ArticleNucleic acids research2015
Multimerization of Drosophila sperm protein Mst77F causes a unique condensed chromatin structure.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Rapid protamine evolution suppresses meiotic drive inScience advances · 2026Article
- The jewel wasp Nasonia vitripennis utilizes two single-copy, protamine-like sperm nuclear basic proteins.G3 (Bethesda, Md.) · 2026Article
- Derepression of Y-linked multicopy protamine-like genes interferes with sperm nuclear compaction inProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Genome-wide occupancy reveals the localization of H1T2 (H1fnt) to repeat regions and a subset of transcriptionally active chromatin domains in rat spermatids.Epigenetics & chromatin · 2021Article
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- Nejire/dCBP-mediated histone H3 acetylation during spermatogenesis is essential for male fertility in Drosophila melanogaster.PloS one · 2018Article
- Unlocking sperm chromatin at fertilization requires a dedicated egg thioredoxin in Drosophila.Nature communications · 2016Article
- The Drosophila chromosomal protein Mst77F is processed to generate an essential component of mature sperm chromatin.Open biology · 2016Article
- The intimate genetics of Drosophila fertilization.Open biology · 2015Review
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Authors and funding
9 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Despite insights on the cellular level, the molecular details of chromatin reorganization in sperm development, which involves replacement of histone proteins by specialized factors to allow ultra most condensation of the genome, are not well understood. Protamines are dispensable for DNA condensation during Drosophila post-meiotic spermatogenesis. Therefore, we analyzed the interaction of Mst77F, another very basic testis-specific protein with chromatin and DNA as well as studied the molecular consequences of such binding. We show that Mst77F on its own causes severe chromatin and DNA aggregation. An intrinsically unstructured domain in the C-terminus of Mst77F binds DNA via electrostatic interaction. This binding results in structural reorganization of the domain, which induces interaction with an N-terminal region of the protein. Via putative cooperative effects Mst77F is induced to multimerize in this state causing DNA aggregation. In agreement, overexpression of Mst77F results in chromatin aggregation in fly sperm. Based on these findings we postulate that Mst77F is crucial for sperm development by giving rise to a unique condensed chromatin structure.
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