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The head protein D of bacterial virus lambda is related to eukaryotic chromosomal proteins.
Author(s) -
Witkiewicz H.,
Schweiger M.
Publication year - 1982
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1982.tb01355.x
Subject(s) - biology , dna , lambda , dna replication , bacteriophage , histone , microbiology and biotechnology , genetics , gene , physics , escherichia coli , optics
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.