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Volumn 59, Issue 20, 1999, Pages 5275-5282

Structure-function studies of the BTB/POZ transcriptional repression domain from the promyelocytic leukemia zinc finger oncoprotein

Author keywords

[No Author keywords available]

Indexed keywords

ONCOPROTEIN; ZINC FINGER PROTEIN;

EID: 0032724185     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (84)

References (43)
  • 1
    • 0027411688 scopus 로고
    • Fusion between a novel Kruppel-like zinc finger gene and the retinoic acid receptor-α locus due to a variant t(11;17) translocation associated with acute promyelocytic leukemia
    • Chen, Z., Brand, N. J., Chen, A., Chen, S-J., Tong, J-H., Wang, Z. Y., Waxman, S., and Zelent, A. Fusion between a novel Kruppel-like zinc finger gene and the retinoic acid receptor-α locus due to a variant t(11;17) translocation associated with acute promyelocytic leukemia. EMBO J., 12: 1161-1167, 1993.
    • (1993) EMBO J. , vol.12 , pp. 1161-1167
    • Chen, Z.1    Brand, N.J.2    Chen, A.3    Chen, S.-J.4    Tong, J.-H.5    Wang, Z.Y.6    Waxman, S.7    Zelent, A.8
  • 2
    • 0017362792 scopus 로고
    • 15/17 translation: A consistent chromosomal change in acute promyelocytic leukaemia
    • Rowley, J. D., Golomb, H. M., and Dougherty, C. 15/17 translation: a consistent chromosomal change in acute promyelocytic leukaemia [letter]. Lancet, 1: 549-550, 1977.
    • (1977) Lancet , vol.1 , pp. 549-550
    • Rowley, J.D.1    Golomb, H.M.2    Dougherty, C.3
  • 3
    • 0028174267 scopus 로고
    • Translocation of the RARα locus to the PML of PLZF gene in acute promyelocytic leukemia
    • Zelent, A. Translocation of the RARα locus to the PML of PLZF gene in acute promyelocytic leukemia. Br. J. Haematol., 86: 451-460, 1994.
    • (1994) Br. J. Haematol. , vol.86 , pp. 451-460
    • Zelent, A.1
  • 5
    • 0028110129 scopus 로고
    • The BTB domain, found primarily in zinc finger proteins, defines an evolutionarily conserved family that includes several developmentally regulated genes in Drosophila
    • Zollman, S., Godt, D., Prive, G. G., Couderc, J-L., and Laski, F. The BTB domain, found primarily in zinc finger proteins, defines an evolutionarily conserved family that includes several developmentally regulated genes in Drosophila. Proc. Natl. Acad. Sci. USA, 91: 10717-10721, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10717-10721
    • Zollman, S.1    Godt, D.2    Prive, G.G.3    Couderc, J.-L.4    Laski, F.5
  • 6
    • 0028040875 scopus 로고
    • The POZ domain: A conserved protein-protein interaction motif
    • Bardwell, V. J., and Treisman, R. The POZ domain: a conserved protein-protein interaction motif. Genes Dev., 8: 1664-1677, 1994.
    • (1994) Genes Dev. , vol.8 , pp. 1664-1677
    • Bardwell, V.J.1    Treisman, R.2
  • 7
    • 0029099016 scopus 로고
    • The BTB/POZ domain: A new protein-protein interaction motif common to DNA- And actin-binding proteins
    • Albagli, O., Dhordain, P., Deweindt, C., Lecocq, G., and Leprince, D. The BTB/POZ domain: a new protein-protein interaction motif common to DNA- and actin-binding proteins. Cell Growth Differ., 6: 1193-1198, 1995.
    • (1995) Cell Growth Differ. , vol.6 , pp. 1193-1198
    • Albagli, O.1    Dhordain, P.2    Deweindt, C.3    Lecocq, G.4    Leprince, D.5
  • 8
    • 0030828003 scopus 로고    scopus 로고
    • Overexpression, purification, characterization, and crystallization of the BTB/POZ domain from the PLZF oncoprotein
    • Li, X., Lopez-Guisa, J. M., Ninan, N., Weiner, E. J., Rauscher, F. J., III, and Marmorstein, R. Overexpression, purification, characterization, and crystallization of the BTB/POZ domain from the PLZF oncoprotein. J. Biol. Chem., 272; 27324-27329, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27324-27329
