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
known:
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 [3].
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 [4] 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) [5].
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 [6], this pattern spans exactly
the first half of the flexible DNA-binding arm.
Neilan J.G. Lu Z. Kutish G.F. Sussman M.D. Roberts P.C. Yozawa T. Rock D.L.
Title
An African swine fever virus gene with similarity to bacterial DNA binding proteins, bacterial integration host factors, and the Bacillus phage SPO1 transcription factor, TF1.
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