Stadler, K., Liu, N., Trotman, L. C., Hiltpold, A., Caderas, G., Klauser, S., Hehlgans, T., Gutte, B. (1995) Design, synthesis, and characterization of HIV-1 enhancer-binding polypeptides derived from bacteriophage 434 repressor. International Journal of Peptide and Protein Research, 46 (3-4). pp. 333-340. ISSN 03678377 (ISSN)
Abstract
We have designed and synthesized HlV-1 enhancer-binding polypeptides that were derived from bacteriophage 434 repressor. These peptides were 39-54 residues long and contained either the recognition helix or the entire helix-turn-helix motif of the DNA-binding domain of 434 repressor. The dissociation constant of the complex formed between the standard peptide (R42) and a synthetic 70-bp HIV enhancer DNA was ca. 10-8 M. The specificity of the interaction of R42 with the two HIV enhancers was demonstrated by competitive band shift assays, stepwise displacement of the p50 subunit of transcription factor NF-κB from its two HIV enhancer binding sites, and DNase I footprinting; R42 seemed to protect best the two TTTCC sequences of the HIV enhancers against digestion by DNase I. R42 analogues with mutated recognition helix had lower DNA binding specificity. It remains to be investigated whether our artificial HIV enhancer-binding polypeptides are active in vivo.
| Item Type: | Paper |
|---|---|
| Additional Information: | PubMed ID: 8537188 |
| Uncontrolled Keywords: | Artificial HIV enhancer-binding polypeptides Bacteriophage 434 repressor-operator model system Band shift Circular dichroism DNase I foot-printing NF-κB antivirus agent repressor protein article bacteriophage dna binding drug design drug synthesis gene expression regulation human immunodeficiency virus 1 repressor gene virus transcription Amino Acid Sequence Bacteriophages Base Sequence Binding Sites Chromatography, Affinity Deoxyribonuclease I DNA Footprinting DNA, Viral DNA-Binding Proteins HIV Enhancer HIV-1 Molecular Sequence Data Repressor Proteins Spectrophotometry, Ultraviolet |
| Subjects: | diseases & disorders > viral diseases > HIV bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > DNA binding protein |
| CSHL Authors: | |
| Communities: | CSHL labs > Trotman lab |
| Depositing User: | Brian Soldo |
| Date: | 1995 |
| Date Deposited: | 23 Mar 2012 16:06 |
| Last Modified: | 08 May 2013 16:51 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/25524 |
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