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Protein-Protein Fusion Catalyzed by Sortase A
Chimeric proteins boast widespread use in areas ranging from cell biology to drug delivery. Post-translational protein fusion using the bacterial transpeptidase sortase A provides an attractive alternative when traditional gene fusion fails. We describe use of this enzyme for in vitro protein ligati...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3071835/ https://www.ncbi.nlm.nih.gov/pubmed/21494692 http://dx.doi.org/10.1371/journal.pone.0018342 |
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author | Levary, David A. Parthasarathy, Ranganath Boder, Eric T. Ackerman, Margaret E. |
author_facet | Levary, David A. Parthasarathy, Ranganath Boder, Eric T. Ackerman, Margaret E. |
author_sort | Levary, David A. |
collection | PubMed |
description | Chimeric proteins boast widespread use in areas ranging from cell biology to drug delivery. Post-translational protein fusion using the bacterial transpeptidase sortase A provides an attractive alternative when traditional gene fusion fails. We describe use of this enzyme for in vitro protein ligation and report the successful fusion of 10 pairs of protein domains with preserved functionality — demonstrating the robust and facile nature of this reaction. |
format | Text |
id | pubmed-3071835 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-30718352011-04-14 Protein-Protein Fusion Catalyzed by Sortase A Levary, David A. Parthasarathy, Ranganath Boder, Eric T. Ackerman, Margaret E. PLoS One Research Article Chimeric proteins boast widespread use in areas ranging from cell biology to drug delivery. Post-translational protein fusion using the bacterial transpeptidase sortase A provides an attractive alternative when traditional gene fusion fails. We describe use of this enzyme for in vitro protein ligation and report the successful fusion of 10 pairs of protein domains with preserved functionality — demonstrating the robust and facile nature of this reaction. Public Library of Science 2011-04-06 /pmc/articles/PMC3071835/ /pubmed/21494692 http://dx.doi.org/10.1371/journal.pone.0018342 Text en Levary 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 Levary, David A. Parthasarathy, Ranganath Boder, Eric T. Ackerman, Margaret E. Protein-Protein Fusion Catalyzed by Sortase A |
title | Protein-Protein Fusion Catalyzed by Sortase A |
title_full | Protein-Protein Fusion Catalyzed by Sortase A |
title_fullStr | Protein-Protein Fusion Catalyzed by Sortase A |
title_full_unstemmed | Protein-Protein Fusion Catalyzed by Sortase A |
title_short | Protein-Protein Fusion Catalyzed by Sortase A |
title_sort | protein-protein fusion catalyzed by sortase a |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3071835/ https://www.ncbi.nlm.nih.gov/pubmed/21494692 http://dx.doi.org/10.1371/journal.pone.0018342 |
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