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1
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Expression and purification of 6xHis-tagged DNA binding domains of functional ecdysteroid receptor from Drosophila melanogaster

100%
Rusin A., Majka A. N., Rymarczyk G., Ożyhar A.
Acta Biochimica Polonica
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1996
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vol. 43
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issue 4
611-621
2
Content available remote

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

100%
Grad I., Kochman M., Ożyhar A.
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2002
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vol. 49
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issue 3
747-756
EN
Nuclear receptors are ligand-dependent transcription factors responsible for controlling differentiation, growth and development of higher eukaryotes. Three amino acids within the recognition α-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.
3
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Two disulphide bridges are present in juvenile hormone binding protein from Galleria mellonella.

100%
Kołodziejczyk R., Dobryszycki P., Ożyhar A., Kochman M.
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EN
The hemolymph juvenile hormone binding protein (JHBP) from Galleria mellonella contains two disulphide bridges/molecule and no free Cys residues. An alignment of primary structures of other Lepidopteran JHBPs indicates that Cys residues, equivalent to Cys10,17,151,195 in G. mellonellaJHBP, may be involved in -S-S- bridge formation.
4
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Identification of specific interaction of juvenile hormone binding protein with isocitrate dehydrogenase

100%
Zalewska M., Ożyhar A., Kochman M.
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2011
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vol. 58
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issue 1
119-124
EN
Juvenile hormone (JH) is essential for multiple physiological processes: it controls larval development, metamorphosis and adult reproduction. In insect hemolymph more than 99 % of JH is bound to juvenile hormone binding protein (JHBP), which protects JH from degradation by nonspecific hydrolases and serves as a carrier to supply the hormone to the target tissues. In Galleria mellonella hemolymph, JHBP is found in a complex with lipid-binding high molecular weight proteins (HMWP) and this interaction is enhanced in the presence of JH. In this report, we present studies on the interaction of JHBP with low molecular weight proteins (LMWP) in the hemolymph. Using ligand blotting we found that JHBP interacts with a protein of about 44 kDa. To identify the protein that preferentially binds JHBP, a LMWP fraction was applied to a Sepharose-bound JHBP and, after washing, the column was eluted with free JHBP acting as a specific competitor or with carbonic anhydrase as a negative control. The eluted proteins were separated by SDS/PAGE and analyzed by mass spectrometry. Isocitrate dehydrogenase was identified as a component of the supramolecular complex of JHBP with hemolymph proteins.
5
Content available remote

Immunoaffinity purification of juvenile hormone-binding protein from Galleria mellonella hemolymph

88%
Wieczorek E., Rodriguez Parkitna J. M., Szkudlarek J., Ożyhar A., Kochman M.
Acta Biochimica Polonica
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1996
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vol. 43
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issue 4
603-610
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