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2 results on '"S, Curtet"'

1. Metabolically controlled histone H4K5 acylation/acetylation ratio drives BRD4 genomic distribution.

Author

Gao M, Wang J, Rousseaux S, Tan M, Pan L, Peng L, Wang S, Xu W, Ren J, Liu Y, Spinck M, Barral S, Wang T, Chuffart F, Bourova-Flin E, Puthier D, Curtet S, Bargier L, Cheng Z, Neumann H, Li J, Zhao Y, Mi JQ, and Khochbin S

Subjects
Acetylation, Acylation, Cell Line, Tumor, Chromatin metabolism, Fatty Acids biosynthesis, Female, Gene Expression Regulation, Leukemic, Humans, Mitochondria metabolism, Mitochondrial Proteins metabolism, Models, Biological, Oxidation-Reduction, Precursor Cell Lymphoblastic Leukemia-Lymphoma genetics, Precursor Cell Lymphoblastic Leukemia-Lymphoma pathology, Protein Binding, Protein Processing, Post-Translational, RNA-Binding Proteins metabolism, Cell Cycle Proteins metabolism, Genome, Human, Histones metabolism, Lysine metabolism, Transcription Factors metabolism
Abstract

In addition to acetylation, histones are modified by a series of competing longer-chain acylations. Most of these acylation marks are enriched and co-exist with acetylation on active gene regulatory elements. Their seemingly redundant functions hinder our understanding of histone acylations' specific roles. Here, by using an acute lymphoblastic leukemia (ALL) cell model and blasts from individuals with B-precusor ALL (B-ALL), we demonstrate a role of mitochondrial activity in controlling the histone acylation/acetylation ratio, especially at histone H4 lysine 5 (H4K5). An increase in the ratio of non-acetyl acylations (crotonylation or butyrylation) over acetylation on H4K5 weakens bromodomain containing protein 4 (BRD4) bromodomain-dependent chromatin interaction and enhances BRD4 nuclear mobility and availability for binding transcription start site regions of active genes. Our data suggest that the metabolism-driven control of the histone acetylation/longer-chain acylation(s) ratio could be a common mechanism regulating the bromodomain factors' functional genomic distribution., Competing Interests: Declaration of interests Y.Z. is a founder, board member, advisor to, and inventor on patents licensed to PTM Biolabs Inc. (Hangzhou, China and Chicago, IL) and Maponos Therapeutics Inc. (Chicago, IL). Z.C. is an employee and equity holder of PTM BioLabs Inc., (Copyright © 2021 The Author(s). Published by Elsevier Inc. All rights reserved.)

Published
2021
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2. Exogenous Expression of Human Protamine 1 (hPrm1) Remodels Fibroblast Nuclei into Spermatid-like Structures.

Author

Iuso D, Czernik M, Toschi P, Fidanza A, Zacchini F, Feil R, Curtet S, Buchou T, Shiota H, Khochbin S, Ptak GE, and Loi P

Subjects
Acetylation, Animals, Cell Nucleus chemistry, Cells, Cultured, Chromatin metabolism, DNA chemistry, DNA metabolism, Female, Fibroblasts cytology, Fibroblasts metabolism, Histones metabolism, Humans, Male, Methylation, Microscopy, Electron, Transmission, Oocytes metabolism, Protamines genetics, Sheep, Spermatids chemistry, Spermatids metabolism, Cell Nucleus metabolism, Chromatin Assembly and Disassembly, Protamines metabolism
Abstract

Protamines confer a compact structure to the genome of male gametes. Here, we find that somatic cells can be remodeled by transient expression of protamine 1 (Prm1). Ectopically expressed Prm1 forms scattered foci in the nuclei of fibroblasts, which coalescence into spermatid-like structures, concomitant with a loss of histones and a reprogramming barrier, H3 lysine 9 methylation. Protaminized nuclei injected into enucleated oocytes efficiently underwent protamine to maternal histone TH2B exchange and developed into normal blastocyst stage embryos in vitro. Altogether, our findings present a model to study male-specific chromatin remodeling, which can be exploited for the improvement of somatic cell nuclear transfer., (Copyright © 2015 The Authors. Published by Elsevier Inc. All rights reserved.)

Published
2015
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