The amino acid sequence of human sperm protamine P1

McKay, Donald J.; Renaux, Bernard; Dixon, Gordon H.

doi:10.1007/bf01116555

Cited by 108 publications

(42 citation statements)

References 13 publications

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“…Also the amino acid compositions (table 1) were virtually identical and typical for protamines, i.e. very rich in arginine and half-cystine, but devoid of alanine, which otherwise is part of the characteristic N-terminus of mammalian type 1 protamines [5,[7][8][9][10][11][12][13][14]. The composition is similar to those published earlier [ 17,18].…”

Section: Resultssupporting

confidence: 72%

“…The alignment demonstrates that strongly basic arginine clusters, which presumably bind to the acidic DNA, tyrosines, which may act as DNA intercalators, and most half-cystines, which disulfide-crosslink sperm chromatin, all are evolutionarily conserved. The presence of valine instead of alanine at the Nterminus is a surprise, as the constancy of Nterminal alanine in all previously sequenced mammalian type 1 protamines [5,[7][8][9][10][11][12][13][14] seemed to indicate its functional importance. In fact, many non-mammalian arginine-rich protamines also possess an N-terminal alanine, the N-terminal sequences being reminiscent of the mammalian counterparts, i.e.…”

Section: Discussionmentioning

confidence: 99%

“…Most mammalian species seem to contain a single type of protamine in their sperm cells, but in man [5][6][7][8] and mouse [9] two main types of protamines (types 1 and 2) have been found. These two types show no convincing structural homology.…”

Section: Introductionmentioning

confidence: 99%

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Primary structure of rabbit sperm protamine, the first protamine of its type with an aberrant N‐terminal

Ammer

Henschen

1988

FEBS Letters

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Rabbit protamine was extracted from S-(pyridylethylated) sperm cell nuclei with hydrochloric acid and then isolated by reversed-phase HPLC. The primary structure was determined by amino acid sequence analysis of the total protein and of fragments obtained by digestion with endoproteinase Lys-C and thermolysin. The protamine contains 49 amino acid residues and is clearly homologous with mammalian type I protamines, 47% of the positions being invariant. Surprisingly, rabbit protamine possesses an N-terminal valine residue, whereas all mammalian and several non-mammalian protamine sequences of this type start with alanine, the N-terminal region being remarkably conserved during evolution.

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Section: Resultssupporting

confidence: 72%

Section: Discussionmentioning

confidence: 99%

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Primary structure of rabbit sperm protamine, the first protamine of its type with an aberrant N‐terminal

Ammer

Henschen

1988

FEBS Letters

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“…79:177a, 1978), rats (20,21), bulls (10,32,36), boars (36,43), rams (29,36,41), stallions (36), guinea pigs (8,9), rabbits (8,9), and humans (2,12,25,33,39). Complete sequence analysis of the P1 protamines from bulls (10,32), boars (43), rams (41), and humans (2,33) and the predicted amino acid sequence derived from a cDNA sequence for mouse protamine 1, (mPl) (24) have revealed identical lengths of 50 amino acids and strong sequence homologies among these mammalian protamines. P1 protamine is organized into three domains consisting of a central basic core with clusters of arginine and two less basic amino-and carboxyl-terminal regions.…”

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confidence: 99%

Mouse protamine 2 is synthesized as a precursor whereas mouse protamine 1 is not.

Yelick¹,

Balhorn²,

Johnson³

et al. 1987

Mol. Cell. Biol.

147

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The nuclei of mouse spermatozoa contain two protamine variants, mouse protamine 1 (mPl) and mouse protamine 2 (mP2). The amino acid sequence predicted from mPl cDNAs demonstrates that mPl 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 mPl. 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.Protamines are small, basic, arginine-rich proteins that replace histones in the later stages of spermatogenesis in many vertebrates (N. B. Hecht, in G. Stein and J. Stein, ed., Basic Chromosomal Proteins: Structure, Organization and Regulation ofthe Gene, in press). During spermatogenesis in mammals, the histones are not directly replaced by protamines but by a population of basic proteins that are transiently associated with the spermatid nucleus (14,35; Hecht, in press). These testis-specific proteins are removed from the condensing chromatin at later stages of spermiogenesis and are replaced by protamines, the predominant class of proteins found complexed with DNA in the mature spermatozoon. Mammalian protamines contain the amino acid cysteine, which is believed to function in the stabilization and compaction of the sperm nucleus through disulfide bond cross-linking (7).Protamines have been isolated from a large number of vertebrates including fish (3, 28), domestic fowl (38), mice (6, 27, 40; A. R.

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“…Bull sperm nuclei are, therefore, probably very stable. Human sperm nuclei, on the other hand, contain protamine II and protamine I [6,8,9,10]. Since protamine II contains less cysteine, human sperm nuclei can be expected to have a lower concentration of disulfide bridges and thus be less stable than bull sperm nuclei.…”

Section: Resultsmentioning

confidence: 99%