The head protein D of bacterial virus lambda is related to eukaryotic chromosomal proteins.
Bacteriophage lambda structural head protein D has physiochemical properties in common with eukaryotic chromosomal proteins. It has a low affinity for hydroxylapatite, it is heat stable and acid soluble. Moreover, it cross-reacts immunologically with histones H2A and H2B. The deduced primary structure of the D protein shows striking homology to calf chromosomal high mobility group HMG-14 protein. There are two clusters of four ( LSAK , ASDE ) and one of three (APA) identical amino acid residues. Additionally the cluster ETK of protein D occurs three times in HMG-14 and 14 single identical residues are present. A mechanism for an alternative to a nucleosomal mode of nuclear DNA condensation and a possible function of HMG proteins are discussed.
D000595:Amino Acid Sequence; D000818:Animals; D000936:Antigen-Antibody Complex; D010582:Bacteriophage lambda / Q000235:genetics*; D036022:Capsid Proteins; D002417:Cattle; D002875:Chromosomes / Q000502:physiology; D002876:Chromosomes, Bacterial / Q000502:physiology; D003429:Cross Reactions; D004926:Escherichia coli / Q000235:genetics; D006657:Histones / Q000235:genetics*; D008970:Molecular Weight; D051381:Rats; D013045:Species Specificity; D013329:Structure-Activity Relationship; D013950:Thymus Gland; D014764:Viral Proteins / Q000235:genetics*
D000936:Antigen-Antibody Complex; D036022:Capsid Proteins; C041745:D protein, Enterobacteria phage lambda; D006657:Histones; D014764:Viral Proteins