Nucleoporin 153 links nuclear pore complex to chromatin architecture by mediating CTCF and cohesin binding
نویسندگان
چکیده
منابع مشابه
CTCF physically links cohesin to chromatin.
Cohesin is required to prevent premature dissociation of sister chromatids after DNA replication. Although its role in chromatid cohesion is well established, the functional significance of cohesin's association with interphase chromatin is not clear. Using a quantitative proteomics approach, we show that the STAG1 (Scc3/SA1) subunit of cohesin interacts with the CCTC-binding factor CTCF bound ...
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It is becoming increasingly clear that eukaryotic genomes are subjected to higher-order chromatin organization by the CCCTC-binding factor/cohesin complex. Their dynamic interactions in three dimensions within the nucleus regulate gene transcription by changing the chromatin architecture. Such spatial genomic organization is functionally important for the spatial disposition of chromosomes to c...
متن کاملCTCF and cohesin regulate chromatin loop stability with distinct dynamics
Folding of mammalian genomes into spatial domains is critical for gene regulation. The insulator protein CTCF and cohesin control domain location by folding domains into loop structures, which are widely thought to be stable. Combining genomic and biochemical approaches we show that CTCF and cohesin co-occupy the same sites and physically interact as a biochemically stable complex. However, usi...
متن کاملCohesin and CTCF differentially affect chromatin architecture and gene expression in human cells.
Recent studies of genome-wide chromatin interactions have revealed that the human genome is partitioned into many self-associating topological domains. The boundary sequences between domains are enriched for binding sites of CTCC-binding factor (CTCF) and the cohesin complex, implicating these two factors in the establishment or maintenance of topological domains. To determine the role of cohes...
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ژورنال
عنوان ژورنال: Nature Communications
سال: 2020
ISSN: 2041-1723
DOI: 10.1038/s41467-020-16394-3