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Bridge Linker-Hi-C (BL-Hi-C) analysis after YY1 knockdown in glioblastoma stem cells

ABSTRACT: Bridge Linker-Hi-C (BL-Hi-C) analysis after YY1 knockdown in glioblastoma stem cells

PROVIDER: PRJNA655726 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR12403817_1.fastq.gz	Fastqsanger.gz
	SRR12403817_2.fastq.gz	Fastqsanger.gz
	SRR12403818_1.fastq.gz	Fastqsanger.gz
	SRR12403818_2.fastq.gz	Fastqsanger.gz
	SRR12403819_1.fastq.gz	Fastqsanger.gz

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Bridge Linker-Hi-C (BL-Hi-C) analysis after YY1 knockdown in glioblastoma stem cells

Project description:Bridge Linker-Hi-C (BL-Hi-C) analysis after YY1 knockdown in glioblastoma stem cells

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Fusobacterium necrophorum BL strain:BL

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Assessing the dynamics and macromolecular interactions of the intrinsically disordered protein YY1

Project description:YY1 is a ubiquitously expressed, intrinsically disordered transcription factor involved in neural development. The oligomeric state of YY1 varies depending on the environment. These changes may alter its DNA binding ability and hence its transcriptional activity. In addition to its oligomeric state, the interaction of YY1 with proteins such as FOXP2 can impact its role in transcription. The aim of this work is to study the structure and dynamics of YY1 binding to DNA and to determine the influence of oligomerisation and associations with FOXP2 on its DNA binding mechanism. Size exclusion chromatography, fluorescence anisotropy and electrophoretic mobility shift assays were used to study YY1 oligomerisation and interaction with FOXP2. To better understand potential structural changes to YY1 upon DNA binding, hydrogen deuterium exchange mass spectrometry was used. The results indicate that YY1 consists of specific structured regions, while most of the sequence remains disordered. Furthermore, the oligomeric nature of the protein is dependent on ionic strength. DNA affects oligomerisation and the protein undergoes changes in structure and dynamics upon DNA binding. YY1 and FOXP2 were found to interact with each other both in isolation and in the presence of YY1-specific DNA. The heterogeneous, dynamic multimerisation of YY1 identified in this work is, therefore, likely to be important for its ability to make heterologous associations with other proteins such as FOXP2. The interactions that YY1 forms with itself, FOXP2 and DNA form part of an intricate mechanism of transcriptional regulation by YY1, which is vital for appropriate neural development.

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