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

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

PROVIDER: PRJNA934867 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR23455243_1.fastq.gz	Fastqsanger.gz
	SRR23455243_2.fastq.gz	Fastqsanger.gz
	SRR23455244_1.fastq.gz	Fastqsanger.gz
	SRR23455244_2.fastq.gz	Fastqsanger.gz
	SRR23455245_1.fastq.gz	Fastqsanger.gz

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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. 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 | 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 [MNase-Seq]

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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 [MNase-Seq]

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

| PRJNA934865 | 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

A single amino acid substitution in the capsid protein of Zika virus contributes to the African lineage-specific virulence phenotypes

Project description:The re-emerged Zika virus (ZIKV) can cause severe neurological complications termed congenital Zika syndrome (CZS) in infants born to ZIKV-infected mothers. However, increasing evidence shows the ancestral African lineage ZIKV displays more virulent phenotype than the contemporary Asian ZIKV in multiple cell and animal models. However, the viral determinants and underlying mechanism of this lineage specific virulence phenotype remain largely unknown. In the present study, phylogenetic analysis and sequence alignment identified a panel of lineage specific amino acid substitutions between African and Asian ZIKVs. Then, these amino acid substitutions were introduced into an infectious clone of Asian ZIKV by standard reverse genetic technology. Further characterization in vitro demonstrated that the recovered mutant virus with a lysine to arginine substitution at position 101 of capsid (C) protein (termed K101R) produced larger plaques in BHK-21 cells, and replicated more efficiently and induced more severe cytopathic effects (CPE) in multiple cells including human neuronal precursor cells (NPCs). More importantly, the K101R mutant virus replicated more efficiently in mouse brain tissues, and induced stronger inflammatory responses, leading to higher mortality than the wild type (WT) virus in neonatal mice. Despite no effect on RNA binding affinity of recombinant C protein to viral RNA, structural modeling and biochemical assays showed that the K101R substitution increased the viral protease cleavage efficiency of full C protein. Taken together, our study identified a single amino acid substitution K101R in the capsid protein responsible for the well-characterized virulence enhancement phenotypes, highlighting the importance of viral determinants for the co-circulating of two lineages of ZIKV.

2023-09-01 | GSE226495 | GEO

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

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