2013
DOI: 10.1038/ncomms3969
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Binding of PHF1 Tudor to H3K36me3 enhances nucleosome accessibility

Abstract: The Tudor domain of human PHF1 recognizes trimethylated lysine 36 of histone H3 (H3K36me3). This interaction modulates methyltransferase activity of the PRC2 complex and plays a role in retention of PHF1 at the DNA damage sites. We have previously determined the structural basis for the association of Tudor with a methylated histone peptide. Here we detail the molecular mechanism of binding of the Tudor domain to the H3KC36me3-nucleosome core particle (H3KC36me3-NCP). Using a combination of TROSY NMR and FRET … Show more

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Cited by 82 publications
(114 citation statements)
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“…Similar phenomena were observed for other Royal superfamily modules; for example, compared with the chromodomain alone, the preformed complex of the MSL3 [29] or RBBP1 [28] chromodomain with DNA displayed enhanced binding ability to H4K20me1 or H4K20me3 peptides, respectively. In addition, the Tudor domain of PHF1 concomitantly interacts with both H3K36me3 and DNA of the H3K36me3-modified nucleosome core particle with in- creased binding ability [30]. In the case of the PWWP domain, binding affinity towards either histone peptide or DNA oligonucleotide is very weak, but it exhibits significantly enhanced binding affinity to methylated nucleosomes.…”
Section: Reviewmentioning
confidence: 98%
“…Similar phenomena were observed for other Royal superfamily modules; for example, compared with the chromodomain alone, the preformed complex of the MSL3 [29] or RBBP1 [28] chromodomain with DNA displayed enhanced binding ability to H4K20me1 or H4K20me3 peptides, respectively. In addition, the Tudor domain of PHF1 concomitantly interacts with both H3K36me3 and DNA of the H3K36me3-modified nucleosome core particle with in- creased binding ability [30]. In the case of the PWWP domain, binding affinity towards either histone peptide or DNA oligonucleotide is very weak, but it exhibits significantly enhanced binding affinity to methylated nucleosomes.…”
Section: Reviewmentioning
confidence: 98%
“…It adds weight to the expectation that we will also find physical coupling of the opposite combination of activities, histone deactivation and repression, which are effectively coordinated in many systems (3,4,6,45). Identification of the H3K36me3 demethylase at FLC will allow its physical association with PRC2 to be investigated.…”
Section: Elf6 and Jumonji Domain-containing Protein 13 Are Partiallymentioning
confidence: 99%
“…Importantly, the Ioc4–H3K36me3 interaction cannot be detected when tested with methylated peptides alone [50,51], and a similar result is observed for the association of the Pdp1 PWWP domain with H4K20me3-nucleosomes [52]. A recent study of the PHF1 Tudor domain also reveals multivalent contacts with H3K36me3 and nucleosomal DNA [53]. In contrast to the PWWP domain this association is far more driven by interaction with the methylated mark itself [53].…”
Section: Contacts Outside the Methylated Histone Tailmentioning
confidence: 83%