Histones H3 and H2a are homologous to the lambda repressor and cro proteins in 22 residue segments implicated in DNA binding.
The histones H3 and H2a from calf thymus are homologous to the repressor and cro repressor proteins of bacteriophage lambda in a 22-residue segment that has been implicated by mutational and model-building studies in DNA binding. In the lambda proteins this segment is folded into a helix-turn-helix unit of supersecondary structure, and we propose that the homologous regions in the histones possess the same fold. Homology was quantified with a unified procedure based on criteria of identity of key residues, primary structural homology and similarity of secondary structural potential. It has previously been shown that a set of other prokaryotic DNA-binding proteins have primary structural homology with the two lambda proteins. Homologies detected between the histones H4 and H2b and members of this set suggest that these histones also contain the putative DNA-binding fold.
D000595:Amino Acid Sequence; D010582:Bacteriophage lambda / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D006657:Histones / Q000378:metabolism*; D011487:Protein Conformation; D012097:Repressor Proteins / Q000378:metabolism*; D014157:Transcription Factors / Q000378:metabolism*; D014764:Viral Proteins; D054334:Viral Regulatory and Accessory Proteins
D004268:DNA-Binding Proteins; D006657:Histones; D012097:Repressor Proteins; D014157:Transcription Factors; D014764:Viral Proteins; D054334:Viral Regulatory and Accessory Proteins; C016649:phage repressor proteins