Regulatory elements in the juvenile hormone binding protein gene from Galleria mellonella — Topography of binding sites for Usp and EcRDBD

2008 ◽  
Vol 1779 (6-7) ◽  
pp. 390-401 ◽  
Author(s):  
Agnieszka J. Sok ◽  
Grażyna Andruszewska ◽  
Anna Niewiadomska-Cimicka ◽  
Iwona Grad ◽  
Grzegorz Rymarczyk ◽  
...  
Keyword(s):  
Juvenile Hormone ◽  
Binding Sites ◽  
Protein Gene ◽  
Galleria Mellonella ◽  
Binding Protein ◽  
Regulatory Elements ◽  
Hormone Binding ◽  
Juvenile Hormone Binding Protein ◽  
Hormone Binding Protein ◽  
Binding Protein Gene

The structure of the juvenile hormone binding protein gene from Galleria mellonella

2005 ◽  
Vol 386 (1) ◽  
pp. 1-10 ◽  
Author(s):  
Agnieszka J. Sok ◽  
Kamila Czajewska ◽  
Andrzej Ożyhar ◽  
Marian Kochman
Keyword(s):  
Juvenile Hormone ◽  
Galleria Mellonella ◽  
Binding Protein ◽  
Core Promoter ◽  
Phase 1 ◽  
Regulatory Elements ◽  
Retinol Binding Protein ◽  
Hormone Binding ◽  
Juvenile Hormone Binding Protein ◽  
Hormone Binding Protein

AbstractJuvenile hormone (JH) and ecdysone are the key hormones controlling insect growth and development. The juvenile hormone binding protein (JHBP) is the first member in the array of proteins participating in JH signal transmission. In the present report a wholejhbpgene sequence (9790 bp) is described. Thejhbpgene contains four introns (A–D). All the introns have common flanking sequences: GT at the 5′ and AG at the 3′ end. The first intron is in phase 1, the second in phase 2, and the third and fourth in phase 1. An analysis of these sequences suggests that U2-class spliceosomes are involved in intron excision from pre-mRNA. Several horizontally transmitted elements from other genes were found in the introns. Alljhbpexons are positioned in local AT-reach regions of the gene. A search for core promoter regulatory elements revealed that the TATA box starts 29 bp preceding the start of transcription; the sequence TCAGTA representing a putative initiator sequence (Inr) starts at position +14. Eight characteristic sequences for bindingBroad-Complexgene products, which coordinate the ecdysone temporal response, are present in the non-coding sequence of thejhbpgene. An analysis of exon locations and intron phases indicates thatjhbpgene organization is related to theretinol binding proteingene, a member of the lipocalin family.

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

1996 ◽  
Vol 43 (4) ◽  
pp. 603-610 ◽  
Author(s):  
E Wieczorek ◽  
J M Parkitna ◽  
J Szkudlarek ◽  
A Ozyhar ◽  
M Kochman
Keyword(s):  
Juvenile Hormone ◽  
Galleria Mellonella ◽  
Binding Protein ◽  
Gel Filtration ◽  
Binding Activity ◽  
Hormone Binding ◽  
Simple Method ◽  
Juvenile Hormone Binding Protein ◽  
Hormone Binding Protein ◽  
Sepharose 4B

Previously described methods of purification of hemolymph juvenile hormone-binding protein (hJHBP) from Lepidoptera were tedious and required multiple steps. These methods resulted in low protein yield (Kramer et al., 1976; Goodman et al., 1978; Peterson et al., 1982; Park et al., 1993; Ozyhar & Kochman, 1987). In this report a simple method of purification of hJHBP from Galleria mellonella (L.) larvae is described. Monoclonal antibodies against hJHBP were obtained and crosslinked to CNBr-activated Sepharose 4B. The hemolymph of G. mellonella was centrifuged and then chromatographed on Sephadex G-200 gel filtration column. Juvenile-hormone-binding activity containing material from Sephadex G-200 column was subjected to purification on an immunoaffinity column. Bound protein was eluted from anti-hJHBP Sepharose 4B gel by lowering pH to 3.0 with 200 mM citric acid 200 mM Na2HPO4 buffer. This method resulted in 320-fold purification of G. mellonella hJHBP with 56% yield.

scholarly journals Evidence for Glycosylation of the Juvenile-Hormone-Binding Protein from Galleria mellonella Hemolymph

1996 ◽  
Vol 242 (3) ◽  
pp. 741-746 ◽  
Author(s):  
Maria Duk ◽  
Hubert Krotkiewski ◽  
Eric Forest ◽  
Jan M. Rodriguez Parkitna ◽  
Marian Kochman ◽  
...  
Keyword(s):  
Juvenile Hormone ◽  
Galleria Mellonella ◽  
Binding Protein ◽  
Hormone Binding ◽  
Juvenile Hormone Binding Protein ◽  
Hormone Binding Protein

Juvenile Hormone Binding Protein and Transferrin from Galleria mellonella Share a Similar Structural Motif

2001 ◽  
Vol 382 (7) ◽  
Author(s):  
Dorota Krzyzanowska ◽  
Andrzej Ozyhar ◽  
Anna Lalik ◽  
Jan M. Rodriguez Parkitna ◽  
Jerzy Szkudlarek ◽  
...  
Keyword(s):  
Juvenile Hormone ◽  
Galleria Mellonella ◽  
Binding Protein ◽  
Structural Motif ◽  
Hormone Binding ◽  
Juvenile Hormone Binding Protein ◽  
Hormone Binding Protein

scholarly journals Identification of specific interaction of juvenile hormone binding protein with isocitrate dehydrogenase.

2011 ◽  
Vol 58 (1) ◽  
Author(s):  
Marta Zalewska ◽  
Andrzej Ożyhar ◽  
Marian Kochman
Keyword(s):  
Molecular Weight ◽  
Juvenile Hormone ◽  
Isocitrate Dehydrogenase ◽  
Galleria Mellonella ◽  
Binding Protein ◽  
Specific Interaction ◽  
Lipid Binding ◽  
Hormone Binding ◽  
Juvenile Hormone Binding Protein ◽  
Hormone Binding Protein

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.

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