Repression of gene expression by the histone methyltransferase G9a is guided by two zinc finger proteins that can recognize consensus sequences in DNA.
In humans, specific sequence features can predict whether meiotic recombination occurs at sites bound by the protein PRDM9, whose DNA-binding zinc-finger domain can unexpectedly bind to gene promoters and to other copies of PRDM9.
Though generally considered a transcriptional repressor, Wiz may also function as a transcriptional activator in the mouse brain and is required for normal behaviour.
Protein binding microarrays highlight the diversification of DNA-binding motifs for the nuclear hormone receptor and C2H2 zinc finger transcription factor families, and reveal unexpected diversity in motifs for the T-box and DM families.
Structural, biochemical, and proteomic analyses of a four-subunit core module of the cleavage and polyadenylation specificity factor complex reveal its molecular architecture and specific determinants of polyadenylation signal recognition in human mRNAs.
A novel zinc finger transcription factor regulates expression of multiple genes in late stage thymocytes and recent thymic emigrants to promote formation of the naïve T cell compartment.
Drosophila has almost all transcription factor binding specificities available to humans; and human transcription factors with divergent specificities operate in cell types that are not found in fruit flies.
While photoreceptor and bipolar cells exhibit very similar cis-regulatory grammars, subtle differences in homeodomain motif enrichment represent a key distinction driving the divergence in their transcriptomes.
ZCWPW1 has co-evolved with PRDM9, in particular the PRDM9-SET domain, and although not involved in PRDM9's role in positioning recombination events, it is required for PRDM9's role in pairing chromosomes.
