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Repeated sequence elements in the high molecular weight basic nuclear proteins from the winter flounder.

D C Young¹, P L Davies

¹Department of Biochemistry, Queen's University, Kingston, Ont., Canada.

Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire

|October 1, 1987

Summary

Winter flounder sperm utilize unique high molecular weight proteins instead of protamines. These proteins contain tandemly repeated sequences, distinct from known proteins, suggesting a novel role in sperm development.

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Area of Science:

Molecular and Cellular Biology
Reproductive Biology
Biochemistry

Background:

Sperm maturation typically involves replacing histones with protamines for DNA condensation.
Winter flounder (Pseudopleuronectes americanus) exhibit an atypical sperm maturation process.

Purpose of the Study:

To characterize the high molecular weight basic nuclear proteins found in winter flounder sperm.
To elucidate the structure and potential function of these unique sperm proteins.

Main Methods:

Limited endoprotease Lys-C digestion to generate peptides.
High-pressure liquid chromatography (HPLC) for peptide purification.
Sequential Edman degradation for amino acid sequencing.

Main Results:

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Digestion yielded peptides, with nine purified and sequenced.
Two distinct homology groups were identified: a repeated dodecapeptide (35% of proteins) and a heptapeptide (11% of proteins).
The dodecapeptide contains a known phosphorylation site; both sequences are unique and not found in databases, with distant similarity to protamines and viral DNA-binding proteins.

Conclusions:

Winter flounder sperm utilize unique, highly abundant basic nuclear proteins, not protamines.
These proteins feature tandemly repeated sequences, including a conserved phosphorylation site.
The unique nature of these sequences suggests a specialized role in winter flounder spermiogenesis.