Enzyme-catalyzed expressed protein ligation

Expressed protein ligation is a valuable method for protein semisynthesis that involves the reaction of recombinant protein C-terminal thioesters with N-Cys containing peptides but the requirement of a Cys residue at the ligation junction can limit its use. Here we employ subtiligase variants to eff...

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Detalles Bibliográficos
Autores principales: Henager, Samuel H., Chu, Nam, Chen, Zan, Bolduc, David, Dempsey, Daniel R., Hwang, Yousang, Wells, James, Cole, Philip A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2016
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5088058/
https://www.ncbi.nlm.nih.gov/pubmed/27669326
http://dx.doi.org/10.1038/nmeth.4004
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author Henager, Samuel H.
Chu, Nam
Chen, Zan
Bolduc, David
Dempsey, Daniel R.
Hwang, Yousang
Wells, James
Cole, Philip A.
author_facet Henager, Samuel H.
Chu, Nam
Chen, Zan
Bolduc, David
Dempsey, Daniel R.
Hwang, Yousang
Wells, James
Cole, Philip A.
author_sort Henager, Samuel H.
collection PubMed
description Expressed protein ligation is a valuable method for protein semisynthesis that involves the reaction of recombinant protein C-terminal thioesters with N-Cys containing peptides but the requirement of a Cys residue at the ligation junction can limit its use. Here we employ subtiligase variants to efficiently ligate Cys-free peptides to protein thioesters. Using this method, we have more accurately determined the effect of C-terminal phosphorylation on the tumor suppressor protein PTEN.
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spelling pubmed-50880582017-03-26 Enzyme-catalyzed expressed protein ligation Henager, Samuel H. Chu, Nam Chen, Zan Bolduc, David Dempsey, Daniel R. Hwang, Yousang Wells, James Cole, Philip A. Nat Methods Article Expressed protein ligation is a valuable method for protein semisynthesis that involves the reaction of recombinant protein C-terminal thioesters with N-Cys containing peptides but the requirement of a Cys residue at the ligation junction can limit its use. Here we employ subtiligase variants to efficiently ligate Cys-free peptides to protein thioesters. Using this method, we have more accurately determined the effect of C-terminal phosphorylation on the tumor suppressor protein PTEN. 2016-09-26 2016-11 /pmc/articles/PMC5088058/ /pubmed/27669326 http://dx.doi.org/10.1038/nmeth.4004 Text en Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Henager, Samuel H.
Chu, Nam
Chen, Zan
Bolduc, David
Dempsey, Daniel R.
Hwang, Yousang
Wells, James
Cole, Philip A.
Enzyme-catalyzed expressed protein ligation
title Enzyme-catalyzed expressed protein ligation
title_full Enzyme-catalyzed expressed protein ligation
title_fullStr Enzyme-catalyzed expressed protein ligation
title_full_unstemmed Enzyme-catalyzed expressed protein ligation
title_short Enzyme-catalyzed expressed protein ligation
title_sort enzyme-catalyzed expressed protein ligation
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5088058/
https://www.ncbi.nlm.nih.gov/pubmed/27669326
http://dx.doi.org/10.1038/nmeth.4004
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