Title
Dot1 histone methyltransferases share a distributive mechanism but have highly diverged catalytic properties
Author
Faculty/Department
Faculty of Sciences. Biology
Publication type
article
Publication
London :Nature Publishing Group ,
Subject
Engineering sciences. Technology
Source (journal)
Scientific reports. - London, 2011, currens
Volume/pages
5(2015) , 11 p.
ISSN
2045-2322
2045-2322
Article Reference
9824
Carrier
E-only publicatie
Target language
English (eng)
Full text (Publishers DOI)
Affiliation
University of Antwerp
Abstract
The conserved histone methyltransferase Dot1 establishes an H3K79 methylation pattern consisting of mono-, di- and trimethylation states on histone H3 via a distributive mechanism. This mechanism has been shown to be important for the regulation of the different H3K79 methylation states in yeast. Dot1 enzymes in yeast, Trypanosoma brucei (TbDot1A and TbDot1B, which methylate H3K76) and human (hDot1L) generate very divergent methylation patterns. To understand how these species-specific methylation patterns are generated, the methylation output of the Dot1 enzymes was compared by expressing them in yeast at various expression levels. Computational simulations based on these data showed that the Dot1 enzymes have highly distinct catalytic properties, but share a distributive mechanism. The mechanism of methylation and the distinct rate constants have implications for the regulation of H3K79/K76 methylation. A mathematical model of H3K76 methylation during the trypanosome cell cycle suggests that temporally-regulated consecutive action of TbDot1A and TbDot1B is required for the observed regulation of H3K76 methylation states.
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Full text (open access)
https://repository.uantwerpen.be/docman/irua/8a3b09/10248.pdf
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