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. 1982;1(12):1559-64.
doi: 10.1002/j.1460-2075.1982.tb01355.x.

The head protein D of bacterial virus lambda is related to eukaryotic chromosomal proteins

H Witkiewicz, M Schweiger

The head protein D of bacterial virus lambda is related to eukaryotic chromosomal proteins

H Witkiewicz et al. EMBO J. 1982.

Abstract

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.

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