메뉴 건너뛰기




Volumn 108, Issue 26, 2011, Pages 10484-10489

Structural and functional characterization of an atypical activation domain in erythroid Krüppel-like factor (EKLF)

Author keywords

Hematopoiesis; Intrinsically unstructured domain; NMR spectroscopy; Transcription factor IIE; Transcriptional activators

Indexed keywords

CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN BINDING PROTEIN; ERYTHROID KRUPPEL LIKE FACTOR;

EID: 79960600766     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1017029108     Document Type: Article
Times cited : (47)

References (48)
  • 1
    • 0035860820 scopus 로고    scopus 로고
    • Kruppel-like factors: Three fingers in many pies
    • Bieker JJ (2001) Kruppel-like factors: Three fingers in many pies. J Biol Chem 276:34355-34358.
    • (2001) J Biol Chem , vol.276 , pp. 34355-34358
    • Bieker, J.J.1
  • 2
    • 0037218919 scopus 로고    scopus 로고
    • Sp1- and Kruppel-like transcription factors
    • Kaczynski J, Cook T, Urrutia R (2003) Sp1- and Kruppel-like transcription factors. Genome Biol 4(2):206.
    • (2003) Genome Biol , vol.4 , Issue.2 , pp. 206
    • Kaczynski, J.1    Cook, T.2    Urrutia, R.3
  • 3
    • 0027211845 scopus 로고
    • A novel, erythroid cell-specific murine transcription factor that binds to the CACCC element and is related to the Kruppel family of nuclear proteins
    • Miller IJ, Bieker JJ (1993) A novel, erythroid cell-specific murine transcription factor that binds the CACCC element and is related to the Kruppel family of nuclear proteins. Mol Cell Biol 13:2776-2786. (Pubitemid 23133950)
    • (1993) Molecular and Cellular Biology , vol.13 , Issue.5 , pp. 2776-2786
    • Miller, I.J.1    Bieker, J.J.2
  • 4
    • 33645743530 scopus 로고    scopus 로고
    • A global role for EKLF in definitive and primitive erythropoiesis
    • Hodge D, et al. (2006) A global role for EKLF in definitive and primitive erythropoiesis. Blood 107:3359-3370.
    • (2006) Blood , vol.107 , pp. 3359-3370
    • Hodge, D.1
  • 5
    • 0028990264 scopus 로고
    • Lethal beta-thalassaemia in mice lacking the erythroid CACCC-transcription factor EKLF
    • Perkins AC, Sharpe AH, Orkin SH (1995) Lethal beta-thalassaemia in mice lacking the erythroid CACCC-transcription factor EKLF. Nature 375:318-322.
    • (1995) Nature , vol.375 , pp. 318-322
    • Perkins, A.C.1    Sharpe, A.H.2    Orkin, S.H.3
  • 6
    • 0029010790 scopus 로고
    • Defective haematopoiesis in fetal liver resulting from inactivation of the EKLF gene
    • Nuez B, Michalovich D, Bygrave A, Ploemacher R, Grosveld F (1995) Defective haematopoiesis in fetal liver resulting from inactivation of the EKLF gene. Nature 375 (6529):316-318.
    • (1995) Nature , vol.375 , Issue.6529 , pp. 316-318
    • Nuez, B.1    Michalovich, D.2    Bygrave, A.3    Ploemacher, R.4    Grosveld, F.5
  • 8
    • 77956622584 scopus 로고    scopus 로고
    • Haploinsufficiency for the erythroid transcription factor KLF1 causes hereditary persistence of fetal hemoglobin
    • Borg J, et al. (2010) Haploinsufficiency for the erythroid transcription factor KLF1 causes hereditary persistence of fetal hemoglobin. Nat Genet 42(9):801-U100.
    • (2010) Nat Genet , vol.42 , Issue.9
    • Borg, J.1
  • 9
    • 77956630402 scopus 로고    scopus 로고
    • KLF1 regulates BCL11A expression and gamma- to beta-globin gene switching
    • Zhou DW, Liu KM, Sun CW, Pawlik KM, Townes TM (2010) KLF1 regulates BCL11A expression and gamma- to beta-globin gene switching. Nat Genet 42(9):742-744.
