메뉴 건너뛰기




Volumn 15, Issue 1, 2007, Pages 75-83

DNA Recognition Mechanism of the ONECUT Homeodomain of Transcription Factor HNF-6

Author keywords

[No Author keywords available]

Indexed keywords

DNA; HEPATOCYTE NUCLEAR FACTOR 6; HOMEODOMAIN PROTEIN; OCTAMER TRANSCRIPTION FACTOR 1;

EID: 33846087417     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2006.11.004     Document Type: Article
Times cited : (37)

References (37)
  • 1
    • 0028108227 scopus 로고
    • Differential DNA-binding specificity of the engrailed homeodomain: the role of residue 50
    • Ades S.E., and Sauer R.T. Differential DNA-binding specificity of the engrailed homeodomain: the role of residue 50. Biochemistry 33 (1994) 9187-9194
    • (1994) Biochemistry , vol.33 , pp. 9187-9194
    • Ades, S.E.1    Sauer, R.T.2
  • 2
    • 0027465103 scopus 로고
    • The solution structure of the Oct-1 POU-specific domain reveals a striking similarity to the bacteriophage lambda repressor DNA-binding domain
    • Assa-Munt N., Mortishire-Smith R.J., Aurora R., Herr W., and Wright P.E. The solution structure of the Oct-1 POU-specific domain reveals a striking similarity to the bacteriophage lambda repressor DNA-binding domain. Cell 73 (1993) 193-205
    • (1993) Cell , vol.73 , pp. 193-205
    • Assa-Munt, N.1    Mortishire-Smith, R.J.2    Aurora, R.3    Herr, W.4    Wright, P.E.5
  • 3
    • 0030417483 scopus 로고    scopus 로고
    • Homeodomain-type DNA recognition
    • Billeter M. Homeodomain-type DNA recognition. Prog. Biophys. Mol. Biol. 66 (1996) 211-225
    • (1996) Prog. Biophys. Mol. Biol. , vol.66 , pp. 211-225
    • Billeter, M.1
  • 4
    • 0041344446 scopus 로고    scopus 로고
    • The onecut transcription factor hepatocyte nuclear factor-6 controls B lymphopoiesis in fetal liver
    • Bouzin C., Clotman F., Renauld J.C., Lemaigre F.P., and Rousseau G.G. The onecut transcription factor hepatocyte nuclear factor-6 controls B lymphopoiesis in fetal liver. J. Immunol. 171 (2003) 1297-1303
    • (2003) J. Immunol. , vol.171 , pp. 1297-1303
    • Bouzin, C.1    Clotman, F.2    Renauld, J.C.3    Lemaigre, F.P.4    Rousseau, G.G.5
  • 7
    • 0030996361 scopus 로고    scopus 로고
    • Synergistic activation of transcription by CBP and p53
    • Gu W., Shi X.L., and Roeder R.G. Synergistic activation of transcription by CBP and p53. Nature 387 (1997) 819-823
    • (1997) Nature , vol.387 , pp. 819-823
    • Gu, W.1    Shi, X.L.2    Roeder, R.G.3
  • 8
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in transcriptional co-activators mediates binding to nuclear receptors
    • Heery D.M., Kalkhoven E., Hoare S., and Parker M.G. A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature 387 (1997) 733-736
    • (1997) Nature , vol.387 , pp. 733-736
    • Heery, D.M.1    Kalkhoven, E.2    Hoare, S.3    Parker, M.G.4
  • 10
    • 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., Cowan S.W., and Kjeldgaard. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47 (1991) 110-119
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 11
    • 0025188837 scopus 로고
    • Crystal structure of an engrailed homeodomain-DNA complex at 2.8 Å resolution: a framework for understanding homeodomain-DNA interactions
    • Kissinger C.R., Liu B.S., Martin-Blanco E., Kornberg T.B., and Pabo C.O. Crystal structure of an engrailed homeodomain-DNA complex at 2.8 Å resolution: a framework for understanding homeodomain-DNA interactions. Cell 63 (1990) 579-590
    • (1990) Cell , vol.63 , pp. 579-590
