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research article

A general method for the covalent labeling of fusion proteins with small molecules in vivo

Keppler, Antje  
•
Gendreizig, Susanne  
•
Gronemeyer, Thomas  
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2003
Nature Biotechnology

Characterizing the movement, interactions, and chem. microenvironment of a protein inside the living cell is crucial to a detailed understanding of its function. Most strategies aimed at realizing this objective are based on genetically fusing the protein of interest to a reporter protein that monitors changes in the environment of the coupled protein. Examples include fusions with fluorescent proteins, the yeast two-hybrid system, and split ubiquitin. However, these techniques have various limitations, and considerable effort is being devoted to specific labeling of proteins in vivo with small synthetic mols. capable of probing and modulating their function. These approaches are currently based on the noncovalent binding of a small mol. to a protein, the formation of stable complexes between biarsenical compds. and peptides contg. cysteines, or the use of biotin acceptor domains. Here we describe a general method for the covalent labeling of fusion proteins in vivo that complements existing methods for noncovalent labeling of proteins and that may open up new ways of studying proteins in living cells.

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Type
research article
DOI
10.1038/nbt765
Web of Science ID

WOS:000180209200030

Author(s)
Keppler, Antje  
Gendreizig, Susanne  
Gronemeyer, Thomas  
Pick, Horst  
Vogel, Horst  
Johnsson, Kai  
Date Issued

2003

Published in
Nature Biotechnology
Volume

21

Issue

1

Start page

86

End page

89

Editorial or Peer reviewed

REVIEWED

Written at

EPFL

EPFL units
LIP  
LCPPM  
Available on Infoscience
February 27, 2006
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/226640
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