • CDK9 inhibitors define elongation checkpoints at both ends of RNA polymerase II-transcribed genes
    • Laitem C, Zaborowska J, Isa NF, Kufs J, Dienstbier M, Murphy S. 2015. CDK9 inhibitors define elongation checkpoints at both ends of RNA polymerase II-transcribed genes. Nat Struct Mol Biol 22: 396-403.
    • (2015) Nat Struct Mol Biol , vol.22 , pp. 396-403
    • Laitem, C.1    Zaborowska, J.2    Isa, N.F.3    Kufs, J.4    Dienstbier, M.5    Murphy, S.6
  • 42
    • 23344437022 scopus 로고    scopus 로고
    • Analysis of the large inactive P-TEFb complex indicates that it contains one 7SK molecule, a dimer of HEXIM1 or HEXIM2, and two P-TEFb molecules containing Cdk9 phosphorylated at threonine 186
    • Li Q, Price JP, Byers SA, Cheng D, Peng J, Price DH. 2005. Analysis of the large inactive P-TEFb complex indicates that it contains one 7SK molecule, a dimer of HEXIM1 or HEXIM2, and two P-TEFb molecules containing Cdk9 phosphorylated at threonine 186. J Biol Chem 280: 28819-28826.
    • (2005) J Biol Chem , vol.280 , pp. 28819-28826
    • Li, Q.1    Price, J.P.2    Byers, S.A.3    Cheng, D.4    Peng, J.5    Price, D.H.6
  • 44
  • 45
    • 33645844251 scopus 로고    scopus 로고
    • The role of Rat1 in coupling mRNA 3′-end processing to transcription termination: Implications for a unified allosteric-torpedo model
    • Luo W, Johnson AW, Bentley DL. 2006. The role of Rat1 in coupling mRNA 3′-end processing to transcription termination: implications for a unified allosteric-torpedo model. Genes Dev 20: 954-965.
    • (2006) Genes Dev , vol.20 , pp. 954-965
    • Luo, W.1    Johnson, A.W.2    Bentley, D.L.3
  • 46
    • 60749109846 scopus 로고    scopus 로고
    • Cell cycle, CDKs and cancer: A changing paradigm
    • Malumbres M, Barbacid M. 2009. Cell cycle, CDKs and cancer: a changing paradigm. Nat Rev Cancer 9: 153-166.
    • (2009) Nat Rev Cancer , vol.9 , pp. 153-166
    • Malumbres, M.1    Barbacid, M.2
  • 47
    • 0029959881 scopus 로고    scopus 로고
    • Control of RNA polymerase II elongation potential by a novel carboxyl-terminal domain kinase
    • Marshall NF, Peng J, Xie Z, Price DH. 1996. Control of RNA polymerase II elongation potential by a novel carboxyl-terminal domain kinase. J Biol Chem 271: 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
  • 48
    • 84892859771 scopus 로고    scopus 로고
    • PAXT-1 promotes XRN2 activity by stabilizing it through a conserved domain
    • Miki TS, Richter H, Ruegger S, Grosshans H. 2014. PAXT-1 promotes XRN2 activity by stabilizing it through a conserved domain. Mol Cell 53: 351-360.
    • (2014) Mol Cell , vol.53 , pp. 351-360
    • Miki, T.S.1    Richter, H.2    Ruegger, S.3    Grosshans, H.4
  • 49
    • 84883186457 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein (HnRNP) K genome-wide binding survey reveals its role in regulating 3′-end RNA processing and transcription termination at the early growth response 1 (EGR1) gene through XRN2 exonuclease
    • Mikula M, Bomsztyk K, Goryca K, Chojnowski K, Ostrowski J. 2013. Heterogeneous nuclear ribonucleoprotein (HnRNP) K genome-wide binding survey reveals its role in regulating 3′-end RNA processing and transcription termination at the early growth response 1 (EGR1) gene through XRN2 exonuclease. J Biol Chem 288: 24788-24798.
    • (2013) J Biol Chem , vol.288 , pp. 24788-24798
    • Mikula, M.1    Bomsztyk, K.2    Goryca, K.3    Chojnowski, K.4    Ostrowski, J.5
  • 50
    • 0037226818 scopus 로고    scopus 로고
    • DNA replication-dependent nuclear dynamics of the Mre11 complex
    • Mirzoeva OK, Petrini JH. 2003. DNA replication-dependent nuclear dynamics of the Mre11 complex. Mol Cancer Res 1: 207-218.
    • (2003) Mol Cancer Res , vol.1 , pp. 207-218
    • Mirzoeva, O.K.1    Petrini, J.H.2
  • 51
    • 78650566210 scopus 로고    scopus 로고
    • Pol II waiting in the starting gates: Regulating the transition from transcription initiation into productive elongation
    • Nechaev S, Adelman K. 2011. Pol II waiting in the starting gates: regulating the transition from transcription initiation into productive elongation. Biochim Biophys Acta 1809: 34-45.
