Reference - Detail
| RRC ID | 33162 |
|---|---|
| Author | Kimura S, Loppin B. |
| Title | Two bromodomain proteins functionally interact to recapitulate an essential BRDT-like function in Drosophila spermatocytes. |
| Journal | Open Biol |
| Abstract |
In mammals, the testis-specific bromodomain and extra terminal (BET) protein BRDT is essential for spermatogenesis. In Drosophila, it was recently reported that the tBRD-1 protein is similarly required for male fertility. Interestingly, however, tBRD-1 has two conserved bromodomains in its N-terminus but it lacks an extra terminal (ET) domain characteristic of BET proteins. Here, using proteomics approaches to search for tBRD-1 interactors, we identified tBRD-2 as a novel testis-specific bromodomain protein. In contrast to tBRD-1, tBRD-2 contains a single bromodomain, but which is associated with an ET domain in its C-terminus. Strikingly, we show that tbrd-2 knock-out males are sterile and display aberrant meiosis in a way highly similar to tbrd-1 mutants. Furthermore, these two factors co-localize and are interdependent in spermatocytes. We propose that Drosophila tBRD-1 and tBRD-2 associate into a functional BET complex in spermatocytes, which recapitulates the activity of the single mammalian BRDT-like protein. |
| Volume | 5(2) |
| Pages | 140145 |
| Published | 2015-2-1 |
| DOI | 10.1098/rsob.140145 |
| PII | rsob.140145 |
| PMID | 25652540 |
| PMC | PMC4345279 |
| MeSH | Amino Acid Sequence Animals Animals, Genetically Modified Drosophila / genetics Drosophila / metabolism* Fertility Gene Order Genetic Loci Male Meiosis Molecular Sequence Data Mutation Nuclear Proteins / chemistry Nuclear Proteins / metabolism* Protein Binding Protein Interaction Domains and Motifs Sequence Alignment Spermatocytes / metabolism* |
| IF | 4.931 |
| Times Cited | 2 |
| WOS Category | BIOCHEMISTRY & MOLECULAR BIOLOGY |
| Altmetric score |
オルトメトリクス指標項目
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| Total number of mentions | 0 |
| Resource | |
| Drosophila | P(GSV6)GS13976 (DGRC#205636) |