Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin.

Vaquero, Alejandro; Scher, Michael; Lee, Donghoon; Erdjument-Bromage, Hediye; Tempst, Paul; Reinberg, Danny

doi:10.1016/j.molcel.2004.08.031

Cited by 916Genomics and Chromatin DynamicsSirtuins and Resveratrol in MedicineNuclear Structure and Function

Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin.

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Vaquero, Alejandro, Scher, Michael, Lee, Donghoon, Erdjument-Bromage, Hediye, Tempst, Paul, Reinberg, Danny·2004·Molecular Cell

DOI 10.1016/j.molcel.2004.08.031

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Abstract

We characterized human SirT1, one of the human homologs of the budding yeast Sir2p, an NAD+-dependent histone deacetylase involved in establishing repressive chromatin and increased life span. SirT1 deacetylates histone polypeptides with a preference for histone H4 lysine 16 (H4-K16Ac) and H3 lysine 9 (H3-K9Ac) in vitro. RNAi-mediated decreased expression of SirT1 in human cells causes hyperacetylation of H4-K16 and H3-K9 in vivo. SirT1 interacts with and deacetylates histone H1 at lysine 26. Using an inducible system directing expression of SirT1 fused to the Gal4-DNA binding domain and a Gal4-reporter integrated in euchromatin, Gal4-SirT1 expression resulted in the deacetylation of H4-K16 and H3-K9, recruitment of H1 within the promoter vicinity, drastically reduced reporter expression, and loss of H3-K79 methylation, a mark restricting silenced chromatin. We propose a model for SirT1-mediated heterochromatin formation that includes deacetylation of histone tails, recruitment and deacetylation of histone H1, and spreading of hypomethylated H3-K79 with resultant silencing.

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SIRT1 deacetylase modulates SUV39H1 by deacetylating SUV39H1 K266 and by deacetylating H3K9Ac to allow SUV39H1 methylation.
“SUV39H1 function is also modulated by the SIRT1 deacetylase, which regulates SUV39H1 in two separate ways: (1) by deacetylating SUV39H1 lysine residue 266 (K266) (Vaquero et al., 2007) and (2) by deacetylating lysine 9 of histone H3 (H3K9Ac) to allow SUV39H1 methylation (Vaquero et al., 2004, 2007).”
From USP7 Is a Master Regulator of Genome Stability (2020) · cites this paper as Vaquero et al., 2004
SIRT1, like Sir2, has recently been shown to directly modify chromatin and silence transcription.
“Additionally, SIRT1, like Sir2, has recently been shown to directly modify chromatin and silence transcription (Vaquero et al., 2004”
From DNA Repair, Genome Stability, and Aging (2005) · cites this paper as Vaquero et al., 2004
Evidence from cell culture models indicates that Sirt1 is involved in heterochromatin formation and might be particularly important in the silencing of certain tumour suppressors.
“evidence from cell culture models indicates that Sirt1 is involved in heterochromatin formation and might be particularly important in the silencing of certain tumour suppressors 45, 46”
From The common biology of cancer and ageing (2007) · cites this paper as [45]

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Authors: Vaquero, A., Scher, M., Lee, D., Erdjument-Bromage, H., Tempst, P., & Reinberg, D.
Affiliations: Howard Hughes Medical Institute (US)
Memorial Sloan Kettering Cancer Center (US)
Corresponding author: Reinberg, Danny
ORCID: Vaquero, Alejandro
Lee, Donghoon
Tempst, Paul
Reinberg, Danny
Venue: Molecular Cell
Publisher: Elsevier BV
Published: 2004-10
Volume: 16
Issue: 1
Pages: 93-105
ISSN: 1097-2765 (ISSN-L)
DOI: 10.1016/j.molcel.2004.08.031
OpenAlex: W2094807579
Cited by: 916
References: 74
Citations by year: 2026: 22 · 2025: 31 · 2024: 46 · 2023: 35 · 2022: 40 · 2021: 45 · 2020: 40 · 2019: 28 · 2018: 44 · 2017: 41 · 2016: 43 · 2015: 55 · 2014: 48 · 2013: 62 · 2012: 56
FWCI: 11.96
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 3211 d)
doi.org/10.15223/policy-017 (stm-asf)
doi.org/10.15223/policy-037 (stm-asf)
doi.org/10.15223/policy-012 (stm-asf)
doi.org/10.15223/policy-029 (stm-asf)
doi.org/10.15223/policy-004 (stm-asf)
Locations: Molecular Cell (publishedVersion)
PubMed (publishedVersion)
Funders: National Cancer Institute (P30-CA-08748, P30CA008748)
National Institute of General Medical Sciences (GM37120, T32 GM 08360, T32GM008360)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
Keywords: SIRT1, histone deacetylase, histone H1, facultative heterochromatin, heterochromatin formation, H4K16ac, histone H3 lysine 9 acetylation, chromatin silencing, NAD+-dependent deacetylation, lifespan
MeSH terms: Acetylation, Cell Nucleus, Gene Expression Regulation, Heterochromatin, Histone Deacetylases, Histones, Humans, NAD, Promoter Regions, Genetic, Sirtuins, Sirtuin 1

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Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin.

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