A Universal Expression Tag for Structural and Functional Studies of Proteins

Modified ubiquitin sequences, each completed with a His tag and a TEV cleavage site, were designed to enhance the expression of protein/peptide targets. With this new system we have been able to characterize several peptide–protein interactions by ITC and by NMR and CD spectroscopic methods, includi...

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Bibliographic Details
Published in:Chembiochem : a European journal of chemical biology 2012-05, Vol.13 (7), p.959-963
Main Authors: Rogov, Vladimir V., Rozenknop, Alexis, Rogova, Natalia Yu, Löhr, Frank, Tikole, Suhas, Jaravine, Victor, Güntert, Peter, Dikic, Ivan, Dötsch, Volker
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Base Sequence
Expressed Sequence Tags - chemistry
Genetic Vectors - genetics
Models, Molecular
Molecular Sequence Data
NMR spectroscopy
Nuclear Magnetic Resonance, Biomolecular - methods
Protein Biosynthesis
protein expression
Protein Structure, Tertiary
Proteins - chemistry
Proteins - genetics
Recombinant Fusion Proteins - biosynthesis
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - genetics
solubility
tags
ubiquitin
Ubiquitin - genetics
Ubiquitin - metabolism
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Description
Summary:Modified ubiquitin sequences, each completed with a His tag and a TEV cleavage site, were designed to enhance the expression of protein/peptide targets. With this new system we have been able to characterize several peptide–protein interactions by ITC and by NMR and CD spectroscopic methods, including the interactions of LIR domains with autophagy modifiers.
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.201200045