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Title of Journal: J Biol Inorg Chem

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Abbravation: JBIC Journal of Biological Inorganic Chemistry

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Springer-Verlag

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DOI

10.1016/0370-2693(74)90768-0

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1432-1327

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DNA targeting and cleavage by an engineered metall

Authors: Siu Wah WongDeyrup Charulata Prasannan Cynthia M Dupureur Sonya J Franklin
Publish Date: 2011/11/25
Volume: 17, Issue: 3, Pages: 387-398
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Abstract

Nature has illustrated through numerous examples that protein dimerization has structural and functional advantages We previously reported the design and characterization of an engineered “metallohomeodomain” protein C2 based on a chimera of the EFhand Cabinding motif and the helix–turn–helix motif of homeodomains Lim and Franklin in Protein Sci 152159–2165 2004 This small metalloprotein binds the hard metal ions CaII and LnIII and interacts with DNA with modest sequence preference and affinity yet exhibits only residual DNA cleavage activity Here we have achieved substantial improvement in function by constructing a covalent dimer of this C2 module F2 to create a larger multidomain protein As assayed via fluorescence spectroscopy this F2 protein binds CaII more avidly 25fold than C2 on a perdomain basis in gel shift selection experiments metallated F2 exhibits a specificity toward 5′TAATTA3′ sequences Finally Ca2F2 cleaves plasmid DNA and generates a linear product in a CaIIdependent way unlike the CaC2 monomer To the best of our knowledge this activation of CaII in the context of an EFhand binding motif is unique and represents a significant step forward in the design of artificial metallonucleases by utilizing biologically significant metal ions

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