메뉴 건너뛰기




Volumn 64, Issue 5-6, 2002, Pages 979-984

Differential activity by DNA-induced quarternary structures of POU transcription factors

Author keywords

Coregulator; Differential function; POU transcription factor; Quarternary arrangement; Regulation

Indexed keywords

DIMER; DNA; OCTAMER TRANSCRIPTION FACTOR 1; REPRESSOR PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR OBF 1; TRANSCRIPTION FACTOR PIT 1; TRANSCRIPTION FACTOR POU; UNCLASSIFIED DRUG;

EID: 0036710562     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(02)01164-4     Document Type: Article
Times cited : (25)

References (16)
  • 1
    • 0030960672 scopus 로고    scopus 로고
    • Transcriptional activation by recruitment
    • Ptashne M, Gann A, Transcriptional activation by recruitment. Nature 1997;569-77.
    • (1997) Nature , pp. 569-577
    • Ptashne, M.1    Gann, A.2
  • 2
    • 0028337542 scopus 로고
    • Transcriptional activation: A complex puzzle with few easy pieces
    • Tjian R., Maniatis T. Transcriptional activation: a complex puzzle with few easy pieces. Cell. 177:1994;5-8.
    • (1994) Cell , vol.177 , pp. 5-8
    • Tjian, R.1    Maniatis, T.2
  • 3
    • 0029562554 scopus 로고
    • The RXR heterodimers and orphan receptors
    • Mangelsdorf D.J., Evans R.M. The RXR heterodimers and orphan receptors. Cell. 83:1995;841-850.
    • (1995) Cell , vol.83 , pp. 841-850
    • Mangelsdorf, D.J.1    Evans, R.M.2
  • 4
    • 0025886340 scopus 로고
    • Octamania: The POU factors in murine development
    • Schöler H.R. Octamania: the POU factors in murine development. Trends Genet. 7:1991;323-329.
    • (1991) Trends Genet. , vol.7 , pp. 323-329
    • Schöler, H.R.1
  • 5
    • 0030918673 scopus 로고    scopus 로고
    • POU domain family values: Flexibility partnerships, and developmental codes
    • Ryan A.K., Rosenfeld M.G. POU domain family values: flexibility partnerships, and developmental codes. Genes Dev. 11:1997;1207-1225.
    • (1997) Genes Dev. , vol.11 , pp. 1207-1225
    • Ryan, A.K.1    Rosenfeld, M.G.2
  • 6
    • 0029124988 scopus 로고
    • The POU domain: Versatility in transcriptional regulation by a flexible two-in-one DNA-binding domain
    • Herr W., Cleary M.A. The POU domain: versatility in transcriptional regulation by a flexible two-in-one DNA-binding domain. Genes Dev. 9:1995;1679-1693.
    • (1995) Genes Dev. , vol.9 , pp. 1679-1693
    • Herr, W.1    Cleary, M.A.2
  • 7
    • 0031057121 scopus 로고    scopus 로고
    • Structure of Pit-1 POU domain bound to DNA as a dimer: Unexpected arrangement and flexibility
    • Jacobson E.M., Li P., Leon-del-Rio A., Rosenfeld M.G., Aggarwal A.K. Structure of Pit-1 POU domain bound to DNA as a dimer: unexpected arrangement and flexibility. Genes Dev. 11:1997;198-212.
    • (1997) Genes Dev. , vol.11 , pp. 198-212
    • Jacobson, E.M.1    Li, P.2    Leon-del-Rio, A.3    Rosenfeld, M.G.4    Aggarwal, A.K.5
  • 8
    • 0032128171 scopus 로고    scopus 로고
    • New POU dimer configuration mediates antagonistic control of an osteopontin preimplantation enhancer by Oct-4 and Sox-2
    • Botquin V., Hess H., Fuhrmann G., Anastassiadis C., Gross M.K., Vriend G.et al. New POU dimer configuration mediates antagonistic control of an osteopontin preimplantation enhancer by Oct-4 and Sox-2. Genes Dev. 12:1998;2073-2090.
    • (1998) Genes Dev. , vol.12 , pp. 2073-2090
    • Botquin, V.1    Hess, H.2    Fuhrmann, G.3    Anastassiadis, C.4    Gross, M.K.5    Vriend, G.6
  • 9
    • 0032545290 scopus 로고    scopus 로고
    • Highly cooperative homodimerization is a conserved property of neural POU proteins
