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  • 1
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    A cascade of histone modifications induces chromatin condensation in mitosis (2014)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2014-01-05
    Description: Metaphase chromosomes are visible hallmarks of mitosis, yet our understanding of their structure and of the forces shaping them is rudimentary. Phosphorylation of histone H3 serine 10 (H3 S10) by Aurora B kinase is a signature event of mitosis, but its function in chromatin condensation is unclear. Using genetically encoded ultraviolet light-inducible cross-linkers, we monitored protein-protein interactions with spatiotemporal resolution in living yeast to identify the molecular details of the pathway downstream of H3 S10 phosphorylation. This modification leads to the recruitment of the histone deacetylase Hst2p that subsequently removes an acetyl group from histone H4 lysine 16, freeing the H4 tail to interact with the surface of neighboring nucleosomes and promoting fiber condensation. This cascade of events provides a condensin-independent driving force of chromatin hypercondensation during mitosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilkins, Bryan J -- Rall, Nils A -- Ostwal, Yogesh -- Kruitwagen, Tom -- Hiragami-Hamada, Kyoko -- Winkler, Marco -- Barral, Yves -- Fischle, Wolfgang -- Neumann, Heinz -- New York, N.Y. -- Science. 2014 Jan 3;343(6166):77-80. doi: 10.1126/science.1244508.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Free Floater (Junior) Research Group "Applied Synthetic Biology," Institute for Microbiology and Genetics, Georg-August University Gottingen, 37077 Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24385627" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/metabolism ; Chromatin/*metabolism ; Chromosomes, Fungal/genetics/metabolism ; Cross-Linking Reagents/chemistry/radiation effects ; DNA-Binding Proteins/metabolism ; Histones/*metabolism ; Lysine/metabolism ; *Mitosis ; Multiprotein Complexes/metabolism ; Phosphorylation ; Protein Interaction Mapping ; *Protein Processing, Post-Translational ; Saccharomyces cerevisiae/genetics/*metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Serine/*metabolism ; Sirtuin 2/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Multimerization of Drosophila sperm protein Mst77F causes a unique condensed chromatin structure (2015)
    Oxford University Press
    Details
    Publication Date: 2015-04-02
    Description: 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.
    Print ISSN: 0305-1048
    Electronic ISSN: 1362-4962
    Topics: Biology
    Published by Oxford University Press
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