Ad. Baxevanis et al., A VARIETY OF DNA-BINDING AND MULTIMERIC PROTEINS CONTAIN THE HISTONE FOLD MOTIF, Nucleic acids research, 23(14), 1995, pp. 2685-2691
The histone fold motif has previously been identified as a structural
feature common to all four core histones and is involved in both histo
ne-histone and histone-DNA interactions. Through the use of a novel mo
tif searching method, a group of proteins containing the histone fold
motif has been established, The proteins in this group are involved in
a wide variety of functions related mostly to DNA metabolism. Most of
these proteins engage in protein-protein or protein-DNA interactions,
as do their core histone counterparts. Among these, the CCAAT-specifi
c transcription factor CBF and its yeast homologue HAP are two example
s of multimeric complexes with different component subunits that conta
in the histone fold motif. The histone fold proteins are distantly rel
ated, with a relatively small degree of absolute sequence similarity.
It is proposed that these proteins may share a similar three-dimension
al conformation despite the lack of significant sequence similarity.