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Reversible Chemoenzymatic Labeling of Native and Fusion Carrier Protein Motifs

The reversible covalent attachment of chemical probes to proteins has long been sought as a means to visualize and manipulate proteins. Here we demonstrate the full reversibility of post-translational custom pantetheine modification of E. coli acyl carrier protein (ACP) for visualization and functio...

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Detalles Bibliográficos
Autores principales: Kosa, Nicolas M., Haushalter, Robert W., Smith, Andrew R., Burkart, Michael D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4128096/
https://www.ncbi.nlm.nih.gov/pubmed/22983458
http://dx.doi.org/10.1038/nmeth.2175
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author Kosa, Nicolas M.
Haushalter, Robert W.
Smith, Andrew R.
Burkart, Michael D.
author_facet Kosa, Nicolas M.
Haushalter, Robert W.
Smith, Andrew R.
Burkart, Michael D.
author_sort Kosa, Nicolas M.
collection PubMed
description The reversible covalent attachment of chemical probes to proteins has long been sought as a means to visualize and manipulate proteins. Here we demonstrate the full reversibility of post-translational custom pantetheine modification of E. coli acyl carrier protein (ACP) for visualization and functional studies. We utilize this iterative enzymatic methodology in vitro for reversible labeling variants and apply these tools to Nuclear Magnetic Resonance (NMR) structural studies of protein-substrate interactions.
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spelling pubmed-41280962014-08-11 Reversible Chemoenzymatic Labeling of Native and Fusion Carrier Protein Motifs Kosa, Nicolas M. Haushalter, Robert W. Smith, Andrew R. Burkart, Michael D. Nat Methods Article The reversible covalent attachment of chemical probes to proteins has long been sought as a means to visualize and manipulate proteins. Here we demonstrate the full reversibility of post-translational custom pantetheine modification of E. coli acyl carrier protein (ACP) for visualization and functional studies. We utilize this iterative enzymatic methodology in vitro for reversible labeling variants and apply these tools to Nuclear Magnetic Resonance (NMR) structural studies of protein-substrate interactions. 2012-09-16 2012-10 /pmc/articles/PMC4128096/ /pubmed/22983458 http://dx.doi.org/10.1038/nmeth.2175 Text en http://www.nature.com/authors/editorial_policies/license.html#terms 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
Kosa, Nicolas M.
Haushalter, Robert W.
Smith, Andrew R.
Burkart, Michael D.
Reversible Chemoenzymatic Labeling of Native and Fusion Carrier Protein Motifs
title Reversible Chemoenzymatic Labeling of Native and Fusion Carrier Protein Motifs
title_full Reversible Chemoenzymatic Labeling of Native and Fusion Carrier Protein Motifs
title_fullStr Reversible Chemoenzymatic Labeling of Native and Fusion Carrier Protein Motifs
title_full_unstemmed Reversible Chemoenzymatic Labeling of Native and Fusion Carrier Protein Motifs
title_short Reversible Chemoenzymatic Labeling of Native and Fusion Carrier Protein Motifs
title_sort reversible chemoenzymatic labeling of native and fusion carrier protein motifs
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4128096/
https://www.ncbi.nlm.nih.gov/pubmed/22983458
http://dx.doi.org/10.1038/nmeth.2175
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