Abstract
CTCF is the main architectural protein found in most of the examined bilaterian organisms. The cluster of the C2H2 zinc-finger domains involved in recognition of long DNA-binding motif is only part of the protein that is evolutionarily conserved, while the N-terminal domain (NTD) has different sequences. Here, we performed biophysical characterization of CTCF NTDs from various species representing all major phylogenetic clades of higher metazoans. With the exception of Drosophilides, the N-terminal domains of CTCFs show an unstructured organization and absence of folded regions in vitro. In contrast, NTDs of Drosophila melanogaster and virilis CTCFs contain unstructured folded regions that form tetramers and dimers correspondingly in vitro. Unexpectedly, most NTDs are able to self-associate in the yeast two-hybrid and co-immunoprecipitation assays. These results suggest that NTDs of CTCFs might contribute to the organization of CTCF-mediated long-distance interactions and chromosomal architecture.
Highlights
CTCF is the main architectural protein found in most of the examined bilaterian organisms
It is believed that CTCF is the main architectural protein in mammals, which is responsible for the organization of topologically associated domains (TADs) boundaries and distance interactions between enhancers and promoters[12,13,14,15,16]
We described the N-terminal multimerization module between 70 and 163 aa of CTCF protein from Drosophila melanogaster, which is essential for functional activity of the dmCTCF protein, but the first 70 residues contribute to its stability and together with 70–163 aa most likely are parts of the entire protein domain[37]
Summary
CTCF is the main architectural protein found in most of the examined bilaterian organisms. NTDs of Drosophila melanogaster and virilis CTCFs contain unstructured folded regions that form tetramers and dimers correspondingly in vitro. Most NTDs are able to self-associate in the yeast two-hybrid and co-immunoprecipitation assays These results suggest that NTDs of CTCFs might contribute to the organization of CTCF-mediated long-distance interactions and chromosomal architecture. It is believed that CTCF is the main architectural protein in mammals, which is responsible for the organization of TAD boundaries and distance interactions between enhancers and promoters[12,13,14,15,16]. In other selected organisms from different bilaterian clades, the N-terminal CTCF domains are intrinsically disordered and unable to form dimers in vitro. The N-terminal domains from CTCF of human and several other organisms showed self-interaction in the yeast two-hybrid (Y2H) and co-immunoprecipitation assays
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