Academic Journal
Formaldehyde reacts with N-terminal proline residues to give bicyclic aminals
| Τίτλος: | Formaldehyde reacts with N-terminal proline residues to give bicyclic aminals |
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| Συγγραφείς: | John, T, Pires, E, Hester, SS, Salah, E, Hopkinson, RJ, Schofield, CJ |
| Στοιχεία εκδότη: | Springer Nature |
| Έτος έκδοσης: | 2023 |
| Συλλογή: | Oxford University Research Archive (ORA) |
| Περιγραφή: | Formaldehyde (HCHO) is a potent electrophile that is toxic above threshold levels, but which is also produced in the nuclei of eukaryotic cells by demethylases. We report studies with the four canonical human histones revealing that histone H2B reacts with HCHO, including as generated by a histone demethylase, to give a stable product. NMR studies show that HCHO reacts with the N-terminal proline and associated amide of H2B to give a 5,5-bicyclic aminal that is relatively stable to competition with HCHO scavengers. While the roles of histone modification by this reaction require further investigation, we demonstrated the potential of N-terminal aminal formation to modulate protein function by conducting biochemical and cellular studies on the effects of HCHO on catalysis by 4-oxalocrotonate tautomerase, which employs a nucleophilic N-terminal proline. The results suggest that reactions of N-terminal residues with HCHO and other aldehydes have potential to alter protein function. |
| Τύπος εγγράφου: | article in journal/newspaper |
| Γλώσσα: | English |
| DOI: | 10.1038/s42004-022-00801-5 |
| Διαθεσιμότητα: | https://doi.org/10.1038/s42004-022-00801-5 https://ora.ox.ac.uk/objects/uuid:ec88e447-d3ed-44f9-b895-7ad3102607f8 |
| Rights: | info:eu-repo/semantics/openAccess ; CC Attribution (CC BY) |
| Αριθμός Καταχώρησης: | edsbas.8DB13EB3 |
| Βάση Δεδομένων: | BASE |
| DOI: | 10.1038/s42004-022-00801-5 |
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