Nucleic Acids Research, Vol 26, Issue 18 4267-4273, Copyright © 1998 by Oxford University Press
N Nishiya, H Sabe, K Nose and M Shibanuma
hic-5 protein is a member of the LIM protein family, containing four LIM
domains in its C-terminal region. It is mainly localized in focal adhesions
and shows striking similarity to paxillin in its LIM domains, although the
function of these LIM domains has remained elusive. In the present study,
we found that full-length and the C-terminal half of hic- 5 protein,
including four LIM domains, bound to DNA in a zinc-dependent manner in
vitro . Mouse genomic fragments that specifically bound to the hic-5
protein were isolated by successive rounds of hic-5 protein- DNA complex
immunoprecipitation and PCR amplification. Seven independent clones were
isolated, which contained high amounts of G+A and/or a long A/T tract. A
DNA binding protein blot assay revealed the specificity of the interaction
between hic-5 protein and the DNA fragment. Using a series of truncated
forms of the hic-5 LIM domains, each of the four LIM domains was found to
contribute to DNA binding in a distinctive manner.
ARTICLES
The LIM domains of hic-5 protein recognize specific DNA fragments in a zinc-dependent manner in vitro
Department of Microbiology, Showa University School of Pharmaceutical Sciences, Hatanodai 1-5-8, Shinagawa-ku, Tokyo, Japan and Osaka Bioscience Institute, Suita, Osaka, Japan.
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