Design of artificial transcriptional activators with rigid poly-L-proline linkers Journal Article
| Authors: | Arora, P. S.; Ansari, A. Z.; Best, T. P.; Ptashne, M.; Dervan, P. B. |
| Article Title: | Design of artificial transcriptional activators with rigid poly-L-proline linkers |
| Abstract: | Typical eukaryotic transcriptional activators are composed of distinct functional domains, including a DNA binding domain and an activating domain. Artificial transcription factors have been designed wherein the DNA binding domain is a minor groove DNA binding hairpin polyamide linked by a flexible tether to short activating peptides, typically 16-20 residues in size. In this study, the linker between the polyamide and the peptide was altered in an incremental fashion using rigid oligoproline "molecular rulers" in the 18-45 Å length range. We find that there is an optimal linker length which separates the DNA and the activation region for transcription activation. |
| Keywords: | dna-binding proteins; protein conformation; protein domain; transcription initiation; transcription factor; peptide; structure-activity relationship; transcription factors; dna; amino acid sequence; molecular sequence data; peptides; base sequence; models, molecular; protein structure, tertiary; chemical structure; dna binding; eukaryote; synthetic peptide; cross-linking reagents; trans-activation (genetics); biomimetic materials; proline derivative; transcription activation; article; polyamides; polyamide |
| Journal Title: | Journal of the American Chemical Society |
| Volume: | 124 |
| Issue: | 44 |
| ISSN: | 0002-7863 |
| Publisher: | American Chemical Society |
| Date Published: | 2002-11-06 |
| Start Page: | 13067 |
| End Page: | 13071 |
| Language: | English |
| DOI: | 10.1021/ja0208355 |
| PUBMED: | 12405833 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Export Date: 14 November 2014 -- Source: Scopus |
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