title: Recombinant expression and purification of human TATA binding protein using a chimeric fusion.
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).
authors: Institute for Organic Chemistry and Chemical Biology, Center of Biomolecular Magnetic Resonance, Goethe University Frankfurt, Frankfurt am Main, Germany.
authors: Robert
authors: R
authors: Silvers
authors: Krishna
authors: K
authors: Saxena
authors: Denis
authors: D
authors: Kudlinzki
authors: Harald
authors: H
authors: Schwalbe
mesh_terms: D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017510:Protein Folding; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D035181:TATA-Box Binding Protein / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification* / Q000378:metabolism
chemical_list: D011993:Recombinant Fusion Proteins; D035181:TATA-Box Binding Protein