DNA Affinity Chromatography

2006 ◽  
Vol 2006 (1) ◽  
pp. pdb.prot4206
Author(s):  
Keith Brocklehurst ◽  
Albert J. Courey ◽  
Sheraz Gul ◽  
Sue-Hwa Lin ◽  
Robert L. Moritz
1994 ◽  
Vol 14 (10) ◽  
pp. 6635-6646
Author(s):  
J A Diehl ◽  
M Hannink

Protein-protein interactions between the CCAAT box enhancer-binding proteins (C/EBP) and the Rel family of transcription factors have been implicated in the regulation of cytokine gene expression. We have used sequence-specific DNA affinity chromatography to purify a complex from avian T cells that binds to a consensus C/EBP motif. Our results provide evidence that Rel-related proteins are components of the C/EBP-DNA complex as a result of protein-protein interactions with the C/EBP proteins. A polyclonal antiserum raised against the Rel homology domain of v-Rel and antisera raised against two human RelA-derived peptides specifically induced a supershift of the C/EBP-DNA complex in mobility shift assays using the affinity-purified C/EBP. In addition, several kappa B-binding proteins copurified with the avian C/EBP complex through two rounds of sequence-specific DNA affinity chromatography. The kappa B-binding proteins are distinct from the C/EBP proteins that directly contact DNA containing the C/EBP binding site. The identification of a protein complex that binds specifically to a consensus C/EBP site and contains both C/EBP and Rel family members suggests a novel mechanism for regulation of gene expression by Rel family proteins.


Author(s):  
Shilpa Oak ◽  
Himanshu Gadgil ◽  
Harry Jarrett ◽  
Robert Moxley

2003 ◽  
pp. 141-153
Author(s):  
Priya Sethu Chockalingam ◽  
Luis A. Jurado ◽  
F. Darlene Robinson ◽  
Harry W. Jarrett

2001 ◽  
Vol 290 (2) ◽  
pp. 147-178 ◽  
Author(s):  
Himanshu Gadgil ◽  
Luis A. Jurado ◽  
Harry W. Jarrett

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