    • Kissinger, C.R.1    Liu, B.S.2    Martin-Blanco, E.3    Kornberg, T.B.4    Pabo, C.O.5
  • 12
    • 0028200262 scopus 로고
    • Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules
    • Klemm J.D., Rould M.A., Aurora R., Herr W., and Pabo C.O. Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules. Cell 77 (1994) 21-32
    • (1994) Cell , vol.77 , pp. 21-32
    • Klemm, J.D.1    Rould, M.A.2    Aurora, R.3    Herr, W.4    Pabo, C.O.5
  • 14
    • 0031573874 scopus 로고    scopus 로고
    • HNF-6 is expressed in endoderm derivatives and nervous system of the mouse embryo and participates to the cross-regulatory network of liver-enriched transcription factors
    • Landry C., Clotman F., Hioki T., Oda H., Picard J.J., Lemaigre F.P., and Rousseau G.G. HNF-6 is expressed in endoderm derivatives and nervous system of the mouse embryo and participates to the cross-regulatory network of liver-enriched transcription factors. Dev. Biol. 192 (1997) 247-257
    • (1997) Dev. Biol. , vol.192 , pp. 247-257
    • Landry, C.1    Clotman, F.2    Hioki, T.3    Oda, H.4    Picard, J.J.5    Lemaigre, F.P.6    Rousseau, G.G.7
  • 15
    • 0032577494 scopus 로고    scopus 로고
    • Isoforms of hepatocyte nuclear factor-6 differ in DNA-binding properties, contain a bifunctional homeodomain, and define the new ONECUT class of homeodomain proteins
    • Lannoy V.J., Burglin T.R., Rousseau G.G., and Lemaigre F.P. Isoforms of hepatocyte nuclear factor-6 differ in DNA-binding properties, contain a bifunctional homeodomain, and define the new ONECUT class of homeodomain proteins. J. Biol. Chem. 273 (1998) 13552-13562
    • (1998) J. Biol. Chem. , vol.273 , pp. 13552-13562
    • Lannoy, V.J.1    Burglin, T.R.2    Rousseau, G.G.3    Lemaigre, F.P.4
  • 16
    • 0034698040 scopus 로고    scopus 로고
    • Transcriptional stimulation by hepatocyte nuclear factor-6. Target-specific recruitment of either CREB-binding protein (CBP) or p300/CBP-associated factor (p/CAF)
    • Lannoy V.J., Rodolosse A., Pierreux C.E., Rousseau G.G., and Lemaigre F.P. Transcriptional stimulation by hepatocyte nuclear factor-6. Target-specific recruitment of either CREB-binding protein (CBP) or p300/CBP-associated factor (p/CAF). J. Biol. Chem. 275 (2000) 22098-22103
    • (2000) J. Biol. Chem. , vol.275 , pp. 22098-22103
    • Lannoy, V.J.1    Rodolosse, A.2    Pierreux, C.E.3    Rousseau, G.G.4    Lemaigre, F.P.5
  • 17
    • 0036360938 scopus 로고    scopus 로고
    • Liver glucokinase gene expression is controlled by the onecut transcription factor hepatocyte nuclear factor-6
    • Lannoy V.J., Decaux J.F., Pierreux C.E., Lemaigre F.P., and Rousseau G.G. Liver glucokinase gene expression is controlled by the onecut transcription factor hepatocyte nuclear factor-6. Diabetologia 45 (2002) 1136-1141
    • (2002) Diabetologia , vol.45 , pp. 1136-1141
    • Lannoy, V.J.1    Decaux, J.F.2    Pierreux, C.E.3    Lemaigre, F.P.4    Rousseau, G.G.5
  • 18
    • 0026321622 scopus 로고
    • DNA binding specificity of homeodomains
    • Laughon A. DNA binding specificity of homeodomains. Biochemistry 30 (1991) 11357-11367
    • (1991) Biochemistry , vol.30 , pp. 11357-11367
    • Laughon, A.1
  • 19
    • 0027228359 scopus 로고
    • Liver-specific factor binding to the liver promoter of a 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase gene
    • Lemaigre F.P., Durviaux S.M., and Rousseau G.G. Liver-specific factor binding to the liver promoter of a 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase gene. J. Biol. Chem. 268 (1993) 19896-19905
