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      Testes and duct deferens of mice during space flight: cytoskeleton structure, sperm-specific proteins and epigenetic events

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          Abstract

          To analyze the effect of gravity on the structure of germinal tissues, we examined tissues of the testes and duct deferens of mice that were exposed to space flight conditions for 21–24 days (experiment Rodent Research-4, SpaceX-10 mission, February 2017, USA). We evaluated the levels of cytoskeletal proteins, sperm-specific proteins, and epigenetic events; in particular, we evaluated levels of 5-hydroxymethylcytosine and of enzymes that regulate DNA methylation/demethylation. We did not detect changes in the levels of cytoskeletal proteins, sperm-specific proteins, DNA-methylases, DNA demethylases, DNA acetylases, or histone deacetylases. However, there were changes at the gene expression level. In particular, there was an increase in the demethylase Tet2 and a decrease in the histone deacetylase Hdac1. These gene expression changes may be of key importance during the early period of readaptation since they could lead to an increase in the expression of target genes.

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          Most cited references32

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          Histone H4-K16 acetylation controls chromatin structure and protein interactions.

          Acetylation of histone H4 on lysine 16 (H4-K16Ac) is a prevalent and reversible posttranslational chromatin modification in eukaryotes. To characterize the structural and functional role of this mark, we used a native chemical ligation strategy to generate histone H4 that was homogeneously acetylated at K16. The incorporation of this modified histone into nucleosomal arrays inhibits the formation of compact 30-nanometer-like fibers and impedes the ability of chromatin to form cross-fiber interactions. H4-K16Ac also inhibits the ability of the adenosine triphosphate-utilizing chromatin assembly and remodeling enzyme ACF to mobilize a mononucleosome, indicating that this single histone modification modulates both higher order chromatin structure and functional interactions between a nonhistone protein and the chromatin fiber.
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            Structure and ligand of a histone acetyltransferase bromodomain.

            Histone acetylation is important in chromatin remodelling and gene activation. Nearly all known histone-acetyltransferase (HAT)-associated transcriptional co-activators contain bromodomains, which are approximately 110-amino-acid modules found in many chromatin-associated proteins. Despite the wide occurrence of these bromodomains, their three-dimensional structure and binding partners remain unknown. Here we report the solution structure of the bromodomain of the HAT co-activator P/CAF (p300/CBP-associated factor). The structure reveals an unusual left-handed up-and-down four-helix bundle. In addition, we show by a combination of structural and site-directed mutagenesis studies that bromodomains can interact specifically with acetylated lysine, making them the first known protein modules to do so. The nature of the recognition of acetyl-lysine by the P/CAF bromodomain is similar to that of acetyl-CoA by histone acetyltransferase. Thus, the bromodomain is functionally linked to the HAT activity of co-activators in the regulation of gene transcription.
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              Function and selectivity of bromodomains in anchoring chromatin-modifying complexes to promoter nucleosomes.

              The functions of the SAGA and SWI/SNF complexes are interrelated and can form stable "epigenetic marks" on promoters in vivo. Here we show that stable promoter occupancy by SWI/SNF and SAGA in the absence of transcription activators requires the bromodomains of the Swi2/Snf2 and Gcn5 subunits, respectively, and nucleosome acetylation. This acetylation can be brought about by either the SAGA or NuA4 HAT complexes. The bromodomain in the Spt7 subunit of SAGA is dispensable for this activity but will anchor SAGA if it is swapped into Gcn5, indicating that specificity of bromodomain function is determined in part by the subunit it occupies. Thus, bromodomains within the catalytic subunits of SAGA and SWI/SNF anchor these complexes to acetylated promoter nucleosomes.
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                Author and article information

                Contributors
                iogneva@yandex.ru
                Journal
                Sci Rep
                Sci Rep
                Scientific Reports
                Nature Publishing Group UK (London )
                2045-2322
                5 July 2019
                5 July 2019
                2019
                : 9
                : 9730
                Affiliations
                [1 ]ISNI 0000 0004 0390 4822, GRID grid.418847.6, Cell Biophysics Laboratory, , State Scientific Center of Russian Federation Institute of Biomedical Problems of the Russian Academy of Sciences, ; Khoroshevskoyoe shosse, 76a, Moscow, 123007 Russia
                [2 ]ISNI 0000 0001 2288 8774, GRID grid.448878.f, I.M. Sechenov First Moscow State Medical University, ; 8-2 Trubetskaya St., Moscow, 119991 Russia
                Article
                46324
                10.1038/s41598-019-46324-3
                6611814
                31278362
                7915a291-2b5c-4fdb-9962-6a4203e0ae56
                © The Author(s) 2019

                Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

                History
                : 3 June 2019
                : 26 June 2019
                Funding
                Funded by: FundRef https://doi.org/10.13039/501100002674, Russian Academy of Sciences (RAS);
                Award ID: Postgenomic technologies and perspective solutions in the biomedicine
                Award ID: Postgenomic technologies and perspective solutions in the biomedicine
                Award ID: Postgenomic technologies and perspective solutions in the biomedicine
                Award Recipient :
                Funded by: FundRef https://doi.org/10.13039/501100003443, Ministry of Education and Science of the Russian Federation (Minobrnauka);
                Award ID: Russian Academic Excellence Project 5-100
                Award ID: Russian Academic Excellence Project 5-100
                Award ID: Russian Academic Excellence Project 5-100
                Award Recipient :
                Categories
                Article
                Custom metadata
                © The Author(s) 2019

                Uncategorized
                cytoskeleton,epigenetic memory
                Uncategorized
                cytoskeleton, epigenetic memory

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