Two bromodomain proteins functionally interact to recapitulate an essential BRDT-like function in Drosophila spermatocytes.

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.

journal_name

Open Biol

journal_title

Open biology

authors

Kimura S,Loppin B

doi

10.1098/rsob.140145

subject

Has Abstract

pub_date

2015-02-01 00:00:00

pages

140145

issue

2

issn

2046-2441

pii

rsob.140145

journal_volume

5

pub_type

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