Your browser doesn't support javascript.
loading
Generation of phospho-ubiquitin variants by orthogonal translation reveals codon skipping.
George, Susanna; Aguirre, Jacob D; Spratt, Donald E; Bi, Yumin; Jeffery, Madeline; Shaw, Gary S; O'Donoghue, Patrick.
Afiliación
  • George S; Department of Biochemistry, The University of Western Ontario, London, Canada.
  • Aguirre JD; Department of Biochemistry, The University of Western Ontario, London, Canada.
  • Spratt DE; Department of Biochemistry, The University of Western Ontario, London, Canada.
  • Bi Y; Department of Biochemistry, The University of Western Ontario, London, Canada.
  • Jeffery M; Department of Biochemistry, The University of Western Ontario, London, Canada.
  • Shaw GS; Department of Biochemistry, The University of Western Ontario, London, Canada.
  • O'Donoghue P; Department of Chemistry, The University of Western Ontario, London, Canada.
FEBS Lett ; 590(10): 1530-42, 2016 05.
Article en En | MEDLINE | ID: mdl-27096575
The activity of the Parkinson's disease-linked E3 ligase parkin is stimulated by phosphorylation at ubiquitin Ser65 (pUb(S65) ). The role of other ubiquitin phospho-sites and their kinases are unknown. We produced pUb variants (pS7, pS12, pS20, pS57, pS65) by genetically encoding phosphoserine with the UAG codon. In release factor-deficient Escherichia coli (ΔRF1), intended to enhance UAG read-through, we discovered ubiquitin variants lacking the UAG-encoded residue, demonstrating previously undocumented +3 frame shifting. We successfully purified each pUb variant from mistranslated products. While pUb(S20) failed to stimulate parkin, parkin was partially active with pUb(S12) . We observed significant ubiquitination when pUb(S65) was the sole substrate.
Asunto(s)
Palabras clave
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: Fosfoserina / Codón de Terminación / Ubiquitina Límite: Humans Idioma: En Revista: FEBS Lett Año: 2016 Tipo del documento: Article País de afiliación: Canadá 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: Fosfoserina / Codón de Terminación / Ubiquitina Límite: Humans Idioma: En Revista: FEBS Lett Año: 2016 Tipo del documento: Article País de afiliación: Canadá Pais de publicación: Reino Unido