title: Reversible labeling of native and fusion-protein motifs.
abstract: 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 Escherichia coli acyl carrier protein for visualization and functional studies. We use this iterative enzymatic methodology in vitro to reversibly label acyl carrier protein variants and apply these tools to NMR structural studies of protein-substrate interactions.
authors.affiliation: Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California, USA.
authors.forename: Nicolas M
authors.initials: NM
authors.lastname: Kosa
authors.forename: Robert W
authors.initials: RW
authors.lastname: Haushalter
authors.forename: Andrew R
authors.initials: AR
authors.lastname: Smith
authors.forename: Michael D
authors.initials: MD
authors.lastname: Burkart
mesh_terms: D000213:Acyl Carrier Protein / Q000737:chemistry*; D020816:Amino Acid Motifs; D009682:Magnetic Resonance Spectroscopy; D011499:Protein Processing, Post-Translational; D011993:Recombinant Fusion Proteins / Q000737:chemistry*
chemical_list: D000213:Acyl Carrier Protein; D011993:Recombinant Fusion Proteins