Design, Synthesis, and Insecticidal Evaluation of New Benzoylureas Containing Amide and Sulfonate Groups Based on the Sulfonylurea Receptor Protein Binding Site for Diflubenzuron and Glibenclamide

Analysis of the DNA sequence upstream of the previously isolated Enterobacter cloacae UW4 ACC deaminase gene (Shah et al. 1998) suggests that this segment contains several features that are thought to be involved in the transcriptional regulation of this gene. These features include half of a CRP (cAMP receptor protein) binding site, an FNR (fumarate-nitrate reduction) regulatory protein binding site, an LRP (leucine responsive regulatory protein) binding site, and an LRP-like protein coding region. ACC deaminase activity was measured following growth of either various Escherichia coli strains carrying a plasmid that contained the Enterobacter cloacae UW4 ACC deaminase gene, or of Enterobacter cloacae UW4. Variables that were compared include aerobic versus anaerobic conditions, the presence and absence of ACC in the growth medium, addition of leucine to the medium, and bacterial strains that did or did not contain either lrp or fnr genes. The data reported are consistent with the involvement of most, if not all, of the above mentioned potential regulatory regions in the expression of ACC deaminase.Key words: 1-aminocyclopropane-1-carboxylate, ACC, plant growth-promoting rhizobacteria, ACC deaminase, Enterobacter cloacae, leucine responsive regulatory protein.

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The ribosomal protein binding site in Saccharomyces cerevisiae ribosomal 5 S RNA. A conserved protein binding site in 5 S RNA.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)36006-x ◽

1979 ◽

Vol 254 (16) ◽

pp. 7724-7729 ◽

Cited By ~ 3

Author(s):

R.N. Nazar

Keyword(s):

Saccharomyces Cerevisiae ◽

Protein Binding ◽

Ribosomal Protein ◽

Binding Site ◽

Protein Binding Site

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Functional homology between the yeast regulatory proteins GAL4 and LAC9: LAC9-mediated transcriptional activation in Kluyveromyces lactis involves protein binding to a regulatory sequence homologous to the GAL4 protein-binding site.

Molecular and Cellular Biology ◽

10.1128/mcb.7.12.4400 ◽

1987 ◽

Vol 7 (12) ◽

pp. 4400-4406 ◽

Cited By ~ 50

Author(s):

K D Breunig ◽

P Kuger

Keyword(s):

Protein Binding ◽

Binding Site ◽

Transcriptional Activation ◽

Kluyveromyces Lactis ◽

Regulatory Protein ◽

Binding Activity ◽

Protein Binding Site ◽

Regulatory Sequence ◽

Functional Homology ◽

Beta Galactosidase

As shown previously, the beta-galactosidase gene of Kluyveromyces lactis is transcriptionally regulated via an upstream activation site (UASL) which contains a sequence homologous to the GAL4 protein-binding site in Saccharomyces cerevisiae (M. Ruzzi, K.D. Breunig, A.G. Ficca, and C.P. Hollenberg, Mol. Cell. Biol. 7:991-997, 1987). Here we demonstrate that the region of homology specifically binds a K. lactis regulatory protein. The binding activity was detectable in protein extracts from wild-type cells enriched for DNA-binding proteins by heparin affinity chromatography. These extracts could be used directly for DNase I and exonuclease III protection experiments. A lac9 deletion strain, which fails to induce the beta-galactosidase gene, did not contain the binding factor. The homology of LAC9 protein with GAL4 (J.M. Salmeron and S. A. Johnston, Nucleic Acids Res. 14:7767-7781, 1986) strongly suggests that LAC9 protein binds directly to UASL and plays a role similar to that of GAL4 in regulating transcription.

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An Internal Polypyrimidine-Tract-Binding Protein-Binding Site in the Hepatitis C Virus RNA Attenuates Translation, Which Is Relieved by the 3′-Untranslated Sequence

Virology ◽

10.1006/viro.1998.9541 ◽

1999 ◽

Vol 254 (2) ◽

pp. 288-296 ◽

Cited By ~ 82

Author(s):

Takayoshi Ito ◽

Michael M.C. Lai

Keyword(s):

Hepatitis C Virus ◽

Hepatitis C ◽

Protein Binding ◽

Binding Site ◽

Protein Binding Site ◽

Polypyrimidine Tract ◽

Hepatitis C Virus Rna ◽

Untranslated Sequence ◽

Polypyrimidine Tract Binding Protein ◽

Virus Rna

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Valine-279 Deletion–Mutation on Arginine Vasopressin Receptor 2 Causes Obstruction in G-Protein Binding Site: A Clinical Nephrogenic Diabetes Insipidus Case and Its Sub-Molecular Pathogenic Analysis

Biomedicines ◽

10.3390/biomedicines9030301 ◽

2021 ◽

Vol 9 (3) ◽

pp. 301

Author(s):

Ming-Chun Chen ◽

Yu-Chao Hsiao ◽

Chun-Chun Chang ◽

Sheng-Feng Pan ◽

Chih-Wen Peng ◽

...

Keyword(s):

Structural Analysis ◽

Protein Binding ◽

Diabetes Insipidus ◽

Binding Site ◽

G Protein ◽

Arginine Vasopressin ◽

Nephrogenic Diabetes Insipidus ◽

Md Simulations ◽

Protein Binding Site ◽

Vasopressin Receptor

Congenital nephrogenic diabetes insipidus (CNDI) is a genetic disorder caused by mutations in arginine vasopressin receptor 2 (AVPR2) or aquaporin 2 genes, rendering collecting duct cells insensitive to the peptide hormone arginine vasopressin stimulation for water reabsorption. This study reports a first identified AVPR2 mutation in Taiwan and demonstrates our effort to understand the pathogenesis caused by applying computational structural analysis tools. The CNDI condition of an 8-month-old male patient was confirmed according to symptoms, family history, and DNA sequence analysis. The patient was identified to have a valine 279 deletion–mutation in the AVPR2 gene. Cellular experiments using mutant protein transfected cells revealed that mutated AVPR2 is expressed successfully in cells and localized on cell surfaces. We further analyzed the pathogenesis of the mutation at sub-molecular levels via long-term molecular dynamics (MD) simulations and structural analysis. The MD simulations showed while the structure of the extracellular ligand-binding domain remains unchanged, the mutation alters the direction of dynamic motion of AVPR2 transmembrane helix 6 toward the center of the G-protein binding site, obstructing the binding of G-protein, thus likely disabling downstream signaling. This study demonstrated that the computational approaches can be powerful tools for obtaining valuable information on the pathogenesis induced by mutations in G-protein-coupled receptors. These methods can also be helpful in providing clues on potential therapeutic strategies for CNDI.

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