Iris J. E. Stulemeijer
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Iris J. E. Stulemeijer has a total of 11 co-authors. Here are the top co-authors by number of shared publications:
- Barbara Marleen Bakker
Laboratory of Paediatrics, University Medical Centre Groningen, University of Groningen, The Netherlands
1 shared publication Dirk De Vos
Department of Biology, University of Antwerp, Antwerp, 2020, Belgium
1 shared publication- Erik Leonardus de Graaf
Fondazione Pisana per la Scienza ONLUS , 56121 Pisa, Italy
1 shared publication - Fred van Leeuwen
Division of Gene Regulation, Netherlands Cancer Institute
1 shared publication - Hanneke Vlaming
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA;
1 shared publication Kirsten van Harten
Division of Gene Regulation, Netherlands Cancer Institute, Amsterdam, 1066 CX, The Netherlands
1 shared publication
Latest Publications
- Open Access
- 12 May 2015
- Published by Springer Nature in Scientific Reports
- Vol. 5 (1) , 9824
Dot1 histone methyltransferases share a distributive mechanism but have highly diverged catalytic properties
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.
- 12 May 2015
- Published by Springer Nature in Scientific Reports
- Vol. 5 (1) , 9824
Open AccessDot1 histone methyltransferases share a distributive mechanism but have highly diverged catalytic properties
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.