    • Li, X.1    Lopez-Guisa, J.M.2    Ninan, N.3    Weiner, E.J.4    Rauscher F.J. III5    Marmorstein, R.6
  • 9
    • 0029066949 scopus 로고
    • The BTB domain of bric a brac mediates dimerization in vitro
    • Chen, W., Zollman, S., Couderc, J. L., and Laski, F. A. The BTB domain of bric a brac mediates dimerization in vitro. Mol. Cell. Biol., 15: 3424-3429, 1995.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3424-3429
    • Chen, W.1    Zollman, S.2    Couderc, J.L.3    Laski, F.A.4
  • 10
    • 0032511890 scopus 로고    scopus 로고
    • The BCL-6 POZ domain and other POZ domains interact with the co-repressors N-CoR and SMART
    • Huynh, K. D., and Bardwell, V. J. The BCL-6 POZ domain and other POZ domains interact with the co-repressors N-CoR and SMART. Oncogene, 17: 2473-2484, 1998.
    • (1998) Oncogene , vol.17 , pp. 2473-2484
    • Huynh, K.D.1    Bardwell, V.J.2
  • 14
    • 0029902260 scopus 로고    scopus 로고
    • BCL-6, a POZ/ zinc-finger protein, is a sequence-specific transcriptional repressor
    • Chang, C-C., Ye, B. H., Chaganti, R. S. K., and Dalla-Favera, R. BCL-6, a POZ/ zinc-finger protein, is a sequence-specific transcriptional repressor. Proc. Natl. Acad. Sci. USA, 93: 6947-6952, 1996.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6947-6952
    • Chang, C.-C.1    Ye, B.H.2    Chaganti, R.S.K.3    Dalla-Favera, R.4
  • 15
    • 0029899571 scopus 로고    scopus 로고
    • Transcriptional repression by the proto-oncogene BCL-6
    • Seyfert, V., Allman, D., He, Y., and Staudt, L. M. Transcriptional repression by the proto-oncogene BCL-6. Oncogene, 12: 2331-2342, 1996.
    • (1996) Oncogene , vol.12 , pp. 2331-2342
    • Seyfert, V.1    Allman, D.2    He, Y.3    Staudt, L.M.4
  • 16
    • 0028822226 scopus 로고
    • The LAZ3/BCL6 oncogene encodes a sequence-specific transcriptional inhibitor: A novel function for the BTB/POZ domain as an autonomous repressing domain
    • Deweindt, C., Albagli, O., Bernardin, F., Dhordain, P., Quief, S., Lantoine, D., Kerckaert, J-P., and Leprince, D. The LAZ3/BCL6 oncogene encodes a sequence-specific transcriptional inhibitor: a novel function for the BTB/POZ domain as an autonomous repressing domain. Cell Growth Differ., 6: 1495-1503, 1995.
    • (1995) Cell Growth Differ. , vol.6 , pp. 1495-1503
    • Deweindt, C.1    Albagli, O.2    Bernardin, F.3    Dhordain, P.4    Quief, S.5    Lantoine, D.6    Kerckaert, J.-P.7    Leprince, D.8
  • 18
    • 0030847164 scopus 로고    scopus 로고
    • SMART corepressor interacts with PLZF and with the PML-retinoic acid receptor α (RARα) and PLZF-RARα oncoproteins associated with acute promyelocytic leukemia
    • Hong, S-H., David, G., Wong, C-W., Dejean, A., and Privalsky, M. L. SMART corepressor interacts with PLZF and with the PML-retinoic acid receptor α (RARα) and PLZF-RARα oncoproteins associated with acute promyelocytic leukemia. Proc. Natl. Acad. Sci. USA, 94: 9028-9033, 1997
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9028-9033
    • Hong, S.-H.1    David, G.2    Wong, C.-W.3    Dejean, A.4    Privalsky, M.L.5
  • 19
    • 0032516221 scopus 로고    scopus 로고
    • Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein
    • David, G., Alland, L., Hong, S-H., Wong, C-W., Depinho, R., and Dejean, A. Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein. Oncogene, 16: 2549-2556, 1998.
    • (1998) Oncogene , vol.16 , pp. 2549-2556
    • David, G.1    Alland, L.2    Hong, S.-H.3    Wong, C.-W.4    Depinho, R.5    Dejean, A.6
  • 20
    • 0032546017 scopus 로고    scopus 로고
    • Role of the histone deacetylase complex in acute promyelocytic leukaemia
    • Lin, R. J., Nagy, L., Inoue, S., Shao, W. L., Miller, W. H., and Evans, R. M. Role of the histone deacetylase complex in acute promyelocytic leukaemia. Nature (Lond.), 391: 811-814, 1998.