    • (1993) J. Biol. Chem. , vol.268 , pp. 19896-19905
    • Lemaigre, F.P.1    Durviaux, S.M.2    Rousseau, G.G.3
  • 20
    • 0029841390 scopus 로고    scopus 로고
    • Hepatocyte nuclear factor 6, a transcription factor that contains a novel type of homeodomain and a single cut domain
    • Lemaigre F.P., Durviaux S.M., Truong O., Lannoy V.J., Hsuan J.J., and Rousseau G.G. Hepatocyte nuclear factor 6, a transcription factor that contains a novel type of homeodomain and a single cut domain. Proc. Natl. Acad. Sci. USA 93 (1996) 9460-9464
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9460-9464
    • Lemaigre, F.P.1    Durviaux, S.M.2    Truong, O.3    Lannoy, V.J.4    Hsuan, J.J.5    Rousseau, G.G.6
  • 21
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33 (1968) 491-497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 23
    • 0024997404 scopus 로고
    • Protein-DNA contacts in the structure of a homeodomain-DNA complex determined by nuclear magnetic resonance spectroscopy in solution
    • Otting G., Qian Y.Q., Billeter M., Muller M., Affolter M., Gehring W.J., and Wuthrich K. Protein-DNA contacts in the structure of a homeodomain-DNA complex determined by nuclear magnetic resonance spectroscopy in solution. EMBO J. 9 (1990) 3085-3092
    • (1990) EMBO J. , vol.9 , pp. 3085-3092
    • Otting, G.1    Qian, Y.Q.2    Billeter, M.3    Muller, M.4    Affolter, M.5    Gehring, W.J.6    Wuthrich, K.7
  • 24
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 25
    • 0034690999 scopus 로고    scopus 로고
    • Control of gene expression by growth hormone in liver: key role of a network of transcription factors
    • Rastegar M., Lemaigre F.P., and Rousseau G.G. Control of gene expression by growth hormone in liver: key role of a network of transcription factors. Mol. Cell. Endocrinol. 164 (2000) 1-4
    • (2000) Mol. Cell. Endocrinol. , vol.164 , pp. 1-4
    • Rastegar, M.1    Lemaigre, F.P.2    Rousseau, G.G.3
  • 26
    • 0029824047 scopus 로고    scopus 로고
    • The transcriptional activator hepatocyte nuclear factor 6 regulates liver gene expression
    • Samadani U., and Costa R.H. The transcriptional activator hepatocyte nuclear factor 6 regulates liver gene expression. Mol. Cell. Biol. 16 (1996) 6273-6284
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6273-6284
    • Samadani, U.1    Costa, R.H.2
  • 27
    • 0033601376 scopus 로고    scopus 로고
    • Cooperative regulation of CYP2C12 gene expression by STAT5 and liver-specific factors in female rats
    • Sasaki Y., Takahashi Y., Nakayama K., and Kamataki T. Cooperative regulation of CYP2C12 gene expression by STAT5 and liver-specific factors in female rats. J. Biol. Chem. 274 (1999) 37117-37124
    • (1999) J. Biol. Chem. , vol.274 , pp. 37117-37124
    • Sasaki, Y.1    Takahashi, Y.2    Nakayama, K.3    Kamataki, T.4
  • 28
    • 2442666735 scopus 로고    scopus 로고
    • Transcriptional networks controlling pancreatic development and β cell function
    • Servitja J.M., and Ferrer J. Transcriptional networks controlling pancreatic development and β cell function. Diabetologia 47 (2004) 597-613
    • (2004) Diabetologia , vol.47 , pp. 597-613
    • Servitja, J.M.1    Ferrer, J.2
  • 29
    • 4043075618 scopus 로고    scopus 로고
    • Structure of the hepatocyte nuclear factor 6α and its interaction with DNA
    • Sheng W., Yan H., Rausa III F.M., Costa R.H., and Liao X. Structure of the hepatocyte nuclear factor 6α and its interaction with DNA. J. Biol. Chem. 279 (2004) 33928-33936
