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Capturing Post-Translational Modification-Triggered Protein-Protein Interactions Using Dual Noncanonical Amino Acid Mutagenesis.
Zheng, Yunan; Gilgenast, Martin J; Hauc, Sacha; Chatterjee, Abhishek.
Afiliación
  • Zheng Y; Department of Chemistry , Boston College , 2609 Beacon Street , Chestnut Hill , Massachusetts 02467 , United States.
  • Gilgenast MJ; Department of Chemistry , Boston College , 2609 Beacon Street , Chestnut Hill , Massachusetts 02467 , United States.
  • Hauc S; Department of Chemistry , Boston College , 2609 Beacon Street , Chestnut Hill , Massachusetts 02467 , United States.
  • Chatterjee A; Department of Chemistry , Boston College , 2609 Beacon Street , Chestnut Hill , Massachusetts 02467 , United States.
ACS Chem Biol ; 13(5): 1137-1141, 2018 05 18.
Article en En | MEDLINE | ID: mdl-29544052
Reversible post-translational modification (PTM) is a powerful and ubiquitous mechanism to regulate protein function. The mechanistic basis of the associated functional regulation by PTMs often involves the recruitment of interaction partners that selectively bind the modified protein. Identifying such functionally important protein-protein interactions that are uniquely triggered by PTMs remains difficult due to several technical challenges. To address this, here we develop technology to site-specifically incorporate two distinct noncanonical amino acids into recombinant proteins: one modeling a PTM of interest and the second harboring a photoaffinity probe. Using lysine-23 acetylation of histone 3 as a model system, we show that such dual-labeled "protein probes" can covalently capture its "reader" protein.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Procesamiento Proteico-Postraduccional / Mutagénesis Sitio-Dirigida / Sustitución de Aminoácidos / Aminoácidos Idioma: En Revista: ACS Chem Biol Año: 2018 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Procesamiento Proteico-Postraduccional / Mutagénesis Sitio-Dirigida / Sustitución de Aminoácidos / Aminoácidos Idioma: En Revista: ACS Chem Biol Año: 2018 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos