Identification of phosphoseryl residues in protamines from mature mammalian spermatozoa.
Abstract: Protamines isolated from ejaculated human, stallion, bull, boar, and ram spermatozoa were subjected to phosphoserine conversion reaction and protein sequencing. Phosphoserines were detected as S-ethylcysteines. Endogenously phosphorylated protamines have previously been found only in ejaculated human sperm. In this study, we demonstrate that ejaculated sperm from other species also contain protamines phosphorylated at serine residues. In P1-protamines, the endogenously phosphorylated serines were located at the N-terminal region in all species studied, whereas in major forms of human and stallion P2-protamines, the serine residues located in the middle region of the molecule were predominantly phosphorylated. These results support the current DNA binding model in the case of the P1-protamines. The internal location of the phosphorylated serines in the P2-protamines indicates, however, that the binding of these proteins to DNA or their interaction with other protamine molecules may differ from that of P1-protamines. This also suggests that, during sperm maturation, P2-protamines may have a role different from that of P1-protamines.
Publication Date: 1994-05-01 PubMed ID: 8025177DOI: 10.1095/biolreprod50.5.981Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The study recognizes that protamines, originating from the sperm of various species, undergo phosphorylation in serine residues. This discovery, previously only seen in human sperm, shows that the process might function differently in P2-protamines than in P1-protamines.
Experiment and Findings
- Protamines are found in the sperm of various species – humans, boars, rams, bulls, and stallions. All these protamines were subjected to a process known as phosphoserine conversion reaction followed by protein sequencing.
- Phosphoserines were identified as S-ethylcysteines. Phosphorylation is a process by which a phosphate group is added to a protein, often changing the function of the protein. In this case, serine residues in the protamines from various species’ sperm were found to be phosphorylated.
- This process was previously only detected in human sperm, but the study found similar occurrences in the sperm of other species.
P1-Protamines and P2-Protamines
- In P1-protamines, phosphorylated serines were found at the N-terminal region, the start of the protein chain. This was the case for all the species included in the study. This supports the existing model of DNA binding in P1-protamines.
- In P2-protamines, predominantly found in humans and stallions, the phosphorylated serines were often located in the middle region of the protein. The internal location of phosphorylated serines suggests a difference in the way these proteins bind to DNA or interact with other protamine molecules. This is distinct from the DNA binding and molecular interaction mode of P1-protamines.
- The position of the phosphorylated serines in P2-protamines suggests that they may serve a different function during the maturation of sperm than P1-protamines. More detailed research would be required to elucidate this possible difference in functions.
Cite This Article
APA
Pirhonen A, Linnala-Kankkunen A, Mäenpää PH.
(1994).
Identification of phosphoseryl residues in protamines from mature mammalian spermatozoa.
Biol Reprod, 50(5), 981-986.
https://doi.org/10.1095/biolreprod50.5.981 Publication
Researcher Affiliations
- Department of Biochemistry & Biotechnology, University of Kuopio, Finland.
MeSH Terms
- Amino Acid Sequence
- Animals
- Cattle
- Chromatography, High Pressure Liquid
- Horses
- Humans
- Male
- Molecular Sequence Data
- Phosphorylation
- Phosphoserine / analysis
- Protamines / analysis
- Protamines / chemistry
- Protamines / metabolism
- Sheep
- Spermatozoa / chemistry
- Swine
Citations
This article has been cited 8 times.- Soria-Meneses PJ, Jurado-Campos A, Gómez-Rubio V, Sánchez-Ajofrín I, Soler AJ, Garde JJ, Fernández-Santos MDR. Determination of Ram (Ovis aries) Sperm DNA Damage Due to Oxidative Stress: 8-OHdG Immunodetection Assay vs. SCSA(®). Animals (Basel) 2022 Nov 25;12(23).
- Arauz-Garofalo G, Jodar M, Vilanova M, de la Iglesia Rodriguez A, Castillo J, Soler-Ventura A, Oliva R, Vilaseca M, Gay M. Protamine Characterization by Top-Down Proteomics: Boosting Proteoform Identification with DBSCAN. Proteomes 2021 Apr 30;9(2).
- Lai Q, Wu W, Li A, Wang W, Yuan M, Yang K. The 38K-Mediated Specific Dephosphorylation of the Viral Core Protein P6.9 Plays an Important Role in the Nucleocapsid Assembly of Autographa californica Multiple Nucleopolyhedrovirus. J Virol 2018 May 1;92(9).
- Lüke L, Tourmente M, Dopazo H, Serra F, Roldan ER. Selective constraints on protamine 2 in primates and rodents. BMC Evol Biol 2016 Jan 22;16:21.
- Li A, Zhao H, Lai Q, Huang Z, Yuan M, Yang K. Posttranslational Modifications of Baculovirus Protamine-Like Protein P6.9 and the Significance of Its Hyperphosphorylation for Viral Very Late Gene Hyperexpression. J Virol 2015 Aug;89(15):7646-59.
- Castillo J, Estanyol JM, Ballescá JL, Oliva R. Human sperm chromatin epigenetic potential: genomics, proteomics, and male infertility. Asian J Androl 2015 Jul-Aug;17(4):601-9.
- Kanippayoor RL, Alpern JH, Moehring AJ. Protamines and spermatogenesis in Drosophila and Homo sapiens : A comparative analysis. Spermatogenesis 2013 Apr 1;3(2):e24376.
- Lüke L, Vicens A, Serra F, Luque-Larena JJ, Dopazo H, Roldan ER, Gomendio M. Sexual selection halts the relaxation of protamine 2 among rodents. PLoS One 2011;6(12):e29247.
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