Cargando…
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...
Autores principales: | , , , |
---|---|
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 |
_version_ | 1782194745160761344 |
---|---|
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. |
format | Text |
id | pubmed-3009751 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT johnsonmatthew targetedaminoterminalacetylationofrecombinantproteinsinecoli AT coultonarthurt targetedaminoterminalacetylationofrecombinantproteinsinecoli AT geevesmichaela targetedaminoterminalacetylationofrecombinantproteinsinecoli AT mulvihilldanielp targetedaminoterminalacetylationofrecombinantproteinsinecoli |