Bacteria synthesize a set of small, usually basic proteins of about 90
residues that bind DNA and are known as histone-like proteins [1,2]. The exact
function of these proteins is not yet clear but they are capable of wrapping
DNA and stabilizing it from denaturation under extreme environmental
conditions. The sequence of a number of different types of these proteins is
The HU proteins, which, in Escherichia coli, are a dimer of closely related
α and β chains and, in other bacteria, can be dimer of identical
chains. HU-type proteins have been found in a variety of eubacteria,
cyanobacteria and archaebacteria, and are also encoded in the chloroplast
genome of some algae .
The integration host factor (IHF), a dimer of closely related chains which
seem to function in genetic recombination as well as in translational and
transcriptional control  in enterobacteria.
The bacteriophage sp01 transcription factor 1 (TF1) which selectively binds
to and inhibits the transcription of hydroxymethyluracil-containing DNA,
such as sp01 DNA, by RNA polymerase in vitro.
The African Swine fever virus protein A104R (or LMW5-AR) .
As a signature pattern for this family of proteins, we use a twenty residue
sequence which includes three perfectly conserved positions. According to the
tertiary structure of one of these proteins , this pattern spans exactly
the first half of the flexible DNA-binding arm.
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