MOESM12 of Spermatid-specific linker histone HILS1 is a poor condenser of DNA and chromatin and preferentially associates with LINE-1 elements
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Additional file 12: Table S1. MACS 1.4.2 output file with annotations.A total of 32731 regions were selected as the overlapping peaks between the two replicates and the overlapping regions were annotated using HOMER.Keywords:
Spermatid
Line (geometry)
Linker
Condenser (optics)
Summary— In addition to the known Sertoli‐cell processes, processes of the mouse spermatid's cytoplasm are found to invaginate neighbouring spermatids. Surrounded by the adjacent Sertoli process, the spermatid processes form a “spermatid‐Sertoli cell process”. They are observed between spermatids at the same step or at different steps of their development and degenerate mostly at step 13 to 15 of spermiogenesis. Whether these structures are related to either spermatid exchanges or connections or participate to cytoplasm elimination is discussed.
Spermatid
Spermiogenesis
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Spermatid
Cell structure
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In the mouse, mature oocytes that have been injected with spermatid nuclei failed to become activated. Additional stimulation is required to trigger activation of the oocytes that leads to embryo development. This study was performed to determine whether simultaneous injection of mouse round spermatids and hamster oscillogen can fertilize oocytes and contribute to normal embryo development.We simultaneously injected mouse oocytes with mouse round spermatid nuclei and a preparation of oocyte-activating protein (oscillogen) from hamster spermatozoa and compared the results with those of injection of testicular spermatozoa.The incidence of normal fertilization and embryo development after simultaneous injection of round spermatid nuclei and hamster oscillogen was not significantly different from that after the injection of testicular spermatozoa. Moreover, the rate of development of two-cell embryos to term did not differ very much between the two groups of oocytes.Simultaneous injection of round spermatid nuclei and oscillogen appears to be an ideal method for successful activation of oocytes by spermatid nuclei in vitro.
Spermatid
Oocyte activation
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During dog-fish spermatogenesis, chromatin undergoes a continuous processing which involves two basic protein transitions: the first from somatic-type histones to spermatid-specific proteins and the second leading to protamines. Two spermatid-specific proteins S1 and S2 were isolated from nuclei of spermatid-enriched testis zone and the amino acid sequence of S1 has been determined. S1 contains 87 amino acids and has a molecular mass of 11179 Da. It is mainly characterized by a high content of basic residues (45%) and the presence of one residue of cysteine. Its primary structure shows that the N-terminal half is highly basic while the hydrophobic residues are preferentially localized in the C-terminal region. Three forms of S1 are present in testis which correspond to di-, mono- and nonphosphorylated molecules. This spermatid-specific protein shares no common structural feature with either histones and dog-fish protamines or rat spermatid-specific protein which has been previously described.
Spermatid
Protein primary structure
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It was shown that after treatment by Ca2+- and Mg2+-dependent DNAses and subsequent dosed ultrasonication the fractions of active and relatively inactive chromatins isolated from liver cell nuclei of rats differing in age contain all main types of histones, but differ considerably in the relative amounts of individual fractions of these proteins. In all age groups studied the proteins of relatively inactive chromatin are largely histones, while the amount of non-histone proteins is higher in active chromatin. In the course of postnatal development the amount of histones in both chromatin fractions is increased and that of non-histone proteins is decreased. This is probably due to heterochromatization of the chromatin complex in liver cells with ageing. In the course of postnatal ontogenesis the spectrum of non-histone proteins in both chromatin fractions is changed.
Non-histone protein
Histone-modifying enzymes
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The percent identity matrices of two sequence multiple alignments between linker histones from chicken and mammalian species are described. Linker histone protein sequences for chicken, mouse, rat and humans, available on public databases were used. This information is related to the research article entitled "Identification of novel post-translational modifications in linker histones from chicken erythrocytes"published in the Journal of Proteomics [1].
Linker
Sequence (biology)
Protein sequencing
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Inducer
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Post-meiotic spermatids become spermatozoa through developmental stages during spermiogenesis. Isolation of spermatid fractions is required to examine the change of protein expression during spermiogenesis. Here, we present a simple method to isolate spermatid fractions from mouse testes using unit gravity sedimentation in a BSA density gradient. Isolation of spermatid fractions can be used to analyze changes of transcript or protein during spermiogenesis. For complete details on the use and execution of this protocol, please refer to Kim et al. (2020).
Spermatid
Spermiogenesis
Isolation
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Spermatid
Spermiogenesis
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Histone-modifying enzymes
ChIA-PET
Histone code
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