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

By A. Vaquero, Michael B Scher, Donghoon Lee, H. Erdjument‐Bromage, Paul Tempst, D. Reinberg. Molecules and Cells, 2004

934 citations recorded by the source corpus.

Subfields: Geriatrics and Gerontology, Oncology, Plant Science

View Paper: https://www.semanticscholar.org/paper/6d07b6170a99e1ec29fe86fa4e2341a1733b4ba6

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Geriatrics and Gerontology

1. L. Guarente
2. D. Sinclair
3. E. Verdin
4. E. Seto
5. R. Mostoslavsky
6. W. Gu
7. F. Alt
8. A. Kazantsev

In Oncology

1. E. Seto
2. W. Gu
3. D. Sinclair
4. E. Verdin
5. F. Alt
6. S. Baylin
7. M. Hottiger
8. L. Guarente

In Plant Science

1. M. Fraga
2. Manel Esteller
3. R. Margueron
4. R. Feil
5. D. Reinberg

Citations in the corpus

• Therapeutic application of histone deacetylase inhibitors for central nervous system disorders (2008, background): “Removal of acetyl groups from specific lysine residues may be determined by specific protein complexes, such as B-cell CLL/lymphoma 11A (zinc finger protein) (BCL11A) and p300/CBP-associated factor (pCAF)–myogenic differentiation 1 (MYOD1), of which SIRT1 is a componen”
• Regulation of SIRT1 and Its Roles in Inflammation (2022, background): “March 2022 | Volume 13 | Article 831168 deacetylation of promoter-associated H3K9 and H4K16, and subsequent suppression of transcription have been particularly well characterized (15–17).”
• The role of histone deacetylases (HDACs) in human cancer (2007, background): “In particular, the most prominent family member, SIRT1, regulates histone acetylation levels (mainly K16-H4 and K9-H3 positions) (Vaquero et al., 2004; Pruitt et al., 2006), and the acetylation of transcription factors such as p53 (Vaziri et al., 2001), p300 histone acethyltransferase (Bouras et…”
• Genomic instability and aging-like phenotype in the absence of mammalian SIRT6. (2006, positive): “In addition, SIRT1, like Sir2, has been shown to modify chromatin and silence transcription of integrated reporter genes via histone deace-tylation (Vaquero et al., 2004).”
• DNA damage-induced alterations in chromatin contribute to genomic integrity and age-related changes in gene expression (2008, positive): “Cell lysates were sonicated (Branson sonifier) and incubated overnight with rabbit a-Sir2a (Upstate), a-NBS1 (Novus), a-RAD51 (Calbiochem), or a-H1AcK26 (Vaquero et al., 2004).”
• Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses. (2005, background): “Meanwhile, the recruitment of SIRT1 also induces deacetylation of linker histone H1 and further promotes formation of facultative heterochromatin (Vaquero et al., 2004).”
• Sirtuins: critical regulators at the crossroads between cancer and aging (2007, background): “SIRT1 also recruits and deacetylates linker histone H1 on K26 to establish heterochromatin (Vaquero et al., 2004).”
• A dual role of linker histone H1.4 Lys 34 acetylation in transcriptional activation. (2012, background): “The linker histone H1 has been shown to be also acetylated in vivo (Garcia et al. 2004; Vaquero et al. 2004; Wisniewski et al. 2007), but this modification has not been functionally characterized.”
• Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II. (2006, methodology): “In Vivo ChIP ChIP assays were performed as described (Vaquero et al., 2004), and primers for the RARb2 promoter and downstream coding region (exon 3) have been described (Lefebvre et al.”
• Ezh1 and Ezh2 maintain repressive chromatin through different mechanisms (2008, methodology): “(Figure 2), we next tested if Ezh1 can recruit the core PRC2 components using a cell model, derived from 293 T-Rex, in which a Gal4 fusion protein, Gal4-Ezh1 in this case, can be induced for expression and artificially tethered to an integrated luciferase reporter containing Gal4 response elements (”
• The world of protein acetylation. (2016, background): “KDACs are divided into two distinct groups with different catalytic mechanisms: Zn2+-dependent HDACs (HDAC1–11) and NAD+-dependent sirtuins (SIRT1–7) [14].”
• Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. (2005, background): “Vaquero et al. (2004) suggested that SIRT1 could promote the formation of facultative heterochromatin at an experimentally recruited euchromatic site through deacetylation of the H4 lysine 16.”
• Epigenetics and the environment: emerging patterns and implications (2012, background): “In addition to roles in the deacetylation of various transcription factors that are involved in the regulation of glucose and fatty acid metabolic pathways, mammalian sirtuins target acetylated histones, such as H4K16a”