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The bromodomain-containing protein tBRD-1 is specifically expressed in spermatocytes and is essential for male fertility
By a conserved cellular differentiation process, spermatogenesis leads to formation of haploid sperm for successful reproduction. In Drosophila and in mammals, post-meiotic spermatid differentiation depends on several translationally repressed and stored mRNAs that are often expressed exclusively in...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Company of Biologists
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3509448/ https://www.ncbi.nlm.nih.gov/pubmed/23213453 http://dx.doi.org/10.1242/bio.20121255 |
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author | Leser, Katja Awe, Stephan Barckmann, Bridlin Renkawitz-Pohl, Renate Rathke, Christina |
author_facet | Leser, Katja Awe, Stephan Barckmann, Bridlin Renkawitz-Pohl, Renate Rathke, Christina |
author_sort | Leser, Katja |
collection | PubMed |
description | By a conserved cellular differentiation process, spermatogenesis leads to formation of haploid sperm for successful reproduction. In Drosophila and in mammals, post-meiotic spermatid differentiation depends on several translationally repressed and stored mRNAs that are often expressed exclusively in the testis through a cell type specific transcriptional program. In Drosophila, the mRNAs of proteins required for post-meiotic chromatin reorganisation, like ProtB and Mst77F, are transcribed in meiotic spermatocytes and subjected to translational repression for days. Transcription of many of these translationally repressed mRNAs depends on testis-specific homologs of TATA box binding protein-associated factors (tTAFs). Here, we identified the testis-specific bromodomain protein, tBRD-1, that is only expressed in primary spermatocytes. Bromodomain proteins are able to recognise and bind acetylated histones and non-histone proteins. We generated tbrd-1 mutant flies and observed that function of tBRD-1 is required for male fertility. tBRD-1 partially colocalised with tTAFs, TAF1 and Polycomb to a Fibrillarin-deficient region within the spermatocyte nucleolus. The nucleolar localisation of tBRD-1 depended on tTAF function but not the other way round. Further, we could show that ectopically expressed tBRD-1-eGFP is able to bind to the interbands of polytene chromosomes. By inhibitor treatment of cultured testis we observed that sub-cellular localisation of tBRD-1 may depend on the acetylation status of primary spermatocytes. |
format | Online Article Text |
id | pubmed-3509448 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The Company of Biologists |
record_format | MEDLINE/PubMed |
spelling | pubmed-35094482012-12-04 The bromodomain-containing protein tBRD-1 is specifically expressed in spermatocytes and is essential for male fertility Leser, Katja Awe, Stephan Barckmann, Bridlin Renkawitz-Pohl, Renate Rathke, Christina Biol Open Research Article By a conserved cellular differentiation process, spermatogenesis leads to formation of haploid sperm for successful reproduction. In Drosophila and in mammals, post-meiotic spermatid differentiation depends on several translationally repressed and stored mRNAs that are often expressed exclusively in the testis through a cell type specific transcriptional program. In Drosophila, the mRNAs of proteins required for post-meiotic chromatin reorganisation, like ProtB and Mst77F, are transcribed in meiotic spermatocytes and subjected to translational repression for days. Transcription of many of these translationally repressed mRNAs depends on testis-specific homologs of TATA box binding protein-associated factors (tTAFs). Here, we identified the testis-specific bromodomain protein, tBRD-1, that is only expressed in primary spermatocytes. Bromodomain proteins are able to recognise and bind acetylated histones and non-histone proteins. We generated tbrd-1 mutant flies and observed that function of tBRD-1 is required for male fertility. tBRD-1 partially colocalised with tTAFs, TAF1 and Polycomb to a Fibrillarin-deficient region within the spermatocyte nucleolus. The nucleolar localisation of tBRD-1 depended on tTAF function but not the other way round. Further, we could show that ectopically expressed tBRD-1-eGFP is able to bind to the interbands of polytene chromosomes. By inhibitor treatment of cultured testis we observed that sub-cellular localisation of tBRD-1 may depend on the acetylation status of primary spermatocytes. The Company of Biologists 2012-05-09 /pmc/articles/PMC3509448/ /pubmed/23213453 http://dx.doi.org/10.1242/bio.20121255 Text en © 2012. Published by The Company of Biologists Ltd http://creativecommons.org/licenses/by-nc-sa/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial Share Alike License (http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Research Article Leser, Katja Awe, Stephan Barckmann, Bridlin Renkawitz-Pohl, Renate Rathke, Christina The bromodomain-containing protein tBRD-1 is specifically expressed in spermatocytes and is essential for male fertility |
title | The bromodomain-containing protein tBRD-1 is specifically expressed in spermatocytes and is essential for male fertility |
title_full | The bromodomain-containing protein tBRD-1 is specifically expressed in spermatocytes and is essential for male fertility |
title_fullStr | The bromodomain-containing protein tBRD-1 is specifically expressed in spermatocytes and is essential for male fertility |
title_full_unstemmed | The bromodomain-containing protein tBRD-1 is specifically expressed in spermatocytes and is essential for male fertility |
title_short | The bromodomain-containing protein tBRD-1 is specifically expressed in spermatocytes and is essential for male fertility |
title_sort | bromodomain-containing protein tbrd-1 is specifically expressed in spermatocytes and is essential for male fertility |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3509448/ https://www.ncbi.nlm.nih.gov/pubmed/23213453 http://dx.doi.org/10.1242/bio.20121255 |
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