Flexibility in crosstalk between H2B ubiquitination and H3 methylation in vivo (Corrigendum)

Hanneke Vlaming; Tibor van Welsem; Erik L de Graaf; David Ontoso; A F Maarten Altelaar; Pedro A San-Segundo; Albert J R Heck; Fred van Leeuwen

doi:10.15252/embr.201471110

Flexibility in crosstalk between H2B ubiquitination and H3 methylation in vivo (Corrigendum)

Hanneke Vlaming, Tibor van Welsem, Erik L de Graaf, David Ontoso, A F Maarten Altelaar, Pedro A San-Segundo, Albert J R Heck, Fred van Leeuwen

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

Histone H2B ubiquitination is a dynamic modification that promotes methylation of histone H3K79 and H3K4. This crosstalk is important for the DNA damage response and has been implicated in cancer. Here, we show that in engineered yeast strains, ubiquitins tethered to every nucleosome promote H3K79 and H3K4 methylation from a proximal as well as a more distal site, but only if in a correct orientation. This plasticity indicates that the exact location of the attachment site, the native ubiquitin-lysine linkage and ubiquitination cycles are not critical for trans-histone crosstalk in vivo. The flexibility in crosstalk also indicates that other ubiquitination events may promote H3 methylation.

Original language	English
Pages (from-to)	1220-1221
Number of pages	2
Journal	EMBO Reports
Volume	15
Issue number	11
DOIs	https://doi.org/10.15252/embr.201471110
Publication status	Published - 2014

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abstract = "Histone H2B ubiquitination is a dynamic modification that promotes methylation of histone H3K79 and H3K4. This crosstalk is important for the DNA damage response and has been implicated in cancer. Here, we show that in engineered yeast strains, ubiquitins tethered to every nucleosome promote H3K79 and H3K4 methylation from a proximal as well as a more distal site, but only if in a correct orientation. This plasticity indicates that the exact location of the attachment site, the native ubiquitin-lysine linkage and ubiquitination cycles are not critical for trans-histone crosstalk in vivo. The flexibility in crosstalk also indicates that other ubiquitination events may promote H3 methylation.",

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T1 - Flexibility in crosstalk between H2B ubiquitination and H3 methylation in vivo (Corrigendum)

AU - Vlaming, Hanneke

AU - van Welsem, Tibor

AU - de Graaf, Erik L

AU - Ontoso, David

AU - Altelaar, A F Maarten

AU - San-Segundo, Pedro A

AU - Heck, Albert J R

AU - van Leeuwen, Fred

PY - 2014

Y1 - 2014

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AB - Histone H2B ubiquitination is a dynamic modification that promotes methylation of histone H3K79 and H3K4. This crosstalk is important for the DNA damage response and has been implicated in cancer. Here, we show that in engineered yeast strains, ubiquitins tethered to every nucleosome promote H3K79 and H3K4 methylation from a proximal as well as a more distal site, but only if in a correct orientation. This plasticity indicates that the exact location of the attachment site, the native ubiquitin-lysine linkage and ubiquitination cycles are not critical for trans-histone crosstalk in vivo. The flexibility in crosstalk also indicates that other ubiquitination events may promote H3 methylation.

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DO - 10.15252/embr.201471110

M3 - Article

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JO - EMBO Reports

JF - EMBO Reports

IS - 11

ER -

Flexibility in crosstalk between H2B ubiquitination and H3 methylation in vivo (Corrigendum)

Abstract

Bibliographical note

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