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Dear Colleagues,

Chromatin is a highly dynamic structure that is extensively and reversibly modified by various factors, including enzymes running DNA transactions, chromatin remodelers, histone and DNA modifications, and other factors to ensure the development and survival of a cell. Chromatin remodelers participate in nearly every DNA transaction in the cell nuclei, including DNA replication, transcription, and repair. Chromatin remodelers include histone chaperones, histone-modifying enzymes and ATP-dependent chromatin remodeling complexes. Chromatin remodelers facilitate various transitions in chromatin structure, including nucleosome sliding, assembly, and disassembly, changes in the nucleosome structure, and histone variant exchange. They also participate in histone transport, deposition, eviction, and storage. However, their mechanisms of action, interacting partners, and their roles in the regulation of cellular metabolism and development of human diseases remain to be further established.

We invite researchers to present their studies of the mechanisms of action and regulation of histone chaperones and chromatin remodelers and their complexes with proteins and other biological molecules, and to discuss their data and opinions on the pages of the International Journal of Molecular Sciences.

Prof. Dr. Vasily M. Studitsky
Guest Editor

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Keywords

histone chaperones
chromatin remodelers
chromatin
mechanism
structure
regulation

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16 pages, 1840 KiB

Open AccessArticle

Lack of the Histone Deacetylase SIRT1 Leads to Protection against Endoplasmic Reticulum Stress through the Upregulation of Heat Shock Proteins

by Jessica Latorre, Nuria de Vera, Tomàs Santalucía, Rafel Balada, Anna Marazuela-Duque, Alejandro Vaquero, Anna M. Planas and Valérie Petegnief

Int. J. Mol. Sci. 2024, 25(5), 2856; https://doi.org/10.3390/ijms25052856 - 01 Mar 2024

Viewed by 916

Abstract

Histone deacetylase SIRT1 represses gene expression through the deacetylation of histones and transcription factors and is involved in the protective cell response to stress and aging. However, upon endoplasmic reticulum (ER) stress, SIRT1 impairs the IRE1α branch of the unfolded protein response (UPR) through the inhibition of the transcriptional activity of XBP-1 and SIRT1 deficiency is beneficial under these conditions. We hypothesized that SIRT1 deficiency may unlock the blockade of transcription factors unrelated to the UPR promoting the synthesis of chaperones and improving the stability of immature proteins or triggering the clearance of unfolded proteins. SIRT1+/+ and SIRT1−/− fibroblasts were exposed to the ER stress inducer tunicamycin and cell survival and expression of heat shock proteins were analyzed 24 h after the treatment. We observed that SIRT1 loss significantly reduced cell sensitivity to ER stress and showed that SIRT1−/− but not SIRT1+/+ cells constitutively expressed high levels of phospho-STAT3 and heat shock proteins. Hsp70 silencing in SIRT1−/− cells abolished the resistance to ER stress. Furthermore, accumulation of ubiquitinated proteins was lower in SIRT1−/− than in SIRT1+/+ cells. Our data showed that SIRT1 deficiency enabled chaperones upregulation and boosted the proteasome activity, two processes that are beneficial for coping with ER stress. Full article

(This article belongs to the Special Issue Histone Chaperones and Chromatin Remodelers: Mechanisms of Action and Regulation)

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Histone Chaperones and Chromatin Remodelers: Mechanisms of Action and Regulation

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