    • Rhee J.M., Gruber C.A., Brodie T.B., Trieu M., Turner E.E. Highly cooperative homodimerization is a conserved property of neural POU proteins. J. Biol. Chem. 273:1998;34196-34205.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34196-34205
    • Rhee, J.M.1    Gruber, C.A.2    Brodie, T.B.3    Trieu, M.4    Turner, E.E.5
  • 10
    • 0033639075 scopus 로고    scopus 로고
    • Synergism with the coactivator OBF-1 (OCA-B, BOB-1) is mediated by a specific POU dimer configuration
    • Tomilin A., Remenyi A., Lins K., Bak H., Leidel S., Vriend G.et al. Synergism with the coactivator OBF-1 (OCA-B, BOB-1) is mediated by a specific POU dimer configuration. Cell. 103:2000;853-864.
    • (2000) Cell , vol.103 , pp. 853-864
    • Tomilin, A.1    Remenyi, A.2    Lins, K.3    Bak, H.4    Leidel, S.5    Vriend, G.6
  • 11
    • 0034634340 scopus 로고    scopus 로고
    • Allosteric effects of Pit-1 DNA sites on long-term repression in cell type specification
    • Scully K.M., Jacobson E.M., Jepsen K., Lunyak V., Viadiu H., Carrier C.et al. Allosteric effects of Pit-1 DNA sites on long-term repression in cell type specification. Science. 290:2000;1127-1131.
    • (2000) Science , vol.290 , pp. 1127-1131
    • Scully, K.M.1    Jacobson, E.M.2    Jepsen, K.3    Lunyak, V.4    Viadiu, H.5    Carrier, C.6
  • 12
    • 0034791092 scopus 로고    scopus 로고
    • Differential dimer activities of the transcription factor Oct-1 by DNA-induced interface swapping
    • Remenyi A., Tomilin A., Pohl E., Lins K., Philippsen A., Reinbold R.et al. Differential dimer activities of the transcription factor Oct-1 by DNA-induced interface swapping. Mol. Cell. 8:2001;569-580.
    • (2001) Mol. Cell , vol.8 , pp. 569-580
    • Remenyi, A.1    Tomilin, A.2    Pohl, E.3    Lins, K.4    Philippsen, A.5    Reinbold, R.6
  • 13
    • 0024477007 scopus 로고
    • Functional cooperativity between protein molecules bound at two distinct sequence elements of the immunoglobulin heavy-chain promoter
    • Poellinger L., Yoza B.K., Roeder R.G. Functional cooperativity between protein molecules bound at two distinct sequence elements of the immunoglobulin heavy-chain promoter. Nature. 337:1989;573-576.
    • (1989) Nature , vol.337 , pp. 573-576
    • Poellinger, L.1    Yoza, B.K.2    Roeder, R.G.3
  • 14
    • 0031784025 scopus 로고    scopus 로고
    • Coactivator OBF-1 makes selective contacts with both the POU-specific domain and the POU homeodomain and acts as a molecular clamp on DNA
    • Sauter P., Matthias P. Coactivator OBF-1 makes selective contacts with both the POU-specific domain and the POU homeodomain and acts as a molecular clamp on DNA. Mol. Cell Biol. 18:1998;7397-7409.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 7397-7409
    • Sauter, P.1    Matthias, P.2
  • 15
    • 0033569643 scopus 로고    scopus 로고
    • Crystal structure of an OCA-B peptide bound to an Oct-1 POU domain/octamer DNA complex: Specific recognition of a protein-DNA interface
    • Chasman D., Cepek K., Sharp P.A., Pabo C.O. Crystal structure of an OCA-B peptide bound to an Oct-1 POU domain/octamer DNA complex: specific recognition of a protein-DNA interface. Genes Dev. 13:1999;2650-2657.
    • (1999) Genes Dev. , vol.13 , pp. 2650-2657
    • Chasman, D.1    Cepek, K.2    Sharp, P.A.3    Pabo, C.O.4
  • 16
    • 0032580207 scopus 로고    scopus 로고
    • Allosteric effects of DNA on transcriptional regulators
    • Lefstin J.A., Yamamoto K.R. Allosteric effects of DNA on transcriptional regulators. Nature. 392:1998;885-888.
    • (1998) Nature , vol.392 , pp. 885-888
    • Lefstin, J.A.1    Yamamoto, K.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.