Tetrameric ZBRK1 DNA binding domain has affinity towards cognate DNA in absence of zinc ions.

Lumbini R Yadav, Mahamaya N Biswal, Vikrant, M V Hosur, Ashok K Varma

Biochemical and biophysical research communications 2014 Jul 18

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Zinc finger transcription regulatory proteins play crucial roles in cell-cycle regulation, DNA damage response and tumor genesis. Human ZBRK1 is a zinc-finger transcription repressor protein, which recognizes double helical DNA containing consensus sequences of 5'GGGXXXCAGXXXTTT3'. In the present study, we have purified recombinant DNA binding domain of ZBRK1, and studied binding with zinc ions and DNA, using biophysical techniques. The elution profile of the purified protein suggests that this ZBRK1 forms a homotetramer in solution. Dissociation and pull down assays also suggest that this domain forms a higher order oligomer. The ZBRK1-DNA binding domain acquires higher stability in the presence of zinc ions and DNA. The secondary structure of the ZBRK1-DNA complex is found to be significantly altered from the standard B-DNA conformation. Copyright © 2014 Elsevier Inc. All rights reserved.

Citation

Lumbini R Yadav, Mahamaya N Biswal, Vikrant, M V Hosur, Ashok K Varma. Tetrameric ZBRK1 DNA binding domain has affinity towards cognate DNA in absence of zinc ions. Biochemical and biophysical research communications. 2014 Jul 18;450(1):283-8