Biology subjects

Polveche, H.

Publications and source records attributed to Polveche, H..

2 recordsLinked to original sources

bioRxiv2018

Physical and functional interaction between SET1/COMPASS complex component CFP-1 and a Sin3 HDAC complex

The CFP1 CXXC zinc finger protein targets the SET1/COMPASS complex to non-methylated CpG rich promoters to implement tri-methylation of histone H3 Ly4 (H3K4me3). Although H3K4me3 is widely associated with gene expression, the effects of CFP1 loss depend on chromatin context, so it is important to understand the relationship between CFP1 and other chromatin factors. Using a proteomics approach, we identified an unexpected link between C. elegans CFP-1 and a Rpd3/Sin3 histone deacetylase complex. We find that mutants of CFP-1, SIN-3, and the catalytic subunit SET-2/SET1 have similar phenotypes and misregulate common genes. CFP-1 directly binds SIN-3 through a region including the conserved PAH1 domain and recruits SIN-3 and the HDA-1/HDAC subunit to H3K4me3 enriched promoters. Our results reveal a novel role for CFP-1 in mediating interaction between SET1/COMPASS and a Sin3 HDAC complex at promoters and uncover coordinate regulation of gene expression by chromatin complexes having distinct activities.

genomics↗

bioRxiv2018

Interplay between coding and exonic splicing regulatory sequences

The inclusion of exons during the splicing process depends on the binding of splicing factors to short low-complexity regulatory sequences. The relationship between exonic splicing regulatory sequences and coding sequences is still poorly understood. We demonstrate that exons that are coregulated by any splicing factor share a similar nucleotide composition bias. We next demonstrate that coregulated exons preferentially code for amino acids with similar physicochemical properties because of the non-randomness properties of the genetic code. Indeed, amino acids sharing physicochemical properties correspond to codons that have the same nucleotide composition bias. These observations reveal an unanticipated bidirectional interplay between the physicochemical features encoded by exons and exon splicing regulation by splicing factors. We propose that the splicing regulation of an exon by a splicing factor is tightly interconnected with the physicochemical properties of the exon-encoded protein domain depending on the splicing-factor affinity for specific nucleotides.

genomics↗