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Biomolecular mirror‐image recognition: Reciprocal chiral‐specific DNA binding of synthetic enantiomers of zinc finger domain from GAGA factor
Author(s) -
Negi Shigeru,
Dhanasekaran Muthu,
Hirata Tsuyoshi,
Urata Hidehito,
Sugiura Yukio
Publication year - 2006
Publication title -
chirality
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.43
H-Index - 77
eISSN - 1520-636X
pISSN - 0899-0042
DOI - 10.1002/chir.20247
Subject(s) - chemistry , circular dichroism , enantiomer , peptide , dna , zinc finger , chirality (physics) , protein–dna interaction , mirror image , stereochemistry , crystallography , biophysics , dna binding protein , biochemistry , transcription factor , gene , physics , biology , optics , chiral symmetry breaking , nambu–jona lasinio model , quantum mechanics , quark
To experimentally demonstrate the mirror‐image recognition in protein and DNA interaction, we have designed a small DNA‐binding peptide based on the zinc‐finger domain of GAGA transcription factor. Circular dichroism data suggest that the conformations of peptide enantiomers as well as the DNA enantiomers have a mirror‐image relationship. The gel mobility shift assay showed that the synthetic enantiomers of the peptide showed reciprocal chiral‐specific interactions with the DNA; the natural L ‐peptide binds specifically with the natural D ‐DNA substrate, and the unnatural D ‐peptide binds specifically with the unnatural L ‐DNA substrate. The present data imply that the folding of the L ‐ and D ‐enantiomers of the peptide as well as the DNA substrates are exact mirror images of each other in 3‐D structure and biological activity, and generalize the chiral‐specific nature of biomolecular interaction. Chirality, 2006. © 2006 Wiley‐Liss, Inc.