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2002 | 49 | 3 |

Tytuł artykułu

Functionality versus strength - has functional selection taken place in the case of the ecdysteroid receptor response element?

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Nuclear receptors are ligand-dependent transcription factors responsible for con­trolling differentiation, growth and development of higher eukaryotes. Three amino acids within the recognition a-helix of the DNA-binding domain of the nuclear recep­tors constitute the so-called "P-box" which determines response element specificity. In the ultraspiracle (Usp) protein, which together with EcR forms the heterodimeric ecdysone receptor, the P-box residues are E19, G20 and G23. Substitution of E19, the most characteristic amino acid for estrogen receptor-like P-boxes, with alanine showed that the mutation did not appreciably alter the affinity of the wild-type Usp DNA-binding domain (UspDBDwT for a probe containing natural ecdysone response element (hsp27wt). Since in many cases E19 contacts a G/C base pair in position -4, which is absent in hsp27wt, we analysed the interaction of UspDBDwT, E19A and other P-box region mutants with the hsp27wt derivative which contains a G/C instead of an T/A base pair in position -4. UspDBDwT exhibited higher affinity for this ele­ment than for hsp27wt. Moreover, a different interaction pattern of P-box region mutants was also observed. Thus we conclude that the E19 residue of UspDBD is not involved in any hsp27wt sequence-discerning contacts. However, substitution of the hsp27wt T/A base pair in position –4 with G/C generates target sequence with distinct functional characteristics and possibly with a new specificity. These results could serve as a basis for understanding the role of the presence of a T/A or G/C base-pair in the position –4 in the two types of ecdysone response elements found in nature.

Wydawca

-

Rocznik

Tom

49

Numer

3

Opis fizyczny

p.747-756,fig.

Twórcy

autor
  • Wroclaw University of Technology, Wybrzeze Wyspianskiego 27, 50-370 Wroclaw, Poland
autor
autor

