Proteomics

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Probing the Role of O-GlcNAcylation in Modulating Protein-DNA Interactions: Insights from a Proteomic Transcription Factor Response Element-Based Pulldown Screening Approach


ABSTRACT: O-linked β-N-acetylglucosamine (O-GlcNAc), a critical post-translational modification (PTM) predominantly found in the nucleus, plays a substantial role in regulating gene expression by modulating transcription factors (TFs) activity. Herein, by utilizing a pulldown screening approach termed as tandem array of transcription factors response elements (catTFREs), we unravel the profound impact of fluctuating levels of O-GlcNAcylation on the DNA binding efficiency of endogenous TFs. The proteins were enriched for label-free quantitative proteomics by LC-MS/MS.

ORGANISM(S): Homo Sapiens

SUBMITTER: Yubo Liu  

PROVIDER: PXD057128 | iProX | Thu Oct 24 00:00:00 BST 2024

REPOSITORIES: iProX

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Publications

DNA probe pulldown screening uncovers O-GlcNAcylation modulation of transcription factor DNA interactions.

Li Guofang G   Meng Fanxu F   Zhong Xiaomin X   Yu Kairan K   Zhang Nana N   Zhang Keren K   Huang Huang H   Li Wenli W   Zhang Jianing J   Wang Wei W   Ren Yan Y   Liu Yubo Y  

Scientific reports 20250702 1


O-linked β-N-acetylglucosamine (O-GlcNAc), a critical post-translational modification predominantly found in the nucleus, plays a substantial role in regulating gene expression by modulating transcription factors (TFs) activity. However, quantitative analysis investigating the influence of O-GlcNAcylation on protein-DNA interactions at a proteome scale remains undone. Herein, a pulldown screening approach using a consensus TF response element (catTFRE) was employed to unravel the impact of fluct  ...[more]

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