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J. Biol. Chem., Vol. 263, Issue 21, 10141-10150, Jul, 1988

An unusual cysteine-containing histone H1-like protein and two protamine-like proteins are the major nuclear proteins of the sperm of the bivalve mollusc Macoma nasuta

J Ausio
Department of Biochemistry and Biophysics, Oregon State University, Corvallis 97331.

The sperm-specific protamine-like (PL) components PL-I, PL-II, and PL- III from the sperm of the bent-nose clam Macoma nasuta have been isolated and characterized for the first time. These proteins coexist in the sperm nuclei with a small percentage of a full histone complement. All of them have a very similar amino acid composition, following what seems to be the general composition prototype for the class Bivalvia (Ausio, J. (1986) Comp. Biochem. Physiol. B Comp. Biochem. 85, 439-449). Nevertheless, they have different molecular weights (PL-I = 23,500, PL-II = 15,600, and PL-III = 7,900) as measured by sedimentation equilibrium in the analytical ultracentrifuge. Furthermore, the PL-I component shares common features with the proteins of the histone H1 family. Yet, it is very unusual, for it contains 2 cysteine residues that are located in the trypsin-resistant core of this protein. The protamine-like fraction PL-III exhibits intraspecific microheterogeneity which is reflected by the presence of two protein variants which most probably are the result of an allelic polymorphism.
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