A Versatile Approach for Site-Specific Lysine Acylation in Proteins.
Angew Chem Int Ed Engl
; 56(6): 1643-1647, 2017 02 01.
Article
en En
| MEDLINE
| ID: mdl-28042700
ABSTRACT
Using amber suppression in coordination with a mutant pyrrolysyl-tRNA synthetase-tRNAPyl pair, azidonorleucine is genetically encoded in E. coli. Its genetic incorporation followed by traceless Staudinger ligation with a phosphinothioester allows the convenient synthesis of a protein with a site-specifically installed lysine acylation. By simply changing the phosphinothioester identity, any lysine acylation type could be introduced. Using this approach, we demonstrated that both lysine acetylation and lysine succinylation can be installed selectively in ubiquitin and synthesized histone H3 with succinylation at its K4 position (H3K4su). Using an H3K4su-H4 tetramer as a substrate, we further confirmed that Sirt5 is an active histone desuccinylase. Lysine succinylation is a recently identified post-translational modification. The reported technique makes it possible to explicate regulatory functions of this modification in proteins.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Procesamiento Proteico-Postraduccional
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Proteínas de Escherichia coli
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Escherichia coli
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Lisina
Idioma:
En
Revista:
Angew Chem Int Ed Engl
Año:
2017
Tipo del documento:
Article
País de afiliación:
Estados Unidos