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Genetically encoded bioorthogonal tryptophan decaging in living cells.
Zhu, Yuchao; Ding, Wenlong; Chen, Yulin; Shan, Ye; Liu, Chao; Fan, Xinyuan; Lin, Shixian; Chen, Peng R.
Afiliación
  • Zhu Y; New Cornerstone Science Laboratory, Synthetic and Functional Biomolecules Center, Key Laboratory of Bioorganic Chemistry and Molecular Engineering of Ministry of Education, Beijing National Laboratory for Molecular Sciences, College of Chemistry and Molecular Engineering, Peking University, Beijing,
  • Ding W; Zhejiang Provincial Key Laboratory for Cancer Molecular Cell Biology, Life Sciences Institute, Zhejiang University, Hangzhou, China.
  • Chen Y; Zhejiang Provincial Key Laboratory for Cancer Molecular Cell Biology, Life Sciences Institute, Zhejiang University, Hangzhou, China.
  • Shan Y; Center for Life Sciences, Shaoxing Institute, Zhejiang University, Shaoxing, China.
  • Liu C; New Cornerstone Science Laboratory, Synthetic and Functional Biomolecules Center, Key Laboratory of Bioorganic Chemistry and Molecular Engineering of Ministry of Education, Beijing National Laboratory for Molecular Sciences, College of Chemistry and Molecular Engineering, Peking University, Beijing,
  • Fan X; Peking-Tsinghua Center for Life Sciences, Peking University, Beijing, China.
  • Lin S; Zhejiang Provincial Key Laboratory for Cancer Molecular Cell Biology, Life Sciences Institute, Zhejiang University, Hangzhou, China.
  • Chen PR; Center for Life Sciences, Shaoxing Institute, Zhejiang University, Shaoxing, China.
Nat Chem ; 16(4): 533-542, 2024 Apr.
Article en En | MEDLINE | ID: mdl-38418535
ABSTRACT
Tryptophan (Trp) plays a critical role in the regulation of protein structure, interactions and functions through its π system and indole N-H group. A generalizable method for blocking and rescuing Trp interactions would enable the gain-of-function manipulation of various Trp-containing proteins in vivo, but generating such a platform remains challenging. Here we develop a genetically encoded N1-vinyl-caged Trp capable of rapid and bioorthogonal decaging through an optimized inverse electron-demand Diels-Alder reaction, allowing site-specific activation of Trp on a protein of interest in living cells. This chemical activation of a genetically encoded caged-tryptophan (Trp-CAGE) strategy enables precise activation of the Trp of interest underlying diverse important molecular interactions. We demonstrate the utility of Trp-CAGE across various protein families, such as catalase-peroxidases and kinases, as translation initiators and posttranslational modification readers, allowing the modulation of epigenetic signalling in a temporally controlled manner. Coupled with computer-aided prediction, our strategy paves the way for bioorthogonal Trp activation on more than 28,000 candidate proteins within their native cellular settings.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Triptófano / Proteínas Idioma: En Revista: Nat Chem Asunto de la revista: QUIMICA Año: 2024 Tipo del documento: Article Pais de publicación: Reino Unido
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Triptófano / Proteínas Idioma: En Revista: Nat Chem Asunto de la revista: QUIMICA Año: 2024 Tipo del documento: Article Pais de publicación: Reino Unido