The lack of protamine 2 (P2) in boar and bull spermatozoa is due to mutations within the P2 gene

The nuclei of spermatozoa in all mammals examined so far contain P1 protamine. A second protamine variant, protamine P2, has to date been isolated only from human and murine spermatozoa where it represents the major fraction of basic nuclear protein. In order to elucidate the reason for this unusual...

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Bibliographic Details
Published in:Nucleic acids research 1990-03, Vol.18 (5), p.1249-1254
Main Authors: MAIER, W.-M, NUSSBAUM, G, DOMENJOUD, L, KLEMM, U, ENGEL, W
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Animals
Base Sequence
Biological and medical sciences
Blotting, Northern
Cattle - genetics
DNA - genetics
DNA - isolation & purification
Fundamental and applied biological sciences. Psychology
Gene Expression
Genes
Holoproteins
Humans
Male
Molecular Sequence Data
Mutation
Nuclear proteins
Nucleic Acid Hybridization
Protamines - analysis
Protamines - genetics
Protein Biosynthesis
Proteins
Sequence Homology, Nucleic Acid
Spermatozoa - analysis
Spermatozoa - metabolism
Swine - genetics
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Summary:The nuclei of spermatozoa in all mammals examined so far contain P1 protamine. A second protamine variant, protamine P2, has to date been isolated only from human and murine spermatozoa where it represents the major fraction of basic nuclear protein. In order to elucidate the reason for this unusual distribution of the protamine variants among mammals we have investigated the expression of protamine P2 in boar and bull. It can be shown that also in these species protamine 2 is transcribed and translated on low levels. Various mutational events though have altered the primary structure of the protein: In boar, a deletion of 8 aminoacids has removed a sequence motif from the amino-terminus of the molecule, which highly probable is of functional relevance. The bovine sequence, as a consequence of numerous point mutations has accumulated neutral and hydrophobic aminoacids which reduce the affinity of the protamine 2 to DNA.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/18.5.1249