Bibliografia

  • Antoniewski C, Laval M, Lepesant JA. (1993) Structural features critical to the activity of an ecdysone receptor binding site. InsectBiochem Mol Biol; 23: 105-14.
  • Antoniewski C, Laval M, Dahan A, Lepesant JA. (1994) The ecdysone response enhancer of the Fbpl gene of Drosophila melanogaster is a direct target for the EcR/USP nuclear receptor. Mol Cell Biol.; 14: 4465-74.
  • Antoniewski C, O'Grady MS, Edmondson RG, Lassieur SM, Benes H. (1995) Characterization of an EcR/USP heterodimer target site that mediates ecdysone responsiveness of the Drosophila Lsp-2gene. Mol Gen Genet.; 249: 545-56.
  • Barik S. (1995) Site-directed mutagenesis by double polymerase chain reaction. Mol Biotechnol.; 3: 1-7.
  • Cherbas L, Lee K, Cherbas P. (1991) Identification of ecdysone response elements by analysis of the Drosophila Eip28/29 gene. Genes Dev.; 5: 120-31.
  • Evans RM. (1988) The steroid and thyroid hormone receptor superfamily. Science.; 240: 889-95.
  • Freedman LP, Luisi BF, Korszun ZR, Basavappa R, Sigler PB, Yamamoto KR. (1988) The function and structure of the metal coordination sites within the glucocorticoid receptor DNA binding domain. Nature.; 334: 543-46.
  • Fried M, Crothers DM. (1981) Equilibria and kinetics of lac repressor-operator interactions by polyacrylamide gel electrophoresis. Nucleic Acids Res.; 9: 6505-25.
  • Gehring U. (1998) Steroid hormone receptors and heat shock proteins. Vitam Horm.; 54: 167-205.
  • Gill SC, von Hippel PH. (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem.; 182: 319-26.
  • Grad I, Niedziela-Majka A, Kochman M, Ozyhar A. (2001) Analysis of Usp DNA-binding domain targeting reveals critical determinants of the ecdysone receptor complex interaction with the response element. Eur J Biochem.; 268: 3751-8.
  • Green S, Kumar V, Theulaz I, Wahli W, Chambon P. (1988) The N-terminal DNA-binding 'zinc finger' of the oestrogen and glucocorticoid receptors determines target gene specificity. EMBO J.; 7: 3037-44.
  • Gronemeyer H, Laudet V. (1995) Transcription factors 3: nuclear receptors. Protein Profile.; 2: 1173-308.
  • Koelle MR, Talbot WS, Segraves WA, Bender MT, Cherbas P, Hogness DS. (1991) The Drosophila EcRgene encodes an ecdysone receptor, a new member of the steroid receptor superfamily. Cell.; 67: 59-77.
  • Kozlova T, Thummel CS. (2000) Steroid regulation of postembryonic development and reproduction in Drosophila. Trends Endocrinol Metab. ; 11: 276-80.
  • Lehmann M, Korge G. (1995) Ecdysone regulation of the Drosophila Sgs-4 gene is mediated by the synergistic action of ecdysone receptor and SEBP 3. EMBO J; 14: 716-26.
  • Lehmann M, Wattler F, Korge G. (1997) Two new regulatory elements controlling the Drosophila Sgs-3 gene are potential ecdysone receptor and fork head binding sites. Mech Dev.; 62: 15-27.
  • Mader S, Kumar V, de Verneuil H, Chambon P. (1989) Three amino acids of the oestrogen receptor are essential to its ability to distinguish an oestrogen from a glucocorticoid-responsive element. Nature.; 338: 271-4.
  • Meinke G, Sigler PB. (1999) DNA-binding mechanism of the monomeric orphan nuclear receptor NGFI-B. Nat Struct Biol.; 6: 471-7.
  • Nelson CC, Hendy SC, Shukin RJ, Cheng H, Bruchovsky N, Koop BF, Rennie PS. (1999) Determinants of DNA sequence specificity of the androgen, progesterone, and glucocorticoid receptors: evidence for differential steroid receptor response elements. Mol Endocrinol.; 13: 2090-107.
  • Niedziela-Majka A, Rymarczyk G, Kochman M, Ozyhar A. (1998) Pure, bacterially expressed DNA-binding domains of the functional ecdysteroid receptor capable of interacting synergistically with the hsp27 20-hydroxyecdysone response element. GST-Induced dimerization of DNA-binding domains alters characteristics of their interaction with DNA. Protein Expr Purif.; 14: 208-20.
  • Niedziela-Majka A, Kochman M, Ozyhar A. (2000) Polarity of the ecdysone receptor complex interaction with the palindromic response element from the hsp27gene promoter. Eur JBiochem.; 267: 507-19.
  • Oro AE, McKeown M, Evans RM. (1990) Relationship between the product of the Drosophila ultraspiracle locus and the vertebrate retinoid X receptor. Nature.; 347: 298-301.
  • Ozyhar A, Strangmann-Diekmann M, Kiltz HH, Pongs O. (1991) Characterization of a specific ecdysteroid receptor-DNA complex reveals common properties for invertebrate and vertebrate hormone-receptor/DNA interactions. Eur J Biochem. ; 200: 329-35.
  • Rastinejad F, Perlmann T, Evans RM, Sigler PB. (1995) Structural determinants of nuclear receptor assembly on DNA direct repeats. Nature.; 375: 203-11.
  • Rastinejad F, Wagner T, Zhao Q, Khorasanizadeh S. (2000) Structure of the RXR-RAR DNA-binding complex on the retinoic acid response element DR1. EMBO J; 19: 1045-54.
  • Renaud JP, Moras D. (2000) Structural studies on nuclear receptors. Cell Mol Life Sci.; 57: 1748-69.
  • Riddihough G, Pelham HRB. (1987) An ecdysone response element in the Drosophila hsp27 promoter. EMBO J.; 6: 3729-34.
  • Schwabe JW, Chapman L, Finch JT, Rhodes D. (1993) The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: how receptors discriminate between their response elements. Cell.; 75: 567-78.
  • Sluder AE, Maina CV. (2001) Nuclear receptors in nematodes: themes and variations. Trends Genet.; 17: 206-13.
  • Smith DB, Johnson KS. (1988) Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene.; 67: 31-40.
  • Studier FW. (1991) Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system. J Mol Biol.; 219: 37-44.
  • Thomas HE, Stunnenberg HG, Stewart AF. (1993) Heterodimerization of the Drosophila ecdysone receptor with retinoid X receptor and ultraspiracle. Nature.; 362: 471-5.
  • Torchia J, Glass C, Rosenfeld MG. (1998) Co-activators and co-repressors in the integration of transcriptional responses. Curr Opin Cell Biol.; 10: 373-83.
  • Umesono K, Evans RM. (1989) Determinants of target gene specificity for steroid/thyroid hormone receptors. Cell.; 57: 1139-46.
  • Vogtli M, Elke C, Imhof MO, Lezzi M. (1998) High level transactivation by the ecdysone receptor complex at the core recognition motif. Nucleic Acids Res.; 26: 2407-14.
  • Yao TP, Segraves WA, Oro AE, McKeown M, Evans RM. (1992) Drosophila ultraspiracle modulates ecdysone receptor function via heterodimer formation. Cell.; 71: 63-72.
  • Zhao Q, Khorasanizadeh S, Miyoshi Y, Lazar MA, Rastinejad F. (1998) Structural elements of an orphan nuclear receptor- DNA complex. Mol Cell.; 1: 849-61.
  • Zhao Q, Chasse SA, Devarakonda S, Sierk ML, Ahvazi B, Rastinejad F. (2000) Structural basis of RXR-DNA interactions. J Mol Biol.; 296: 509-20.

Typ dokumentu

Bibliografia

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Identyfikator YADDA

bwmeta1.element.agro-article-2674cc6d-cd20-4231-a02a-34a3f61fbf05
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