ParkinsonCanadaV1, Main, Exploration, bibRecord, 000344

Generation of phospho-ubiquitin variants by orthogonal translation reveals codon skipping.

Identifieur interne : 000344 ( Main/Exploration ); précédent : 000343; suivant : 000345

Generation of phospho-ubiquitin variants by orthogonal translation reveals codon skipping.

Auteurs : Susanna George [Canada] ; Jacob D. Aguirre [Canada] ; Donald E. Spratt [Canada] ; Yumin Bi [Canada] ; Madeline Jeffery [Canada] ; Gary S. Shaw [Canada] ; Patrick O'Donoghue [Canada]

Source :

FEBS letters [ 1873-3468 ] ; 2016.

RBID : pubmed:27096575

Abstract

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.

DOI: 10.1002/1873-3468.12182
PubMed: 27096575

Affiliations:

Le document en format XML

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<front><div type="abstract" xml:lang="en">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.</div>
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La maladie de Parkinson au Canada (serveur d'exploration)

Generation of phospho-ubiquitin variants by orthogonal translation reveals codon skipping.

Generation of phospho-ubiquitin variants by orthogonal translation reveals codon skipping.

Source :

Abstract

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	La maladie de Parkinson au Canada (serveur d'exploration)
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