1. Recombinant expression and purification of human TATA binding protein using a chimeric fusion.
- Author
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Silvers R, Saxena K, Kudlinzki D, and Schwalbe H
- Subjects
- Amino Acid Sequence, Escherichia coli genetics, Humans, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Protein Folding, Recombinant Fusion Proteins chemistry, Recombinant Fusion Proteins genetics, Recombinant Fusion Proteins isolation & purification, Recombinant Fusion Proteins metabolism, TATA-Box Binding Protein chemistry, TATA-Box Binding Protein metabolism, Cloning, Molecular, TATA-Box Binding Protein genetics, TATA-Box Binding Protein isolation & purification
- Abstract
The TATA binding protein (TBP) is the central core protein of the transcription factor II D that binds directly to the TATA box and therefore plays an integral part in eukaryotic transcription. This pivotal position of TBP is underlined by the vast number of interaction partners involved. Expression and purification of human TATA binding protein (hTBP) has remained a challenge due to protein instability and the protein loss during expression and purification involved. Here, we present a novel approach for high yield expression and purification of human TBP core (hTBPc) protein. Protein fold and activity are verified by nuclear magnetic resonance (NMR) spectroscopy and microscale thermophoresis (MST)., (Copyright © 2012 Elsevier Inc. All rights reserved.)
- Published
- 2012
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