    • (2010) Nat Genet , vol.42 , Issue.9 , pp. 742-744
    • Zhou, D.W.1    Liu, K.M.2    Sun, C.W.3    Pawlik, K.M.4    Townes, T.M.5
  • 10
    • 0028174097 scopus 로고
    • Analyses of beta-thalassemia mutant DNA interactions with erythroid Kruppel-like factor (EKLF), an erythroid cell-specific transcription factor
    • Feng WC, Southwood CM, Bieker JJ (1994) Analyses of beta-thalassemia mutant DNA interactions with erythroid Kruppel-like factor (EKLF), an erythroid cell-specific transcription factor. J Biol Chem 269:1493-1500.
    • (1994) J Biol Chem , vol.269 , pp. 1493-1500
    • Feng, W.C.1    Southwood, C.M.2    Bieker, J.J.3
  • 11
    • 8644288177 scopus 로고    scopus 로고
    • Stage-specific repression by the EKLF transcriptional activator
    • Chen XY, Bieker JJ (2004) Stage-specific repression by the EKLF transcriptional activator. Mol Cell Biol 24:10416-10424.
    • (2004) Mol Cell Biol , vol.24 , pp. 10416-10424
    • Chen, X.Y.1    Bieker, J.J.2
  • 12
    • 0032544123 scopus 로고    scopus 로고
    • Acetylation and modulation of erythroid Kruppel-like factor (EKLF) activity by interaction with histone acetyltransferases
    • Zhang W, Bieker JJ (1998) Acetylation and modulation of erythroid Kruppel-like factor (EKLF) activity by interaction with histone acetyltransferases. Proc Natl Acad Sci USA 95:9855-9860.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 9855-9860
    • Zhang, W.1    Bieker, J.J.2
  • 13
    • 0035099483 scopus 로고    scopus 로고
    • Site-specific acetylation by p300 or CREB binding protein regulates erythroid Kruppel-like factor transcriptional activity via its interaction with the SWI-SNF complex
    • DOI 10.1128/MCB.21.7.2413-2422.2001
    • Zhang W, Kadam S, Emerson BM, Bieker JJ (2001) Site-specific acetylation by p300 or CREB binding protein regulates erythroid Kruppel-like factor transcriptional activity via its interaction with the SWI-SNF complex. Mol Cell Biol 21:2413-2422. (Pubitemid 32222094)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.7 , pp. 2413-2422
    • Zhang, W.1    Kadam, S.2    Emerson, B.M.3    Bieker, J.J.4
  • 14
    • 53549113643 scopus 로고    scopus 로고
    • Acetylation of EKLF is essential for epigenetic modification and transcriptional activation of the beta-globin locus
    • Sengupta T, Chen K, Milot E, Bieker JJ (2008) Acetylation of EKLF is essential for epigenetic modification and transcriptional activation of the beta-globin locus. Mol Cell Biol 28:6160-6170.