    • (2004) J. Biol. Chem. , vol.279 , pp. 33928-33936
    • Sheng, W.1    Yan, H.2    Rausa III, F.M.3    Costa, R.H.4    Liao, X.5
  • 30
    • 0035378197 scopus 로고    scopus 로고
    • Protein kinase A phosphorylates hepatocyte nuclear factor-6 and stimulates glucose-6-phosphatase catalytic subunit gene transcription
    • Streeper R.S., Hornbuckle L.A., Svitek C.A., Goldman J.K., Oeser J.K., and O'Brien R.M. Protein kinase A phosphorylates hepatocyte nuclear factor-6 and stimulates glucose-6-phosphatase catalytic subunit gene transcription. J. Biol. Chem. 276 (2001) 19111-19118
    • (2001) J. Biol. Chem. , vol.276 , pp. 19111-19118
    • Streeper, R.S.1    Hornbuckle, L.A.2    Svitek, C.A.3    Goldman, J.K.4    Oeser, J.K.5    O'Brien, R.M.6
  • 31
    • 0036210624 scopus 로고    scopus 로고
    • Maintaining HNF6 expression prevents AdHNF3β-mediated decrease in hepatic levels of Glut-2 and glycogen
    • Tan Y., Adami G., and Costa R.H. Maintaining HNF6 expression prevents AdHNF3β-mediated decrease in hepatic levels of Glut-2 and glycogen. Hepatology 35 (2002) 790-798
    • (2002) Hepatology , vol.35 , pp. 790-798
    • Tan, Y.1    Adami, G.2    Costa, R.H.3
  • 32
    • 0001940082 scopus 로고
    • MAD phasing: treatment of dispersive differences as isomorphous replacement information
    • Terwilliger T.C. MAD phasing: treatment of dispersive differences as isomorphous replacement information. Acta Crystallogr. D Biol. Crystallogr. 50 (1994) 17-23
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 17-23
    • Terwilliger, T.C.1
  • 34
    • 0029951161 scopus 로고    scopus 로고
    • Conservation and diversification in homeodomain-DNA interactions: a comparative genetic analysis
    • Wilson D.S., Sheng G., Jun S., and Desplan C. Conservation and diversification in homeodomain-DNA interactions: a comparative genetic analysis. Proc. Natl. Acad. Sci. USA 93 (1996) 6886-6891
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6886-6891
    • Wilson, D.S.1    Sheng, G.2    Jun, S.3    Desplan, C.4
  • 35
    • 0026002757 scopus 로고
    • Crystal structure of a MAT α 2 homeodomain-operator complex suggests a general model for homeodomain-DNA interactions
    • Wolberger C., Vershon A.K., Liu B., Johnson A.D., and Pabo C.O. Crystal structure of a MAT α 2 homeodomain-operator complex suggests a general model for homeodomain-DNA interactions. Cell 67 (1991) 517-528
    • (1991) Cell , vol.67 , pp. 517-528
    • Wolberger, C.1    Vershon, A.K.2    Liu, B.3    Johnson, A.D.4    Pabo, C.O.5
  • 36
    • 0028919759 scopus 로고
    • Crystal structure of a paired domain-DNA complex at 2.5 Å resolution reveals structural basis for Pax developmental mutations
    • Xu W., Rould M.A., Jun S., Desplan C., and Pabo C.O. Crystal structure of a paired domain-DNA complex at 2.5 Å resolution reveals structural basis for Pax developmental mutations. Cell 80 (1995) 639-650
    • (1995) Cell , vol.80 , pp. 639-650
    • Xu, W.1    Rould, M.A.2    Jun, S.3    Desplan, C.4    Pabo, C.O.5
  • 37
    • 33644872571 scopus 로고    scopus 로고
    • LAFIRE: software for automating the refinement process of protein-structure analysis
    • Yao M., Zhou Y., and Tanaka I. LAFIRE: software for automating the refinement process of protein-structure analysis. Acta Crystallogr. D Biol. Crystallogr. 62 (2006) 189-196
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 189-196
    • Yao, M.1    Zhou, Y.2    Tanaka, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.