Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain

By Andrew J. Bannister, P. Zegerman, J. Partridge, E. Miska, Jean O. Thomas, Robin C. Allshire, Tony Kouzarides. Nature, 2001

3,042 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/3730863586b1c9cd64a8b8c433c3a3e6d1c9aa99

How researchers see this paper

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

In Molecular Biology

Citations in the corpus

Regulation of nucleosome dynamics by histone modifications (2013, neutral): “92).”
Vernalization requires epigenetic silencing of FLC by histone methylation (2004, background): “Methylated K9 of histone H3 triggers the binding of HETEROCHROMATIN PROTEIN 1, leading to heterochromatin formation and silencin”
Histone Tails and the H3 αN Helix Regulate Nucleosome Mobility and Stability (2007, background): “These include the chromodomains of HP1 and PRC1, which interact specifically with histones methylated at histone H3 lysine 9 and 27, respectively ( 4 , 14, 27), and bromodomain-containing proteins which bind acetylated histone tails (26, 42).”
Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails. (2001, background): “Consistent with the finding that the localization of Swi6p to heterochromatin requires the HMT activity of Clr4 in S. pombe (Bannister et al. 2001; Nakayama et al. 2001), HP1 localization was found to be dispersed in Suv39h1 -null PMEFs.”
Erasing the methyl mark: histone demethylases at the center of cellular differentiation and disease. (2008, background): “2005), the H3K9me3/me2 mark has generally been associated with transcriptional repression and formation of heterochromatin involving the recruitment of factors such as the HP1 proteins (Bannister et al. 2001; Lachner et al. 2001).”
Histone H3 methylation by Set2 directs deacetylation of coding regions by Rpd3S to suppress spurious intragenic transcription. (2005, background): “Similar to HP1, Drosophila Polycomb and yeast Chd1, Eaf3 contains a chromodomain, which could direct this protein and Rpd3S to coding regions by binding to methylated histones (Bannister et al., 2001; Lachner et al., 2001; Pray-Grant et al., 2005).”
Histone Marks in the 'Driver's Seat': Functional Roles in Steering the Transcription Cycle. (2017, background): “In addition, the histone methyltransferase G9a is recruited, which deposits H3K9me2 at these sites and in turn recruits the reader protein heterochromatin protein 1 γ (HP1γ) [89].”