RNA interactions are essential for proper CTCF function
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA517076 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR8487480.fastq.gz | Fastqsanger.gz | |||
| SRR8487490.fastq.gz | Fastqsanger.gz | |||
| SRR8487500_1.fastq.gz | Fastqsanger.gz | |||
| SRR8487500_2.fastq.gz | Fastqsanger.gz | |||
| SRR8487481.fastq.gz | Fastqsanger.gz |
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Project description:As an essential regulator of higher-order chromatin structures, CTCF is a highly conserved DNA binding protein with a central DNA-binding domain of 11 tandem zinc fingers, which are flanked by N- and C-terminal domains of intrinsically disordered regions. The N-terminal domain interacts with cohesin complex and the central ZF domains recognize a large range of diverse genomic sites. However, the function of C-terminal unstructured domain remains less understood. Here, we found that deletion of C-terminal fragment of 116 amino acid increases CTCF-DNA binding. By genetic dissection of this fragment, we uncovered a negatively-charged region responsible for repressing CTCF binding to DNA. Thus, the unstructured C-terminal domain play an important role in maintaining proper CTCF-DNA interactions.
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Project description:As an essential regulator of higher-order chromatin structures, CTCF is a highly conserved DNA binding protein with a central DNA-binding domain of 11 tandem zinc fingers, which are flanked by N- and C-terminal domains of intrinsically disordered regions. The N-terminal domain interacts with cohesin complex and the central ZF domains recognize a large range of diverse genomic sites. However, the function of C-terminal unstructured domain remains less understood. Here, we found that deletion of C-terminal fragment of 116 amino acid increases CTCF-DNA binding. By genetic dissection of this fragment, we uncovered a negatively-charged region responsible for repressing CTCF binding to DNA. Thus, the unstructured C-terminal domain play an important role in maintaining proper CTCF-DNA interactions.
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Project description:As an essential regulator of higher-order chromatin structures, CTCF is a highly conserved DNA binding protein with a central DNA-binding domain of 11 tandem zinc fingers, which are flanked by N- and C-terminal domains of intrinsically disordered regions. The N-terminal domain interacts with cohesin complex and the central ZF domains recognize a large range of diverse genomic sites. However, the function of C-terminal unstructured domain remains less understood. Here, we found that deletion of C-terminal fragment of 116 amino acid increases CTCF-DNA binding. By genetic dissection of this fragment, we uncovered a negatively-charged region responsible for repressing CTCF binding to DNA. Thus, the unstructured C-terminal domain play an important role in maintaining proper CTCF-DNA interactions.
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Project description:As an essential regulator of higher-order chromatin structures, CTCF is a highly conserved DNA binding protein with a central DNA-binding domain of 11 tandem zinc fingers, which are flanked by N- and C-terminal domains of intrinsically disordered regions. The N-terminal domain interacts with cohesin complex and the central ZF domains recognize a large range of diverse genomic sites. However, the function of C-terminal unstructured domain remains less understood. Here, we found that deletion of C-terminal fragment of 116 amino acid increases CTCF-DNA binding. By genetic dissection of this fragment, we uncovered a negatively-charged region responsible for repressing CTCF binding to DNA. Thus, the unstructured C-terminal domain play an important role in maintaining proper CTCF-DNA interactions.
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