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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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BL-Hi-C is an efficient and sensitive approach for capturing structural and regulatory chromatin interactions

Project description:We propose a novel in situ Hi-C method named Bridge-Linker-Hi-C (BL-Hi-C) for structural and regulatory chromatin interactions capture by restriction enzyme targeting and two-step proximity ligation. It improves the sensitivity and specificity for active chromatin loop detection and can reveal a better enhancer-promoter regulatory architecture than conventional method at a lower sequencing depth and with a simpler protocol.

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Leishmania regulates host YY1: comparative proteomic analysis identifies infection modulated YY1 dependent proteinsLeishmania regulates host YY1: comparative proteomic analysis identifies infection modulated YY1 dependent proteins

Project description:The protein Yin-Yang 1 (YY1) is a ubiquitous multifunctional transcription factor. Interestingly, there are several cellular functions controlled by YY1 that could play a role in Leishmania pathogenesis. Leishmaniasis is a human disease caused by protozoan parasites of the genus Leishmania. This study examined the potential role of macrophage YY1 in promoting Leishmania intracellular survival. Knockdown of YY1 resulted in attenuated survival of Leishmania in infected macrophages, suggesting a role of YY1 in Leishmania persistence. Biochemical fractionation studies revealed Leishmania infection caused redistribution of YY1 to the cytoplasm from the nucleus where it is primarily located. Inhibition of nuclear transport by leptomycin B attenuates infection-mediated YY1 redistribution and reduces Leishmania survival. This suggests that Leishmania induces the translocation of YY1 from the nucleus to the cytoplasm of infected cells, where it may regulate host molecules to favour parasite survival. A label-free quantitative whole proteome approach showed that the expression of a large number of macrophage proteins was dependent on the YY1 level. Interestingly, several of these proteins were modulated in Leishmania-infected cells, revealing YY1-dependent host response and suggesting their potential role in Leishmania pathogenesis. Together, these findings identify YY1 as a novel and essential virulence factor by proxy that promotes Leishmania survival.

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YY1 stabilizes super enhancer-promoter loops and gene expression during mesenchymal stem cell aging (Hi-C)

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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.

2024-01-26 | PXD038431 | Pride

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