The histone chaperone SPT2 regulates chromatin structure and function in Metazoa

Page view(s)
141
Checked on Jul 19, 2024
The histone chaperone SPT2 regulates chromatin structure and function in Metazoa
Title:
The histone chaperone SPT2 regulates chromatin structure and function in Metazoa
Journal Title:
Nature Structural & Molecular Biology
Publication Date:
18 January 2024
Citation:
Saredi, G., Carelli, F. N., Rolland, S. G. M., Furlan, G., Piquet, S., Appert, A., Sanchez-Pulido, L., Price, J. L., Alcon, P., Lampersberger, L., Déclais, A.-C., Ramakrishna, N. B., Toth, R., Macartney, T., Alabert, C., Ponting, C. P., Polo, S. E., Miska, E. A., Gartner, A., … Rouse, J. (2024). The histone chaperone SPT2 regulates chromatin structure and function in Metazoa. Nature Structural & Molecular Biology. https://doi.org/10.1038/s41594-023-01204-3
Abstract:
AbstractHistone chaperones control nucleosome density and chromatin structure. In yeast, the H3–H4 chaperone Spt2 controls histone deposition at active genes but its roles in metazoan chromatin structure and organismal physiology are not known. Here we identify the Caenorhabditis elegans ortholog of SPT2 (CeSPT-2) and show that its ability to bind histones H3–H4 is important for germline development and transgenerational epigenetic gene silencing, and that spt-2 null mutants display signatures of a global stress response. Genome-wide profiling showed that CeSPT-2 binds to a range of highly expressed genes, and we find that spt-2 mutants have increased chromatin accessibility at a subset of these loci. We also show that SPT2 influences chromatin structure and controls the levels of soluble and chromatin-bound H3.3 in human cells. Our work reveals roles for SPT2 in controlling chromatin structure and function in Metazoa.
License type:
Attribution 4.0 International (CC BY 4.0)
Funding Info:
This work was supported by the Medical Research Council (grant number MC_UU_00018/5) and the pharmaceutical companies supporting the Division of Signal Transduction Therapy Unit (Boehinger‐Ingelheim, GlaxoSmithKline and Merck KGaA) (J.R.); the Wellcome Trust (grant number 217170) and the MRC (grant number MR/S021620/1) (J.A.); the Korean Institute for Basic Science (grant number IBS-R022-A2-2023) (A.G. and S.G.M.R.); Cancer Research UK (grant number C13474/A27826) and the Wellcome Trust (grant number 219475/Z/19/Z) (E.A.M.); the European Research Council (grant number ERC-2018-CoG-818625) (S.E.P.); the Medical Research Council (grant number MC_UU_00007/15) (C.P.P.); the European Research Council (ERC-2016-StG-715127) (C.A.); the Medical Research Council (grant number MC_U105192715 to L. Passmore). G.S. was supported by an EMBO Long-Term Fellowship (ALTF 951-2018) and a SULSA ECR Development Fund; this project has received funding from the European Union’s Horizon 2020 research and innovation programme under the Marie Skłodowska-Curie grant agreement no. 845448 (G.S.). G.F. was supported by an EMBO Long-Term Fellowship (ALTF 1132-2018). P.A. was supported by an EMBO Long-Term Fellowship (ALTF 692–2018).
Description:
ISSN:
1545-9985
1545-9993