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Sperm chromatin structure and reproductive fitness are altered by substitution of a single amino acid in mouse Protamine 1 [MNase-Seq]

ABSTRACT: Sperm chromatin structure and reproductive fitness are altered by substitution of a single amino acid in mouse Protamine 1 [MNase-Seq]

PROVIDER: PRJNA934865 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR23455092_1.fastq.gz	Fastqsanger.gz
	SRR23455092_2.fastq.gz	Fastqsanger.gz
	SRR23455093_1.fastq.gz	Fastqsanger.gz
	SRR23455093_2.fastq.gz	Fastqsanger.gz
	SRR23455094_1.fastq.gz	Fastqsanger.gz

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Similar Datasets

Sperm chromatin structure and reproductive fitness are altered by substitution of a single amino acid in mouse Protamine 1 [MNase-Seq]

Project description:Conventional dogma presumes that protamine-mediated DNA compaction in sperm is achieved by electrostatic interactions between DNA and the arginine-rich core of protamines. However, phylogenetic analysis reveals several non-arginine residues conserved within, but not across species. The significance of these residues or post-translational modifications are poorly understood. Here, we investigated the functional role of K49, a rodent-specific lysine residue in mouse protamine 1 (P1) that is acetylated early in spermiogenesis and retained in sperm. In vivo, alanine substitution (P1 K49A) results in loss of programmatic histone retention, decreased sperm motility, decreased male fertility, and in zygotes, premature P1 removal from paternal chromatin, altered DNA replication, and embryonic arrest. In vitro, P1 K49A decreases protamine-DNA binding and alters DNA compaction/decompaction kinetics. Hence, a single amino acid substitution outside the P1 arginine core is sufficient to profoundly alter protein function and developmental outcomes, suggesting that protamine non-arginine residues are essential for reproductive fitness.

2023-05-09 | GSE225268 | GEO

Sperm chromatin structure and reproductive fitness are altered by substitution of a single amino acid in mouse Protamine 1

2023-05-09 | GSE225271 | GEO

Sperm chromatin structure and reproductive fitness are altered by substitution of a single amino acid in mouse Protamine 1 [scRNA-Seq]

2023-05-09 | GSE225270 | GEO

Sperm chromatin structure and reproductive fitness are altered by substitution of a single amino acid in mouse Protamine 1

Project description:Sperm chromatin structure and reproductive fitness are altered by substitution of a single amino acid in mouse Protamine 1

| PRJNA934862 | ENA

Sperm chromatin structure and reproductive fitness are altered by substitution of a single amino acid in mouse Protamine 1 [scRNA-Seq]

Project description:Sperm chromatin structure and reproductive fitness are altered by substitution of a single amino acid in mouse Protamine 1 [scRNA-Seq]

| PRJNA934867 | ENA

Sperm chromatin structure and reproductive fitness are altered by substitution of a single amino acid in mouse protamine 1.

Project description:Conventional dogma presumes that protamine-mediated DNA compaction in sperm is achieved by electrostatic interactions between DNA and the arginine-rich core of protamines. Phylogenetic analysis reveals several non-arginine residues conserved within, but not across species. The significance of these residues and their post-translational modifications are poorly understood. Here, we investigated the role of K49, a rodent-specific lysine residue in protamine 1 (P1) that is acetylated early in spermiogenesis and retained in sperm. In sperm, alanine substitution (P1(K49A)) decreases sperm motility and male fertility-defects that are not rescued by arginine substitution (P1(K49R)). In zygotes, P1(K49A) leads to premature male pronuclear decompaction, altered DNA replication, and embryonic arrest. In vitro, P1(K49A) decreases protamine-DNA binding and alters DNA compaction and decompaction kinetics. Hence, a single amino acid substitution outside the P1 arginine core is sufficient to profoundly alter protein function and developmental outcomes, suggesting that protamine non-arginine residues are essential for reproductive fitness.

| S-EPMC10833441 | biostudies-literature

SPERM CHROMATIN STRUCTURE AND REPRODUCTIVE FITNESS ARE ALTERED BY SUBSTITUTION OF A SINGLE AMINO ACID IN MOUSE PROTAMINE 1

Project description:Quantification of histone PTMs from mouse sperm chromatin.

2023-05-11 | MSV000091920 | MassIVE

Mouse sperm protamine mass spectrometry

Project description:Conventional dogma presumes that protamine-mediated DNA compaction in sperm is achieved by passive electrostatics between DNA and the arginine-rich core of protamines. However, phylogenetic analysis reveals several non-arginine residues that are conserved within, but not across, species. The functional significance of these residues or post-translational modifications are poorly understood. In this experiment, we investigated the presence of post-translational modifications on mouse protamine 1 to begin to dissect their function in vivo.

2023-05-17 | PXD028917 | Pride

Alterations in the abundance of protamine proteoforms related to sperm chromatin packaging, obesity, and age in men with unexplained infertility

Project description:Protamine1 (P1) and Protamine 2 family (P2) are the most relevant nuclear proteins in the male gamete since are necessary to compact and protect the paternal genome. Human and mouse sperm contain a complex population of protamine proteoforms, which raises the interest to decipher whether it responds to a need of protein redundancy to ensure proper chromatin compaction, or whether specific protamine proteoforms have functional implications. In this study, we apply an optimized strategy based on Top-Down Mass Spectrometry to quantify alterations in the protamine proteoform profile of normozoospermic men with unexplained infertility and either molecular (high P1/P2) or lifestyle (obesity and advanced age) alterations. Accumulation of P2 immature forms was associated to higher P1/P2 ratios, suggesting an impaired processing of P2 in these patients. Men with obesity and intracellular oxidative stress revealed alterations in P1 proteoforms with mass shift(s) of +61 Da, either phosphorylated or not, and advanced age men showed a specific loss of diphosphorylated P1. These results point to alterations on protamine modifying mechanisms, such as proteolysis and phosphorylation, rather than on protamine synthesis, as critical factors for proper sperm chromatin maturity with impact on male fertility

2025-04-25 | PXD049367 | Pride

Characterization of human sperm protamine proteoforms through a combination of top-down and bottom-up mass spectrometry approaches

Project description:Protamine 1 (P1) and protamine 2 family (P2) are the most abundant nuclear basic spermspecific proteins, packing 85-95% of the paternal DNA. P1 is synthesized as a mature form, whereas P2 components (HP2, HP3 and HP4) arise from the proteolysis of the precursor (pre-P2). Due to the particular protamine physical-chemical properties, their identification by standardized bottom-up mass spectrometry (MS) strategies are not straightforward. Therefore, the aim of this study was to identify the sperm protamine proteoforms profile including P1 and P2 members and their post-translational modifications in normozoospermic individuals using two complementary strategies, a top-down MS approach and a proteinase K-digestion based bottom-up MS approach. By top-down MS approach, both described and new truncated P1 and pre-P2 proteoforms were identified. Likewise, intact P1, pre-P2, and P2 mature forms and their phosphorylation pattern were detected, as well as a +61 Da modification in different proteoforms. Additionally, the bottom-up MS approach revealed phosphorylated residues for pre-P2 and the new P2 isoform 2, which is not annotated at UniProtKB database. Implementing these strategies in comparative studies of different infertile phenotypes would permit to determine alterations in the protamine proteoforms pattern and elucidate the role of phosphorylation/dephosphorylation dynamics in male fertility.

2019-11-11 | PXD014618 | Pride

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