    • (2008) Mol Cell Biol , vol.28 , pp. 6160-6170
    • Sengupta, T.1    Chen, K.2    Milot, E.3    Bieker, J.J.4
  • 15
    • 33747623081 scopus 로고    scopus 로고
    • Lineage-specific activators affect beta-globin locus chromatin in multipotent hematopoietic progenitors
    • DOI 10.1038/sj.emboj.7601232, PII 7601232
    • Bottardi S, Ross J, Pierre-Charles N, Blank V, Milot E (2006) Lineage-specific activators affect beta-globin locus chromatin in multipotent hematopoietic progenitors. EMBO J 25:3586-3595. (Pubitemid 44264869)
    • (2006) EMBO Journal , vol.25 , Issue.15 , pp. 3586-3595
    • Bottardi, S.1    Ross, J.2    Pierre-Charles, N.3    Blank, V.4    Milot, E.5
  • 16
    • 63149139035 scopus 로고    scopus 로고
    • Distinct modes of gene regulation by a cell-specific transcriptional activator
    • Sengupta T, Cohet N, Morle F, Bieker JJ (2009) Distinct modes of gene regulation by a cell-specific transcriptional activator. Proc Natl Acad Sci USA 106:4213-4218.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 4213-4218
    • Sengupta, T.1    Cohet, N.2    Morle, F.3    Bieker, J.J.4
  • 17
    • 0029906977 scopus 로고    scopus 로고
    • Erythroid Kruppel-like factor (EKLF) contains a multifunctional transcriptional activation domain important for inter- and intramolecular interactions
    • Chen X, Bieker JJ (1996) Erythroid Krueppel-like factor (EKLF) contains a multifunctional transcriptional activation domain important for inter- and intramolecular interactions. EMBO J 15:5888-5896. (Pubitemid 26375510)
    • (1996) EMBO Journal , vol.15 , Issue.21 , pp. 5888-5896
    • Chen, X.1    Bieker, J.J.2
  • 18
    • 0032483169 scopus 로고    scopus 로고
    • Regulation of erythroid Kruppel-like factor (EKLF) transcriptional activity by phosphorylation of a protein kinase casein kinase II site within its interaction domain
    • DOI 10.1074/jbc.273.36.23019
    • Ouyang L, Chen X, Bieker JJ (1998) Regulation of erythroid Kruppel-like factor (EKLF) transcriptional activity by phosphorylation of a protein kinase casein kinase II site within its interaction domain. J Biol Chem 273:23019-23025. (Pubitemid 28417480)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.36 , pp. 23019-23025
    • Ouyang, L.1    Chen, X.2    Bieker, J.J.3
  • 19
    • 0025024469 scopus 로고
    • Presence of a potent transcription activating sequence in the p53 protein
    • Fields S, Jang SK (1990) Presence of a potent transcription activating sequence in the p53 protein. Science 249:1046-1049.
    • (1990) Science , vol.249 , pp. 1046-1049
    • Fields, S.1    Jang, S.K.2
  • 20
    • 0026086914 scopus 로고
    • Critical structural elements of the VP16 transcriptional activation domain
    • Cress WD, Triezenberg SJ (1991) Critical structural elements of the VP16 transcriptional activation domain. Science 251:87-90. (Pubitemid 21916859)
    • (1991) Science , vol.251 , Issue.4989 , pp. 87-90
    • Cress, W.D.1    Triezenberg, S.J.2
  • 22
    • 0030864137 scopus 로고    scopus 로고
    • Two tandem and independent sub-activation domains in the amino terminus of p53 require the adaptor complex for activity
    • Candau R, et al. (1997) Two tandem and independent sub-activation domains in the amino terminus of p53 require the adaptor complex for activity. Oncogene 15:807-816. (Pubitemid 27390133)
    • (1997) Oncogene , vol.15 , Issue.7 , pp. 807-816
    • Candau, R.1    Scolnick, D.M.2    Darpino, P.3    Ying, C.Y.4    Halazonetis, T.D.5    Berger, S.L.6
  • 24
    • 66149124079 scopus 로고    scopus 로고
    • Cooperative regulation of p53 by modulation of ternary complex formation with CBP/p300 and HDM2
    • Ferreon JC, et al. (2009) Cooperative regulation of p53 by modulation of ternary complex formation with CBP/p300 and HDM2. Proc Natl Acad Sci USA 106:6591-6596.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 6591-6596
    • Ferreon, J.C.1
  • 26
    • 49449118629 scopus 로고    scopus 로고
    • NMR structure of the complex between the Tfb1 subunit of TFIIH and the activation domain of VP16: Structural similarities between VP16 and p53
    • Langlois C, et al. (2008) NMR structure of the complex between the Tfb1 subunit of TFIIH and the activation domain of VP16: Structural similarities between VP16 and p53. J Am Chem Soc 130:10596-10604.
    • (2008) J Am Chem Soc , vol.130 , pp. 10596-10604
    • Langlois, C.1
  • 27
    • 33745214419 scopus 로고    scopus 로고
    • Structure of the Tfb1/p53 complex: Insights into the interaction between the p62/Tfb1 subunit of TFIIH and the activation domain of p53
    • Di Lello P, et al. (2006) Structure of the Tfb1/p53 complex: Insights into the interaction between the p62/Tfb1 subunit of TFIIH and the activation domain of p53. Mol Cell 22:731-740.
