The many faces of histone H3K79 methylation

Zeenat Farooq; Shahid Banday; Tej K. Pandita; Mohammad Altaf

doi:10.1016/j.mrrev.2016.03.005

The many faces of histone H3K79 methylation

Zeenat Farooq, Shahid Banday, Tej K. Pandita, Mohammad Altaf

Research output: Contribution to journal › Review article › peer-review

105 Scopus citations

Abstract

Dot1/DOT1L (disruptor of telomeric silencing-1) is an evolutionarily conserved histone methyltransferase that methylates lysine 79 located within the globular domain of histone H3. Dot1 was initially identified by a genetic screen as a disruptor of telomeric silencing in Saccharomyces cerevisiae; further, it is the only known non-SET domain containing histone methyltransferase. Methylation of H3K79 is involved in the regulation of telomeric silencing, cellular development, cell-cycle checkpoint, DNA repair, and regulation of transcription. hDot1L-mediated H3K79 methylation appears to have a crucial role in transformation as well as disease progression in leukemias involving several oncogenic fusion proteins. This review summarizes the multiple functions of Dot1/hDOT1L in a range of cellular processes.

Original language	English (US)
Pages (from-to)	46-52
Number of pages	7
Journal	Mutation Research - Reviews in Mutation Research
Volume	768
DOIs	https://doi.org/10.1016/j.mrrev.2016.03.005
State	Published - Apr 1 2016

Keywords

Chromatin
DNA repair
Histone methylation

ASJC Scopus subject areas

Genetics
Health, Toxicology and Mutagenesis

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10.1016/j.mrrev.2016.03.005

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title = "The many faces of histone H3K79 methylation",

abstract = "Dot1/DOT1L (disruptor of telomeric silencing-1) is an evolutionarily conserved histone methyltransferase that methylates lysine 79 located within the globular domain of histone H3. Dot1 was initially identified by a genetic screen as a disruptor of telomeric silencing in Saccharomyces cerevisiae; further, it is the only known non-SET domain containing histone methyltransferase. Methylation of H3K79 is involved in the regulation of telomeric silencing, cellular development, cell-cycle checkpoint, DNA repair, and regulation of transcription. hDot1L-mediated H3K79 methylation appears to have a crucial role in transformation as well as disease progression in leukemias involving several oncogenic fusion proteins. This review summarizes the multiple functions of Dot1/hDOT1L in a range of cellular processes.",

keywords = "Chromatin, DNA repair, Histone methylation",

author = "Zeenat Farooq and Shahid Banday and Pandita, {Tej K.} and Mohammad Altaf",

note = "Funding Information: The authors thank the members of Bhat Laboratory and Dr. Ajazul Hamid Wani for their fruitful discussions. The work is supported by the Ramanujan Fellowship grant from DST, India , and a UGC start-up grant from the University Grants Commission, New Delhi, India , and RO1 CA129537 and RO1 CA154320, USA. The authors declare that there are no conflicts of interest. Funding Information: The authors thank the members of Bhat Laboratory and Dr. Ajazul Hamid Wani for their fruitful discussions. The work is supported by the Ramanujan Fellowship grant from DST, India, and a UGC start-up grant from the University Grants Commission, New Delhi, India, and RO1 CA129537 and RO1 CA154320, USA. The authors declare that there are no conflicts of interest. Publisher Copyright: {\textcopyright} 2016 Elsevier B.V.",

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doi = "10.1016/j.mrrev.2016.03.005",

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AU - Farooq, Zeenat

AU - Banday, Shahid

AU - Pandita, Tej K.

AU - Altaf, Mohammad

N1 - Funding Information: The authors thank the members of Bhat Laboratory and Dr. Ajazul Hamid Wani for their fruitful discussions. The work is supported by the Ramanujan Fellowship grant from DST, India , and a UGC start-up grant from the University Grants Commission, New Delhi, India , and RO1 CA129537 and RO1 CA154320, USA. The authors declare that there are no conflicts of interest. Funding Information: The authors thank the members of Bhat Laboratory and Dr. Ajazul Hamid Wani for their fruitful discussions. The work is supported by the Ramanujan Fellowship grant from DST, India, and a UGC start-up grant from the University Grants Commission, New Delhi, India, and RO1 CA129537 and RO1 CA154320, USA. The authors declare that there are no conflicts of interest. Publisher Copyright: © 2016 Elsevier B.V.

PY - 2016/4/1

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N2 - Dot1/DOT1L (disruptor of telomeric silencing-1) is an evolutionarily conserved histone methyltransferase that methylates lysine 79 located within the globular domain of histone H3. Dot1 was initially identified by a genetic screen as a disruptor of telomeric silencing in Saccharomyces cerevisiae; further, it is the only known non-SET domain containing histone methyltransferase. Methylation of H3K79 is involved in the regulation of telomeric silencing, cellular development, cell-cycle checkpoint, DNA repair, and regulation of transcription. hDot1L-mediated H3K79 methylation appears to have a crucial role in transformation as well as disease progression in leukemias involving several oncogenic fusion proteins. This review summarizes the multiple functions of Dot1/hDOT1L in a range of cellular processes.

AB - Dot1/DOT1L (disruptor of telomeric silencing-1) is an evolutionarily conserved histone methyltransferase that methylates lysine 79 located within the globular domain of histone H3. Dot1 was initially identified by a genetic screen as a disruptor of telomeric silencing in Saccharomyces cerevisiae; further, it is the only known non-SET domain containing histone methyltransferase. Methylation of H3K79 is involved in the regulation of telomeric silencing, cellular development, cell-cycle checkpoint, DNA repair, and regulation of transcription. hDot1L-mediated H3K79 methylation appears to have a crucial role in transformation as well as disease progression in leukemias involving several oncogenic fusion proteins. This review summarizes the multiple functions of Dot1/hDOT1L in a range of cellular processes.

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The many faces of histone H3K79 methylation

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