    • (2011) Biochim Biophys Acta , vol.1809 , pp. 34-45
    • Nechaev, S.1    Adelman, K.2
  • 52
    • 84880048366 scopus 로고    scopus 로고
    • Dismantling promoter-driven RNA polymerase II transcription complexes in vitro by the termination factor Rat1
    • Pearson EL, Moore CL. 2013. Dismantling promoter-driven RNA polymerase II transcription complexes in vitro by the termination factor Rat1. J Biol Chem 288: 19750-19759.
    • (2013) J Biol Chem , vol.288 , pp. 19750-19759
    • Pearson, E.L.1    Moore, C.L.2
  • 53
    • 0031587993 scopus 로고    scopus 로고
    • Structural modifications of RNA influence the 5′ exoribonucleolytic hydrolysis by XRN1 and HKE1 of Saccharomyces cerevisiae
    • Poole TL, Stevens A. 1997. Structural modifications of RNA influence the 5′ exoribonucleolytic hydrolysis by XRN1 and HKE1 of Saccharomyces cerevisiae. Biochem Biophys Res Commun 235: 799-805.
    • (1997) Biochem Biophys Res Commun , vol.235 , pp. 799-805
    • Poole, T.L.1    Stevens, A.2
  • 54
  • 55
    • 84887979292 scopus 로고    scopus 로고
    • Modelling the CDK-dependent transcription cycle in fission yeast
    • Sansó M, Fisher RP. 2013. Modelling the CDK-dependent transcription cycle in fission yeast. Biochem Soc Trans 41: 1660-1665.
    • (2013) Biochem Soc Trans , vol.41 , pp. 1660-1665
    • Sansó, M.1    Fisher, R.P.2
  • 56
    • 84861872358 scopus 로고    scopus 로고
    • Phosphorylation by cyclin-dependent kinase-9 controls ubiquitin- conjugating enzyme-2A function
    • Shchebet A, Karpiuk O, Kremmer E, Eick D, Johnsen SA. 2012. Phosphorylation by cyclin-dependent kinase-9 controls ubiquitin- conjugating enzyme-2A function. Cell Cycle 11: 2122- 2127.
    • (2012) Cell Cycle , vol.11 , pp. 2122-2127
    • Shchebet, A.1    Karpiuk, O.2    Kremmer, E.3    Eick, D.4    Johnsen, S.A.5
  • 59
    • 0037121926 scopus 로고    scopus 로고
    • Human Dcp2: A catalytically active mRNA decapping enzyme located in specific cytoplasmic structures
    • van Dijk E, Cougot N, Meyer S, Babajko S, Wahle E, Seraphin B. 2002. Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures. EMBO J 21: 6915-6924.
    • (2002) EMBO J , vol.21 , pp. 6915-6924
    • van Dijk, E.1    Cougot, N.2    Meyer, S.3    Babajko, S.4    Wahle, E.5    Seraphin, B.6
  • 61
    • 9644308046 scopus 로고    scopus 로고
    • Human 5′ →3′ exonuclease Xrn2 promotes transcription termination at co-transcriptional cleavage sites
    • West S, Gromak N, Proudfoot NJ. 2004. Human 5′ →3′ exonuclease Xrn2 promotes transcription termination at co-transcriptional cleavage sites. Nature 432: 522-525.
    • (2004) Nature , vol.432 , pp. 522-525
    • West, S.1    Gromak, N.2    Proudfoot, N.J.3
  • 62
    • 64749111945 scopus 로고    scopus 로고
    • Structure and function of the 5 ′→3′ exoribonuclease Rat1 and its activating partner Rai1
    • Xiang S, Cooper-Morgan A, Jiao X, Kiledjian M, Manley JL, Tong L. 2009. Structure and function of the 5 ′→3′ exoribonuclease Rat1 and its activating partner Rai1. Nature 458: 784-788.
    • (2009) Nature , vol.458 , pp. 784-788
    • Xiang, S.1    Cooper-Morgan, A.2    Jiao, X.3    Kiledjian, M.4    Manley, J.L.5    Tong, L.6
  • 63
    • 30744449491 scopus 로고    scopus 로고
    • P-TEFb-mediated phosphorylation of hSpt5 C-terminal repeats is critical for processive transcription elongation
    • Yamada T, Yamaguchi Y, Inukai N, Okamoto S, Mura T, Handa H. 2006. P-TEFb-mediated phosphorylation of hSpt5 C-terminal repeats is critical for processive transcription elongation. Mol Cell 21: 227-237.
    • (2006) Mol Cell , vol.21 , pp. 227-237
    • Yamada, T.1    Yamaguchi, Y.2    Inukai, N.3    Okamoto, S.4    Mura, T.5    Handa, H.6
  • 64
    • 23744467035 scopus 로고    scopus 로고
    • Recruitment of P-TEFb for stimulation of transcriptional elongation by the bromodomain protein Brd4
    • Yang Z, Yik JH, Chen R, He N, Jang MK, Ozato K, Zhou Q. 2005. Recruitment of P-TEFb for stimulation of transcriptional elongation by the bromodomain protein Brd4. Mol Cell 19: 535-545.
    • (2005) Mol Cell , vol.19 , pp. 535-545
    • Yang, Z.1    Yik, J.H.2    Chen, R.3    He, N.4    Jang, M.K.5    Ozato, K.6    Zhou, Q.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.