2012
DOI: 10.1074/jbc.m111.288167
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Insights into Role of Bromodomain, Testis-specific (Brdt) in Acetylated Histone H4-dependent Chromatin Remodeling in Mammalian Spermiogenesis

Abstract: Background: Brdt is a double bromodomain containing, testis-specific protein known to recognize acetylated H4. Results: Smarce1, identified as a novel Brdt interacting partner, shows enhanced interaction upon hyperacetylation of histone H4. Conclusion: Brdt, a chromatin remodeling factor, associates with Smarce1 in haploid spermatids. Significance: This study sheds light on the molecular events underlying global chromatin remodeling during mammalian spermiogenesis.

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Cited by 63 publications
(67 citation statements)
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“…The mechanism of BRDT action seems to entail recognition of acetylated chromatin via BD1 in elongating spermatids, followed by a process the investigators termed ''chromatin squeezing'' through interaction of two (or more) BRDT molecules, which would facilitate histone eviction. A similar observation was also reported in rat spermatids (Dhar et al 2012), but an indirect effect of Brdt on histone eviction cannot be excluded.…”
Section: Chromatin Post-translational Modifications (Ptms) In Post-mesupporting
confidence: 62%
“…The mechanism of BRDT action seems to entail recognition of acetylated chromatin via BD1 in elongating spermatids, followed by a process the investigators termed ''chromatin squeezing'' through interaction of two (or more) BRDT molecules, which would facilitate histone eviction. A similar observation was also reported in rat spermatids (Dhar et al 2012), but an indirect effect of Brdt on histone eviction cannot be excluded.…”
Section: Chromatin Post-translational Modifications (Ptms) In Post-mesupporting
confidence: 62%
“…Adult Brdt À/À mouse testes lack post-meiotic germ cells [Dhar et al 2012;Gaucher et al 2012;Jacobson et al 2000;Plaseski et al 2012;Pivot-Pajot et al 2003]. In this study, we genotyped 9 RNF8 SNPs and 5 BRDT SNPs to investigate whether genetic changes of the SNPs were risk factors for NOA.…”
Section: Introductionmentioning
confidence: 99%
“…At the molecular level, Brdt interacts with Smarce1, a component of the ATP-dependent SWI/SNF family of chromatin remodeling complexes that function to destabilize histone-DNA interaction. In spermatid nuclei, the interaction between Smarce1 and Brdt is enhanced by histone H4 acetylation [30]. Meanwhile, Brdt can interact with itself [30,31].…”
Section: Biological Significance Of Protein Acetylation In Spermatogementioning
confidence: 97%
“…In spermatid nuclei, the interaction between Smarce1 and Brdt is enhanced by histone H4 acetylation [30]. Meanwhile, Brdt can interact with itself [30,31]. Under conditions that promote histone acetylation, Brdt molecules interact in a head-to-tail manner, which identifies its directional alignment and probable "polymerization" on chromatin [31].…”
Section: Biological Significance Of Protein Acetylation In Spermatogementioning
confidence: 99%
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