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Kaiso uses all three zinc fingers and adjacent sequence motifs for high affinity binding to sequence‐specific and methyl‐CpG DNA targets
Author(s) -
Buck-Koehntop Bethany A.,
Martinez-Yamout Maria A.,
Jane Dyson H.,
Wright Peter E.
Publication year - 2012
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/j.febslet.2012.01.045
Subject(s) - zinc finger , dna , cpg site , sequence (biology) , sequence motif , dna binding protein , dna sequencing , dna methylation , computational biology , chemistry , biology , microbiology and biotechnology , genetics , gene , transcription factor , gene expression
Kaiso is a Cys 2 His 2 zinc finger (ZF) protein that mediates methyl‐CpG‐dependent and sequence‐specific transcriptional repression. As a first step towards elucidating the structural and molecular basis for recognition of these disparate DNA sequences, the minimal binding region of Kaiso was identified and optimal DNA sequences for high‐affinity interactions were characterized. Contrary to previous findings, Kaiso requires all three zinc fingers plus adjacent protein regions for DNA recognition. An N‐terminal extension contributes to structural stability, while an extended C‐terminal region augments DNA binding. Complexes formed between the optimized Kaiso construct and both DNA sequences are suitable for future structural evaluation.