    • (1998) Nature (Lond.) , vol.391 , pp. 811-814
    • Lin, R.J.1    Nagy, L.2    Inoue, S.3    Shao, W.L.4    Miller, W.H.5    Evans, R.M.6
  • 22
    • 0029097233 scopus 로고
    • A transcriptional co-repressor that interacts with nuclear hormone receptors
    • Chen, J. D., and Evans, R. M. A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature (Lond.), 377: 454-457, 1995.
    • (1995) Nature (Lond.) , vol.377 , pp. 454-457
    • Chen, J.D.1    Evans, R.M.2
  • 24
    • 0030959244 scopus 로고    scopus 로고
    • Role for N-CoR and histone deacetylase in Sin3-mediated transcriptional repression
    • Alland, L., Muhle, R., Hou, H., Potes, J., Chin, L., and Schreiber-Agus, N. Role for N-CoR and histone deacetylase in Sin3-mediated transcriptional repression. Nature (Lond.), 387: 49-55, 1997.
    • (1997) Nature (Lond.) , vol.387 , pp. 49-55
    • Alland, L.1    Muhle, R.2    Hou, H.3    Potes, J.4    Chin, L.5    Schreiber-Agus, N.6
  • 25
    • 0031941912 scopus 로고    scopus 로고
    • Distinct interactions of PML-RARα and PLZF-RARα with co-repressors determine differential responses to RA in APL
    • He, L. Z., Guidez, F., Tribioli, C., Peruzzi, D., Ruthardt, M., Zelent, A., and Pandolfi, P. P. Distinct interactions of PML-RARα and PLZF-RARα with co-repressors determine differential responses to RA in APL. Nat. Genet., 18: 126-135, 1998.
    • (1998) Nat. Genet. , vol.18 , pp. 126-135
    • He, L.Z.1    Guidez, F.2    Tribioli, C.3    Peruzzi, D.4    Ruthardt, M.5    Zelent, A.6    Pandolfi, P.P.7
  • 28
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • L. Sawyer, N. Isaacs, and S. Bailey (eds.), Warrington, United Kingdom: SERC Daresbury Laboratory
    • Otwinowski, Z. Oscillation data reduction program. In: L. Sawyer, N. Isaacs, and S. Bailey (eds.), Proceedings of the CCP4 Study Weekend: Data Collection and Processing, pp. 56-62. Warrington, United Kingdom: SERC Daresbury Laboratory, 1993.
    • (1993) Proceedings of the CCP4 Study Weekend: Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 29
    • 0030818593 scopus 로고    scopus 로고
    • PHASES-95: A program package for the processing and analysis of diffraction data from macromolecules
    • C. W. Carter and R. M. Sweet (eds.), Orlando, FL: Academic Press
    • Furey, W., and Swaminathan, S. PHASES-95: a program package for the processing and analysis of diffraction data from macromolecules. In: C. W. Carter and R. M. Sweet (eds.), Methods in Enzymology, Vol. 277, pp. 590-620. Orlando, FL: Academic Press, 1997.
    • (1997) Methods in Enzymology , vol.277 , pp. 590-620
    • Furey, W.1    Swaminathan, S.2
  • 30
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., and Cowen, S. W. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A, 47: 110-119, 1991.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowen, S.W.3
  • 32
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity assessing the accuracy of crystal structures
    • Brunger, A. T. The free R value: a novel statistical quantity assessing the accuracy of crystal structures. Nature (Lond.), 335: 472-474, 1992.
    • (1992) Nature (Lond.) , vol.335 , pp. 472-474
    • Brunger, A.T.1
  • 33
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Washington DC
    • Brunger, A. T., Kuriyan, J., and Karplus, M. Crystallographic R factor refinement by molecular dynamics. Science (Washington DC), 235: 458-460, 1987.
    • (1987) Science , vol.235 , pp. 458-460
    • Brunger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 34
    • 84901961522 scopus 로고
    • Slow-cooling protocols for crystallographic refinement by simulated annealing
    • Brunger, A. T., and Krukowski, A. Slow-cooling protocols for crystallographic refinement by simulated annealing. Acta Crystallogr. A, 46: 585-593, 1990.
