| Texto completo | |
| Autor(es): Mostrar menos - |
Weller, Caroline E.
;
Dhall, Abhinav
;
Ding, Feizhi
;
Linares, Edlaine
;
Whedon, Samuel D.
;
Senger, Nicholas A.
;
Tyson, Elizabeth L.
;
Bagert, John D.
;
Li, Xiaosong
;
Augusto, Ohara
;
Chatterjee, Champak
Número total de Autores: 11
|
| Tipo de documento: | Artigo Científico |
| Fonte: | NATURE COMMUNICATIONS; v. 7, SEP 29 2016. |
| Citações Web of Science: | 19 |
| Resumo | |
Access to protein substrates homogenously modified by ubiquitin (Ub) is critical for biophysical and biochemical investigations aimed at deconvoluting the myriad biological roles for Ub. Current chemical strategies for protein ubiquitylation, however, employ temporary ligation auxiliaries that are removed under harsh denaturing conditions and have limited applicability. We report an unprecedented aromatic thiol-mediated N-O bond cleavage and its application towards native chemical ubiquitylation with the ligation auxiliary 2-aminooxyethanethiol. Our interrogation of the reaction mechanism suggests a disulfide radical anion as the active species capable of cleaving the N-O bond. The successful semisynthesis of full-length histone H2B modified by the small ubiquitin-like modifier-3 (SUMO-3) protein further demonstrates the generalizability and compatibility of our strategy with folded proteins. (AU) | |
| Processo FAPESP: | 13/07937-8 - Redoxoma |
| Beneficiário: | Ohara Augusto |
| Modalidade de apoio: | Auxílio à Pesquisa - Centros de Pesquisa, Inovação e Difusão - CEPIDs |