Birds of prey
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA431699 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:Mandarin fish Siniperca chuatsi (Basilewsky) (Percichthyidae), as a demersal piscivore, has very specialized feeding habits, for as soon as they start feeding the fry of this fish feed solely on fry of other fish species. In rearing conditions, mandarin fish has been found to accept live prey fish only, and refuse dead prey fish or artificial diets, very little is currently known about the molecular mechanisms of multiple genes which cover different pathways influencing the specialized food habit, such as live prey. We performed transcriptome comparisons between dead prey fish feeders and nonfeeders in mandarin fish. The determination mechanisms of specialized food habit (live prey fish) in mandarin fish could provide some instructions for research of food habit in animals, including mammals.
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Project description:Lysine methylation is part of the posttranscriptional histone code employed to recruit modification specific readers to chromatin. Unbiased, quantitative mass spectrometry approaches combined with peptide pull-downs have been used to study histone methylation-dependent binders in mammalian cells. Here, we extend the study to birds by investigating the interaction partners for H3K4me3, H3K9me3, H3K27me3 and H3K36me3 in chicken (gallus gallus) and zebra finch (taeniopygia guttata) using label free quantitative proteomics. In general, we find very strong overlap in interaction partners for the trimethyl marks in birds compared to mammals, underscoring the known conserved function of these modifications. In agreement with their epigenetic role, we find binding of PHF2 and members of the TFIID, SAGA, SET1 and NURF complex to the activation mark H3K4me3. Our data furthermore supports the existence of a LID complex in vertebrates recruited to the H3K4me3. The repressive marks are bound by the HP1 proteins and the EED subunit of the PRC2 complex as well as by WIZ. Like the screens in mammals, we found ZNF462, ZNF828 and POGZ enriched at H3K9me3. However, we noted some unexpected differences. First, we did not observe the enrichment of CDYL and CDYL2 at the repressive marks. Second N-PAC (also known as GLYR1), an H3K36me3 interactor in mammals, is not binding to this modification in our screen. This suggests that despite strong conservation of the histone tail sequence, species-specific differences in epigenetic readers may have evolved.
2016-01-04 | PXD002282 | Pride