    • (1990) Acta Crystallogr. A , vol.46 , pp. 585-593
    • Brunger, A.T.1    Krukowski, A.2
  • 35
    • 0028070557 scopus 로고
    • Torsion angle dynamics: Reduced variable conformational sampling enhances crystallographic structure refinement
    • Rice, L. M., and Brunger, A. T. Torsion angle dynamics: reduced variable conformational sampling enhances crystallographic structure refinement. Proteins, 19: 277-290, 1994.
    • (1994) Proteins , vol.19 , pp. 277-290
    • Rice, L.M.1    Brunger, A.T.2
  • 36
    • 0028172551 scopus 로고
    • Protein hydration observed by X-ray diffraction: Solvation properties of penicillopepsin ard neuraminidase crystal structures
    • Jiang, J. S., and Brunger, A. T. Protein hydration observed by X-ray diffraction: solvation properties of penicillopepsin ard neuraminidase crystal structures. J. Mol. Biol., 243: 100-115, 1994.
    • (1994) J. Mol. Biol. , vol.243 , pp. 100-115
    • Jiang, J.S.1    Brunger, A.T.2
  • 37
    • 84945096204 scopus 로고
    • Model bias in macromolecular crystal structures
    • Hodel, A., Kim, S-H., and Brunger, A. T. Model bias in macromolecular crystal structures. Acta Crystallogr. A, 48: 851-858, 1992.
    • (1992) Acta Crystallogr. A , vol.48 , pp. 851-858
    • Hodel, A.1    Kim, S.-H.2    Brunger, A.T.3
  • 38
    • 0030589514 scopus 로고    scopus 로고
    • Phi/Psi-chology: Ramachandran revisted
    • Kleywegt, G. J., and Jones, T. A. Phi/Psi-chology: Ramachandran revisted. Curr. Biol., 4: 1395-1400, 1996b.
    • (1996) Curr. Biol. , vol.4 , pp. 1395-1400
    • Kleywegt, G.J.1    Jones, T.A.2
  • 39
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson, G. L. A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal. Biochem., 83: 346-356, 1977.
    • (1977) Anal. Biochem. , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 40
    • 0033013868 scopus 로고    scopus 로고
    • KAP-1 corepressor protein interacts and colocalizes with heterochromatic and euchromatic HPl proteins: A potential role for Kruppel-associated Box-zinc finger proteins in heterochromatin-mediated gene silencing
    • Ryan, R. F., Schultz, D. C., Ayyanathan, K., Singh, P. B., Friedman, J. R., Fredericks, W. J., and Rauscher. F. J. KAP-1 corepressor protein interacts and colocalizes with heterochromatic and euchromatic HPl proteins: a potential role for Kruppel-associated Box-zinc finger proteins in heterochromatin-mediated gene silencing. Mol. Cell. Biol.. 19: 4366-4378, 1999.
    • (1999) Mol. Cell. Biol.. , vol.19 , pp. 4366-4378
    • Ryan, R.F.1    Schultz, D.C.2    Ayyanathan, K.3    Singh, P.B.4    Friedman, J.R.5    Fredericks, W.J.6    Rauscher, F.J.7
  • 41
    • 17144450753 scopus 로고    scopus 로고
    • The N-terminal POZ domain of GAGA mediates the formation of oligomers that bind DNA with high affinity and specificity
    • Espinas, M. L., Jimenez-Garcia, E., Vaquero, A., Canudas, S., Bernues, J., and Azorin, F. The N-terminal POZ domain of GAGA mediates the formation of oligomers that bind DNA with high affinity and specificity. J. Biol. Chem., 274: 16461-16469, 1999.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16461-16469
    • Espinas, M.L.1    Jimenez-Garcia, E.2    Vaquero, A.3    Canudas, S.4    Bernues, J.5    Azorin, F.6
  • 42
  • 43
    • 0033081466 scopus 로고    scopus 로고
    • Co-operative DNA binding by GAGA transcription factor requires the conserved BTB/POZ domain and reorganizes promoter topology
    • Katsani, K. R., Hajibagheri, M. A. N., and Verrijzer, C. P. Co-operative DNA binding by GAGA transcription factor requires the conserved BTB/POZ domain and reorganizes promoter topology. EMBO J., 18: 698-708, 1999.
    • (1999) EMBO J. , vol.18 , pp. 698-708
    • Katsani, K.R.1    Hajibagheri, M.A.N.2    Verrijzer, C.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.