    • (2006) Mol Cell , vol.22 , pp. 731-740
    • Di Lello, P.1
  • 28
    • 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, et al. (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
  • 29
    • 4744373424 scopus 로고    scopus 로고
    • RNA polymerase II carboxy-terminal domain phosphorylation is required for cotranscriptional pre-mRNA splicing and 3'-end formation
    • DOI 10.1128/MCB.24.20.8963-8969.2004
    • Bird G, Zorio DAR, Bentley DL (2004) RNA polymerase II carboxy-terminal domain phosphorylation is required for cotranscriptional pre-mRNA splicing and 3'-end formation. Mol Cell Biol 24:8963-8969. (Pubitemid 39313901)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.20 , pp. 8963-8969
    • Bird, G.1    Zorio, D.A.R.2    Bentley, D.L.3
  • 32
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • DOI 10.1016/S0092-8674(00)80521-8
    • Gu W, Roeder RG (1997) Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 90:595-606. (Pubitemid 27357952)
    • (1997) Cell , vol.90 , Issue.4 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 33
    • 19644388865 scopus 로고    scopus 로고
    • NMR structure of the amino-terminal domain from the Tfb1 subunit of TFIIH and characterization of its phosphoinositide and VP16 binding sites
    • DOI 10.1021/bi050099s
    • Di Lello P, et al. (2005) NMR structure of the amino-terminal domain from the Tfb1 subunit of TFIIH and characterization of its phosphoinositide and VP16 binding sites. Biochemistry 44:7678-7686. (Pubitemid 40740751)
    • (2005) Biochemistry , vol.44 , Issue.21 , pp. 7678-7686
    • Di, L.P.1    Nguyen, B.D.2    Jones, T.N.3    Potempa, K.4    Kobor, M.S.5    Legault, P.6    Omichinski, J.G.7
  • 34
    • 0035896553 scopus 로고    scopus 로고
    • Novel transactivation domain in erythroid Kruppel-like factor (EKLF)
    • Pandya K, Donze D, Townes TM (2001) Novel transactivation domain in erythroid Kruppel-like factor (EKLF). J Biol Chem 276:8239-8243.
    • (2001) J Biol Chem , vol.276 , pp. 8239-8243
    • Pandya, K.1    Donze, D.2    Townes, T.M.3
  • 35
    • 0036132645 scopus 로고    scopus 로고
    • Distinct domains of erythroid Kruppel-like factor modulate chromatin remodeling and transactivation at the endogenous beta-globin gene promoter
    • Brown RC, et al. (2002) Distinct domains of erythroid Kruppel-like factor modulate chromatin remodeling and transactivation at the endogenous beta-globin gene promoter. Mol Cell Biol 22:161-170.
    • (2002) Mol Cell Biol , vol.22 , pp. 161-170
    • Brown, R.C.1
  • 36
    • 65449119145 scopus 로고    scopus 로고
    • Structural basis for recruitment of CBP/p300 coactivators by STAT1 and STAT2 transactivation domains
    • Wojciak JM, Martinez-Yamout MA, Dyson HJ, Wright PE (2009) Structural basis for recruitment of CBP/p300 coactivators by STAT1 and STAT2 transactivation domains. EMBO J 28:948-958.
