Yelick P C, Balhorn R, Johnson P A, Corzett M, Mazrimas J A, Kleene K C, Hecht N B
Mol Cell Biol. 1987 Jun;7(6):2173-9. doi: 10.1128/mcb.7.6.2173-2179.1987.
The nuclei of mouse spermatozoa contain two protamine variants, mouse protamine 1 (mP1) and mouse protamine 2 (mP2). The amino acid sequence predicted from mP1 cDNAs demonstrates that mP1 is a 50-amino-acid protein with strong homology to other mammalian P1 protamines. Nucleotide sequence analysis of independently isolated, overlapping cDNA clones indicated that mP2 is initially synthesized as a precursor protein which is subsequently processed into the spermatozoan form of mP2. The existence of the mP2 precursor was confirmed by amino acid composition and sequence analysis of the largest of a set of four basic proteins isolated from late-step spermatids whose synthesis is coincident with that of mP1. The sequence of the first 10 amino acids of this protein, mP2 precursor 1, exactly matches that predicted from the nucleotide sequence of cDNA and genomic mP2 clones. The amino acid composition of isolated mP2 precursor 1 very closely matches that predicted from the mP2 cDNA nucleotide sequence. Sequence analysis of the amino terminus of isolated mature mP2 identified the final processing point within the mP2 precursor. These studies demonstrated that mP2 is synthesized as a precursor containing 106 amino acids which is processed into the mature, 63-amino-acid form found in spermatozoa.
小鼠精子的细胞核包含两种鱼精蛋白变体,即小鼠鱼精蛋白1(mP1)和小鼠鱼精蛋白2(mP2)。从mP1 cDNA预测的氨基酸序列表明,mP1是一种由50个氨基酸组成的蛋白质,与其他哺乳动物的P1鱼精蛋白具有高度同源性。对独立分离的重叠cDNA克隆进行核苷酸序列分析表明,mP2最初作为前体蛋白合成,随后加工成精子中的mP2形式。从晚期精子细胞中分离出的一组四种碱性蛋白中最大的一种,其氨基酸组成和序列分析证实了mP2前体的存在,该蛋白的合成与mP1的合成同时发生。这种蛋白(mP2前体1)的前10个氨基酸序列与从cDNA和基因组mP2克隆的核苷酸序列预测的序列完全匹配。分离得到的mP2前体1的氨基酸组成与从mP2 cDNA核苷酸序列预测的组成非常接近。对分离出的成熟mP2的氨基末端进行序列分析,确定了mP2前体内的最终加工位点。这些研究表明,mP2最初作为一种含有106个氨基酸的前体合成,随后加工成精子中发现的成熟的、由63个氨基酸组成的形式。