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Quantitative imaging of loop extruders rebuilding interphase genome architecture after mitosis.
J Cell Biol
March 2025
Cell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL) , Heidelberg, Germany.
How cells establish the interphase genome organization after mitosis is incompletely understood. Using quantitative and super-resolution microscopy, we show that the transition from a Condensin to a Cohesin-based genome organization occurs dynamically over 2 h. While a significant fraction of Condensins remains chromatin-bound until early G1, Cohesin-STAG1 and its boundary factor CTCF are rapidly imported into daughter nuclei in telophase, immediately bind chromosomes as individual complexes, and are sufficient to build the first interphase TAD structures.
View Article and Find Full Text PDFPain in rheumatoid arthritis: Emerging role of high mobility group box 1 protein-HMGB1.
Life Sci
January 2025
Agroprocessing and Technology Division, CSIR-National Institute for Interdisciplinary Science and Technology, Thiruvananthapuram 695019, Kerala, India; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad 201002, India. Electronic address:
Rheumatoid arthritis (RA) is a chronic inflammatory disease where pain, driven by both inflammatory and non-inflammatory processes, is a major concern for patients. This pain can persist even after joint inflammation subsides. High mobility group box-1 (HMGB1) is a non-histone-DNA binding protein located in the nucleus that plays a key role in processes such as DNA transcription, recombination, and replication.
View Article and Find Full Text PDFThe CECR2 bromodomain displays distinct binding modes to select for acetylated histone proteins versus non-histone ligands.
bioRxiv
December 2024
Department of Pharmacology, Larner College of Medicine, University of Vermont, Burlington, VT, 05405, USA.
The cat eye syndrome chromosome region candidate 2 (CECR2) protein is an epigenetic regulator involved in chromatin remodeling and transcriptional control. The CECR2 bromodomain (CECR2-BRD) plays a pivotal role in directing the activity of CECR2 through its capacity to recognize and bind acetylated lysine residues on histone proteins. This study elucidates the binding specificity and structural mechanisms of CECR2-BRD interactions with both histone and non-histone ligands, employing techniques such as isothermal titration calorimetry (ITC), nuclear magnetic resonance (NMR) spectroscopy, and a high-throughput peptide assay.
View Article and Find Full Text PDF[The Drosophila Zinc Finger Proteins Aef1 and CG10543 Are Co-Localized with SAGA, SWI/SNF, and ORC Complexes on Gene Promoters and Involved in Transcription Regulation].
Mol Biol (Mosk)
December 2024
Institute of Gene Biology, Russian Academy of Sciences, Moscow, 119334 Russia.
In previous studies, we purified the DUB-module of the Drosophila SAGA complex and showed that a number of zinc proteins interact with it, including Aef1 and CG10543. In this work, we conducted a genome-wide study of the Aef1 and CG10543 proteins and showed that they are localized predominantly on the promoters of active genes. The binding sites of these proteins co-localize with the SAGA and dSWI/SNF chromatin modification and remodeling complexes, as well as with the ORC replication complex.
View Article and Find Full Text PDFKi-67 and CDK1 Control the Dynamic Association of Nuclear Lipids with Mitotic Chromosomes.
J Lipid Res
December 2024
Institute of Molecular Biology, Academia Sinica, Taipei, 11529, Taiwan. Electronic address:
Nuclear lipids play roles in regulatory processes such as signaling, transcriptional regulation, and DNA repair. In this report, we demonstrate that nuclear lipids may contribute to Ki-67-regulated chromosome integrity during mitosis. In COS-7 cells, nuclear lipids are enriched at the perichromosomal layer and excluded from intrachromosomal regions during early mitosis, but are then detected in intrachromosomal regions during late mitosis, as revealed by TT-ExM, an improved expansion microscopy technique that enables high-sensitivity, super-resolution imaging of proteins, lipids, and nuclear DNA.
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