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

Maier, Wolf‐Martin; Nussbaum, Gregor; Domenjoud, Lionel; Klemm, Uwe; Engel, Wolfgang

doi:10.1093/nar/18.5.1249

Cited by 70 publications

(53 citation statements)

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“…2, amino acid sequences for the nine primate P2 pro-protamines predicted from the coding sequences of their cognate genes are compared. In view of the highly variable expression of the pro-P2 gene in mammals [8,251, the presence of a pro-P2 gene sequence in the non-human genomes does not imply that the genes are expressed. The mean length of pro-P2 is 101 residues with an increase of one residue to 102 in M-nemistrina and a decrease to 99 residues in red howler (A. seniculus).…”

Section: Resultsmentioning

confidence: 99%

“…The C-terminal coding sequence of bull P2 also contains several mutations that lead to a reduction of the number of basic residues through their replacement by neutral and hydrophobic residues that may decrease the binding of bull P2 to DNA [8].…”

Section: N I ___)mentioning

confidence: 99%

“…These genes possess mutations in 5' and 3' control regions that could depress both transcription and post-transcriptional polyadenylation [8]. In addition, in both bull and boar there is a mutation in the coding region leading to the loss of an amino acid sequence motif, R-L-H-R-I-H, which is present in mouse and human and which may be crucial for correct protamine P2…”

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Evolution of pro‐protamine P2 genes in primates

Retief

Dixon

1993

European Journal of Biochemistry

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Protamines P1 and P2 form a family of small basic peptides that represent the major sperm proteins in placental mammals. In human and mouse protamine P2 is one of the most abundant sperm proteins. The protamine P2 gene codes for a P2 precursor, pro-P2 which is later processed by proteolytic cleavages in its N-terminal region to form the mature P2 protamines. We have used polymerase chain amplification to directly sequence the pro-P2 genes of the five major primate families: red howler (Alouattu seniculus) is a New World monkey (Cebidae); the two macaque species, Macucu muluttu and M. nemistrinu are Old World monkeys (Cercopithecidae), the gibbon, Hylobutes lur, represents one branch of the apes (Hylobatidae); the orangutan, Pongo pygmueus, gorilla, Gorilla gorilla and two species of chimpanzee Pun paniscus and Pun troglodytes represent a second ape family (Pongidae). These pro-P2 genes are compared with that of human [Domenjoud, L., Nussbaum, G., Adham, I. M., Greeske, G. & Engel, W. (1990) Genomics 8, 127-1331.The overall size and organization of the genes are conserved within the group. The mean length of pro-P2 is 101 residues, with an increase to 102 in M. nemistrinu and a decrease to 99 residues in red howler (A. seniculus). In gorilla and red howler one of two 79-bp tandem repeats that occurs 3' of the gene is deleted. Of the 101 deduced amino acids examined, an amino acid change occurs in one or more primates at 45 positions. Considering only the most recently diverged group, the human/gorilla/chimpannzee clade, this represents a very high mutation rate of 0.99 changes/100 sites in lo6 years. This rapid mutation rate is characteristic of both members of the protamine gene family, P1 and P2. Consideration of the variable nature of the sequences at the multiple sites of proteolysis during the processing of the pro-P2 indicates either that there are several processing enzymes of differing specificities, or more likely that the folded structure of the pro-P2 limits accessibility of a non-specific protease to certain exposed sites.In the majority of placental mammals the major sperm basic protein is protamine 1, a small, highly arginine-rich protein of 50-52 residues (for review see [l]). However, in primates and a very limited number of rodents (typically, mouse), a second sperm protamine, P2, comprises a major portion of the total sperm protamine [2, 31. There are significant differences in the structures and synthesis of P1 and P2 in the mouse [4]. Protamine P2 is synthesized as a 106-amino-acid precursor, pro-P2, which is subsequently processed to the mature 63-residue P2 by removal of its N-terminal leader peptide of 43 residues via a series of intermediate proteins [ 5 ] . In contrast, protamine P1 is not processed. The major qualitative difference between P1 and P2 is the presence of 8 or 9 His residues in human P2 [2], compared to a single one in human P1. There are 12 or 13 His in mouse P2, but none in mouse P1 [3]. Human P2 exists in two major forms in mature sperm, HP2a and HP2b, differing by the pr...

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Section: Resultsmentioning

confidence: 99%

Section: N I ___)mentioning

confidence: 99%

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confidence: 99%

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Evolution of pro‐protamine P2 genes in primates

Retief

Dixon

1993

European Journal of Biochemistry

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“…However, patients possessing a high percentage of mature sperm with single-stranded DNA are still capable of fertilization, as Ab patients had a median fertilization rate of 25.0%. Previous studies have supported this finding (23,36)° Studies carried out on animals which possess the P2 gene but produce no or low levels of protamine 2 (12,13,38,39) have suggested that reduction in either P 1 or P2 may be explained by either reduced protamine transcription and translation or unstable products as a result of failed posttranscriptional modification. Lack of P2 in the boar has been shown to be due to mutations within the P2 gene (31).…”

Section: Discussionmentioning

confidence: 72%

“…PI is found throughout the animal kingdom, whereas P2 has been isolated only in humans and a few other mammals (mouse, hamster and stallion) studied to date (7)(8)(9)(10)(11)(12). The P2 gene has, however, been shown to exist in the genomes of bull and boar (13), despite their lacking the P2 protein. In human sperm of fertile men P1 and P2 are found at the ratio of approximately 1:1 (2).…”

Section: Introductionmentioning

confidence: 99%