    • (2009) EMBO J , vol.28 , pp. 948-958
    • Wojciak, J.M.1    Martinez-Yamout, M.A.2    Dyson, H.J.3    Wright, P.E.4
  • 37
    • 69449101615 scopus 로고    scopus 로고
    • Structural basis for subversion of cellular control mechanisms by the adenoviral E1A oncoprotein
    • Ferreon JC, Martinez-Yamout MA, Dyson HJ, Wright PE (2009) Structural basis for subversion of cellular control mechanisms by the adenoviral E1A oncoprotein. Proc Natl Acad Sci USA 106:13260-13265.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 13260-13265
    • Ferreon, J.C.1    Martinez-Yamout, M.A.2    Dyson, H.J.3    Wright, P.E.4
  • 38
    • 1642576027 scopus 로고    scopus 로고
    • Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: Regulation by competition between intrinsically unstructured ligands for non-identical binding sites
    • DOI 10.1074/jbc.M310348200
    • De Guzman RN, Martinez-Yamout MA, Dyson HJ, Wright PE (2004) Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: Regulation by competition between intrinsically unstructured ligands for nonidentical binding sites. J Biol Chem 279:3042-3049. (Pubitemid 38114297)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.4 , pp. 3042-3049
    • De Guzman, R.N.1    Martinez-Yamout, M.A.2    Dyson, H.J.3    Wright, P.E.4
  • 39
    • 41949104574 scopus 로고    scopus 로고
    • Structural insight into the TFIIE-TFIIH interaction: TFIIE and p53 share the binding region on TFIIH
    • DOI 10.1038/emboj.2008.47, PII EMBOJ200847
    • Okuda M, et al. (2008) Structural insight into the TFIIE-TFIIH interaction: TFIIE and p53 share the binding region on TFIIH. EMBO J 27:1161-1171. (Pubitemid 351508156)
    • (2008) EMBO Journal , vol.27 , Issue.7 , pp. 1161-1171
    • Okuda, M.1    Tanaka, A.2    Satoh, M.3    Mizuta, S.4    Takazawa, M.5    Ohkuma, Y.6    Nishimura, Y.7
  • 40
    • 38349084363 scopus 로고    scopus 로고
    • p53 and TFIIEalpha share a common binding site on the Tfb1/p62 subunit of TFIIH
    • Di Lello P, et al. (2008) p53 and TFIIEalpha share a common binding site on the Tfb1/p62 subunit of TFIIH. Proc Natl Acad Sci USA 105:106-111.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 106-111
    • Di Lello, P.1
  • 43
    • 36248983372 scopus 로고    scopus 로고
    • Kruppel-like factor 4 is acetylated by p300 and regulates gene transcription via modulation of histone acetylation
    • DOI 10.1074/jbc.M701847200
    • Evans PM, et al. (2007) Krurppel-like factor 4 is acetylated by p300 and regulates gene transcription via modulation of histone acetylation. J Biol Chem 282:33994-34002. (Pubitemid 350159428)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.47 , pp. 33994-34002
    • Evans, P.M.1    Zhang, W.2    Chen, X.3    Yang, J.4    Bhakat, K.K.5    Liu, C.6
  • 44
    • 0038137207 scopus 로고    scopus 로고
    • Phosphorylation of Kruppel-like factor 5 (KLF5/IKLF) at the CBP interaction region enhances its transactivation function
    • Zhang ZP, Teng CT (2003) Phosphorylation of Kruppel-like factor 5 (KLF5/IKLF) at the CBP interaction region enhances its transactivation function. Nucleic Acids Res 31:2196-2208.
    • (2003) Nucleic Acids Res , vol.31 , pp. 2196-2208
    • Zhang, Z.P.1    Teng, C.T.2
  • 45
    • 79960575502 scopus 로고    scopus 로고
    • Role of the KLF15 transcription factor in an anti-hypertrophic pathway involving GSK3 beta
    • Hussain S, Lara-Pezzi E, Brand N (2008) Role of the KLF15 transcription factor in an anti-hypertrophic pathway involving GSK3 beta. Heart 94:A53-A54.
    • (2008) Heart , vol.94
    • Hussain, S.1    Lara-Pezzi, E.2    Brand, N.3
  • 46
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • DOI 10.1023/A:1008392405740
    • Cornilescu G, Delaglio F, Bax A (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR 13:289-302. (Pubitemid 29143535)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.3 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 47
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger AT, et al. (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr D Biol Crystallogr 54:905-921.
    • (1998) Acta Crystallogr D Biol Crystallogr , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 48
    • 37549066702 scopus 로고    scopus 로고
    • Sumoylation of EKLF promotes transcriptional repression and is involved in inhibition of megakaryopoiesis
    • Siatecka M, Xue L, Bieker JJ (2007) Sumoylation of EKLF promotes transcriptional repression and is involved in inhibition of megakaryopoiesis. Mol Cell Biol 27:8547-8560.
    • (2007) Mol Cell Biol , vol.27 , pp. 8547-8560
    • Siatecka, M.1    Xue, L.2    Bieker, J.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.