Abstract
The nuclei of sperm of the mussel Mytilus edulis contain three specific proteins: (1) a major protamine-like component (φ1); (2) a lysine-rich protein (φ3); and (3) a histone-like component (φ2b). The latter is characterized here for the first time. It is also shown that the φ3 protein does not contain modified lysines, but has some phosphorylated serines. Nuclease digestion of whole nuclei gives a continuous distribution of sizes for DNA, without any evidence of a nucleosome structure. X-ray diffraction indicates that DNA is organized as bundles of parallel molecules without any signs of either crystallinity or higher order structure.
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