Sortagging: a versatile method for protein labeling
- 23 September 2007
- journal article
- Published by Springer Science and Business Media LLC in Nature Chemical Biology
- Vol. 3 (11), 707-708
- https://doi.org/10.1038/nchembio.2007.31
Abstract
Genetically encoded reporter constructs that yield fluorescently labeled fusion proteins are a powerful tool for observing cell biological phenomena, but they have limitations. Sortagging (sortase-mediated transpeptidation) is a versatile chemoenzymatic system for site-specific labeling of proteins with small (<2 kDa) probes. Sortagging combines the precision of a genetically encoded tag with the specificity of an enzymatic reaction and the ease and chemical versatility of peptide synthesis. Here we apply this technique to proteins in vitro and on the surface of living cells.Keywords
This publication has 15 references indexed in Scilit:
- Synthesis of Biologically Active Peptide Nucleic Acid−Peptide Conjugates by Sortase-Mediated LigationThe Journal of Organic Chemistry, 2007
- Fluorescence imaging of amyloid formation in living cells by a functional, tetracysteine-tagged α-synucleinNature Methods, 2007
- Sortase A as a Novel Molecular “Stapler” for Sequence-Specific Protein ConjugationBioconjugate Chemistry, 2007
- Targeting proteins to the cell wall of sporulating Bacillus anthracisMolecular Microbiology, 2006
- Site-specific labeling of proteins with small molecules in live cellsCurrent Opinion in Biotechnology, 2005
- Sortase-Mediated Protein Ligation: A New Method for Protein EngineeringJournal of the American Chemical Society, 2004
- Overexpression and Mislocalization of a Tail‐Anchored GFP Redefines the Identity of Peroxisomal ERTraffic, 2003
- Development and Use of Fluorescent Protein Markers in Living CellsScience, 2003
- Multicolor and Electron Microscopic Imaging of Connexin TraffickingScience, 2002
- Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus at the LPXTG motifProceedings of the National Academy of Sciences of the United States of America, 1999