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Targeted Amino-Terminal Acetylation of Recombinant Proteins in E. coli

One major limitation in the expression of eukaryotic proteins in bacteria is an inability to post-translationally modify the expressed protein. Amino-terminal acetylation is one such modification that can be essential for protein function. By co-expressing the fission yeast NatB complex with the tar...

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Detalles Bibliográficos
Autores principales: Johnson, Matthew, Coulton, Arthur T., Geeves, Michael A., Mulvihill, Daniel P.
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3009751/
https://www.ncbi.nlm.nih.gov/pubmed/21203426
http://dx.doi.org/10.1371/journal.pone.0015801
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author Johnson, Matthew
Coulton, Arthur T.
Geeves, Michael A.
Mulvihill, Daniel P.
author_facet Johnson, Matthew
Coulton, Arthur T.
Geeves, Michael A.
Mulvihill, Daniel P.
author_sort Johnson, Matthew
collection PubMed
description One major limitation in the expression of eukaryotic proteins in bacteria is an inability to post-translationally modify the expressed protein. Amino-terminal acetylation is one such modification that can be essential for protein function. By co-expressing the fission yeast NatB complex with the target protein in E.coli, we report a simple and widely applicable method for the expression and purification of functional N-terminally acetylated eukaryotic proteins.
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spelling pubmed-30097512011-01-03 Targeted Amino-Terminal Acetylation of Recombinant Proteins in E. coli Johnson, Matthew Coulton, Arthur T. Geeves, Michael A. Mulvihill, Daniel P. PLoS One Research Article One major limitation in the expression of eukaryotic proteins in bacteria is an inability to post-translationally modify the expressed protein. Amino-terminal acetylation is one such modification that can be essential for protein function. By co-expressing the fission yeast NatB complex with the target protein in E.coli, we report a simple and widely applicable method for the expression and purification of functional N-terminally acetylated eukaryotic proteins. Public Library of Science 2010-12-23 /pmc/articles/PMC3009751/ /pubmed/21203426 http://dx.doi.org/10.1371/journal.pone.0015801 Text en Johnson et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Johnson, Matthew
Coulton, Arthur T.
Geeves, Michael A.
Mulvihill, Daniel P.
Targeted Amino-Terminal Acetylation of Recombinant Proteins in E. coli
title Targeted Amino-Terminal Acetylation of Recombinant Proteins in E. coli
title_full Targeted Amino-Terminal Acetylation of Recombinant Proteins in E. coli
title_fullStr Targeted Amino-Terminal Acetylation of Recombinant Proteins in E. coli
title_full_unstemmed Targeted Amino-Terminal Acetylation of Recombinant Proteins in E. coli
title_short Targeted Amino-Terminal Acetylation of Recombinant Proteins in E. coli
title_sort targeted amino-terminal acetylation of recombinant proteins in e. coli
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3009751/
https://www.ncbi.nlm.nih.gov/pubmed/21203426
http://dx.doi.org/10.1371/journal.pone.0015801
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