Abstract
Bromodomain and Extra-terminal motif (BET) proteins play a central role in transcription regulation and chromatin signalling pathways. They are present in unicellular eukaryotes and in this study, the role of the BET protein Bdf1 has been explored in Saccharomyces cerevisiae. Mutation of Bdf1 bromodomains revealed defects on both the formation of spores and the meiotic progression, blocking cells at the exit from prophase, before the first meiotic division. This phenotype is associated with a massive deregulation of the transcription of meiotic genes and Bdf1 bromodomains are required for appropriate expression of the key meiotic transcription factor NDT80 and almost all the Ndt80-inducible genes, including APC complex components. Bdf1 notably accumulates on the promoter of Ndt80 and its recruitment is dependent on Bdf1 bromodomains. In addition, the ectopic expression of NDT80 during meiosis partially bypasses this dependency. Finally, purification of Bdf1 partners identified two independent complexes with Bdf2 or the SWR complex, neither of which was required to complete sporulation. Taken together, our results unveil a new role for Bdf1 –working independently from its predominant protein partners Bdf2 and the SWR1 complex–as a regulator of meiosis-specific genes.
Highlights
Protein members of the Bromodomain and Extra-terminal motif (BET) family share a conserved modular architecture, with two bromodomains in their N-terminal part, an extra-terminal recruitment (ET) domain and other conserved motifs
In this study we investigated the functional role of the bromodomains of the chromatin protein Bdf1 during yeast gametogenesis
Bdf1 bromodomains are required for the expression of key meiotic genes and the master regulator NDT80
Summary
Protein members of the BET family share a conserved modular architecture, with two bromodomains in their N-terminal part, an extra-terminal recruitment (ET) domain and other conserved motifs. BET proteins are present in unicellular eukaryotes such as the model organism Saccharomyces cerevisiae, where two homologous genes, Bdf and Bdf, are expressed. Bdf has a typical BET protein structure, with two bromodomains, one ET domain and other conserved motifs. Multiple functional roles have been proposed for this protein, which was first described as a regulator of snRNA [2] and identified as part of the yeast’s general transcription factor, TFIID [3]. Unlike its human homologue TAF(II)250, the TAF(II)145 protein lacks a module with bromodomains. Bdf plays a role in regulating gene expression in response to various stresses [5,6,7,8]
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