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Synthesis of a new zinc finger peptide; comparison of its `code' deduced and `CASTing' derived binding sites
Author(s) -
Corbi Nicoletta,
Perez Marie,
Maione Rossella,
Passananti Claudio
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01257-x
Subject(s) - zinc finger , zinc finger nuclease , dna , oligonucleotide , protein–dna interaction , binding site , ring finger domain , gene , genetic code , nucleotide , peptide , chemistry , biochemistry , computational biology , biology , stereochemistry , dna binding protein , transcription factor
Using two synthetic oligonucleotides, we have constructed a new gene containing three zinc finger motifs of the Cys 2 ‐His 2 type. We named this artificial gene `Mago'. The Mago nucleotide triplets encoding the amino acid positions, described to be crucial for DNA binding specificity, have been chosen on the basis of the proposed recognition `code' that relates the zinc finger's primary structure to the DNA binding target. Here we demonstrate that Mago protein specifically binds the `code' DNA target, with a dissociation constant ( K d ) comparable to the K d of the well known Zif268 protein with its binding site. Moreover, we show that the deduced Mago `code' and the `experimental' selected DNA binding sites are almost identical, differing only in two nucleotides at the side positions.