Dot1 regulates nucleosome dynamics by its inherent histone chaperone activity in yeast

Dot1 (disruptor of telomeric silencing-1, DOT1L in humans) is the only known enzyme responsible for histone H3 lysine 79 methylation (H3K79me) and is evolutionarily conserved in most eukaryotes. Yeast Dot1p lacks a SET domain and does not methylate free histones and thus may have different actions w...

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Published inNature communications Vol. 9; no. 1; pp. 240 - 14
Main Authors Lee, Soyun, Oh, Seunghee, Jeong, Kwiwan, Jo, Hyelim, Choi, Yoonjung, Seo, Hogyu David, Kim, Minhoo, Choe, Joonho, Kwon, Chang Seob, Lee, Daeyoup
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 16.01.2018
Nature Publishing Group
Nature Portfolio
Subjects
45/15
45/91
631/337/100/101
631/337/100/1701
82/29
Chromatin
Chromatin remodeling
Eukaryotes
Histone H3
Histones
Humanities and Social Sciences
Lysine
Methylation
multidisciplinary
Nucleosomes
Science
Science (multidisciplinary)
Transcription
Yeast
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Abstract Dot1 (disruptor of telomeric silencing-1, DOT1L in humans) is the only known enzyme responsible for histone H3 lysine 79 methylation (H3K79me) and is evolutionarily conserved in most eukaryotes. Yeast Dot1p lacks a SET domain and does not methylate free histones and thus may have different actions with respect to other histone methyltransferases. Here we show that Dot1p displays histone chaperone activity and regulates nucleosome dynamics via histone exchange in yeast. We show that a methylation-independent function of Dot1p is required for the cryptic transcription within transcribed regions seen following disruption of the Set2–Rpd3S pathway. Dot1p can assemble core histones to nucleosomes and facilitate ATP-dependent chromatin-remodeling activity through its nucleosome-binding domain, in vitro. Global analysis indicates that Dot1p appears to be particularly important for histone exchange and chromatin accessibility on the transcribed regions of long-length genes. Our findings collectively suggest that Dot1p-mediated histone chaperone activity controls nucleosome dynamics in transcribed regions. Dot1 is an evolutionarily conserved enzyme, responsible for histone H3K79 methylation in most eukaryotes. Here authors show that, in yeast, Dot1p has histone chaperone activity and regulates nucleosome dynamics via histone exchange in transcribed regions.
AbstractList Dot1 (disruptor of telomeric silencing-1, DOT1L in humans) is the only known enzyme responsible for histone H3 lysine 79 methylation (H3K79me) and is evolutionarily conserved in most eukaryotes. Yeast Dot1p lacks a SET domain and does not methylate free histones and thus may have different actions with respect to other histone methyltransferases. Here we show that Dot1p displays histone chaperone activity and regulates nucleosome dynamics via histone exchange in yeast. We show that a methylation-independent function of Dot1p is required for the cryptic transcription within transcribed regions seen following disruption of the Set2–Rpd3S pathway. Dot1p can assemble core histones to nucleosomes and facilitate ATP-dependent chromatin-remodeling activity through its nucleosome-binding domain, in vitro. Global analysis indicates that Dot1p appears to be particularly important for histone exchange and chromatin accessibility on the transcribed regions of long-length genes. Our findings collectively suggest that Dot1p-mediated histone chaperone activity controls nucleosome dynamics in transcribed regions.
Abstract Dot1 (disruptor of telomeric silencing-1, DOT1L in humans) is the only known enzyme responsible for histone H3 lysine 79 methylation (H3K79me) and is evolutionarily conserved in most eukaryotes. Yeast Dot1p lacks a SET domain and does not methylate free histones and thus may have different actions with respect to other histone methyltransferases. Here we show that Dot1p displays histone chaperone activity and regulates nucleosome dynamics via histone exchange in yeast. We show that a methylation-independent function of Dot1p is required for the cryptic transcription within transcribed regions seen following disruption of the Set2–Rpd3S pathway. Dot1p can assemble core histones to nucleosomes and facilitate ATP-dependent chromatin-remodeling activity through its nucleosome-binding domain, in vitro. Global analysis indicates that Dot1p appears to be particularly important for histone exchange and chromatin accessibility on the transcribed regions of long-length genes. Our findings collectively suggest that Dot1p-mediated histone chaperone activity controls nucleosome dynamics in transcribed regions.
Dot1 (disruptor of telomeric silencing-1, DOT1L in humans) is the only known enzyme responsible for histone H3 lysine 79 methylation (H3K79me) and is evolutionarily conserved in most eukaryotes. Yeast Dot1p lacks a SET domain and does not methylate free histones and thus may have different actions with respect to other histone methyltransferases. Here we show that Dot1p displays histone chaperone activity and regulates nucleosome dynamics via histone exchange in yeast. We show that a methylation-independent function of Dot1p is required for the cryptic transcription within transcribed regions seen following disruption of the Set2–Rpd3S pathway. Dot1p can assemble core histones to nucleosomes and facilitate ATP-dependent chromatin-remodeling activity through its nucleosome-binding domain, in vitro. Global analysis indicates that Dot1p appears to be particularly important for histone exchange and chromatin accessibility on the transcribed regions of long-length genes. Our findings collectively suggest that Dot1p-mediated histone chaperone activity controls nucleosome dynamics in transcribed regions. Dot1 is an evolutionarily conserved enzyme, responsible for histone H3K79 methylation in most eukaryotes. Here authors show that, in yeast, Dot1p has histone chaperone activity and regulates nucleosome dynamics via histone exchange in transcribed regions.
Dot1 is an evolutionarily conserved enzyme, responsible for histone H3K79 methylation in most eukaryotes. Here authors show that, in yeast, Dot1p has histone chaperone activity and regulates nucleosome dynamics via histone exchange in transcribed regions.
ArticleNumber 240
Author Lee, Soyun
Jo, Hyelim
Choi, Yoonjung
Jeong, Kwiwan
Lee, Daeyoup
Kim, Minhoo
Choe, Joonho
Oh, Seunghee
Kwon, Chang Seob
Seo, Hogyu David
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SSID ssj0000391844
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Snippet Dot1 (disruptor of telomeric silencing-1, DOT1L in humans) is the only known enzyme responsible for histone H3 lysine 79 methylation (H3K79me) and is...
Abstract Dot1 (disruptor of telomeric silencing-1, DOT1L in humans) is the only known enzyme responsible for histone H3 lysine 79 methylation (H3K79me) and is...
Dot1 is an evolutionarily conserved enzyme, responsible for histone H3K79 methylation in most eukaryotes. Here authors show that, in yeast, Dot1p has histone...
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pubmedcentral
proquest
crossref
pubmed
springer
SourceType Open Website
Open Access Repository
Aggregation Database
Index Database
Publisher
StartPage 240
SubjectTerms 45/15
45/91
631/337/100/101
631/337/100/1701
82/29
Chromatin
Chromatin remodeling
Eukaryotes
Histone H3
Histones
Humanities and Social Sciences
Lysine
Methylation
multidisciplinary
Nucleosomes
Science
Science (multidisciplinary)
Transcription
Yeast
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Title Dot1 regulates nucleosome dynamics by its inherent histone chaperone activity in yeast
URI https://link.springer.com/article/10.1038/s41467-017-02759-8
https://www.ncbi.nlm.nih.gov/pubmed/29339748
https://www.proquest.com/docview/1988111787
https://search.proquest.com/docview/1989576568
https://pubmed.ncbi.nlm.nih.gov/PMC5770421
https://doaj.org/article/212d26a446b048c1a4d3006d7bb52b5b
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