New AdoMet Analogues as Tools for Enzymatic Transfer of Photo-Cross-Linkers and Capturing RNA-Protein Interactions
| Autor: | Armido Studer, Florian Mäsing, Fabian Muttach, Andrea Rentmeister |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
chemistry.chemical_classification
Methyltransferase 010405 organic chemistry Biomolecule Aryl Organic Chemistry EIF4E General Chemistry 010402 general chemistry 01 natural sciences Combinatorial chemistry Catalysis 0104 chemical sciences chemistry.chemical_compound chemistry Biochemistry Diazirine Nucleic acid Benzophenone Azide |
| Zdroj: | Chemistry - A European Journal. 23:5988-5993 |
| ISSN: | 0947-6539 |
| DOI: | 10.1002/chem.201605663 |
| Popis: | Elucidation of biomolecular interactions is of utmost importance in biochemistry. Photo-cross-linking offers the possibility to precisely determine RNA-protein interactions. However, despite the inherent specificity of enzymes, approaches for site-specific introduction of photo-cross-linking moieties into nucleic acids are scarce. Methyltransferases in combination with synthetic analogues of their natural cosubstrate S-adenosyl-l-methionine (AdoMet) allow for the post-synthetic site-specific modification of biomolecules. We report on three novel AdoMet analogues bearing the most widespread photo-cross-linking moieties (aryl azide, diazirine, and benzophenone). We show that these photo-cross-linkers can be enzymatically transferred to the methyltransferase target, that is, the mRNA cap, with high efficiency. Photo-cross-linking of the resulting modified mRNAs with the cap interacting protein eIF4E was successful with aryl azide and diazirine but not benzophenone, reflecting the affinity of the modified 5' caps. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
| Nepřihlášeným uživatelům se plný text nezobrazuje | K zobrazení výsledku je třeba se přihlásit. |