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Volume 8 Journal of Biotechnology & Biomaterials
ISSN: 2155-952X Biotech Congress 2018 & Enzymology 2018
March 05-07, 2018
JOINT EVENT
20th Global Congress on Biotechnology
3rd International Conference on Enzymology and Molecular Biology
&
March 05-07, 2018 London, UK
Molecular enzymology of DNAmethyltransferases – conformational changes and allosteric regulation
Albert Jeltsch
University Stuttgart, Germany
DNA methylation is an essential epigenetic chromatin modification. The setup and maintenance of DNA methylation patterns
depends on the coordinated activity of DNA methyltransferases (DNMTs) and their allosteric regulation by interacting proteins,
other chromatin modifications and post-translational modifications. I will present novel assays for DNMTs including single enzyme
assays to study their mechanism and conformationally locked mutants to study allosteric effects. Based on this, recent data regarding
the regulation and targeting of DNMTs by allosteric effect will be presented. Moreover, I will present insights into the mechanism of
DNMTs regarding target site location, specificity and processivity.
Figure 1: Domain structure and 3D structure of DNMT1. A) Domain structure of DNMT1 (for descriptions of the domains refer to
the main text). B-D) Different structures of DNMT1 with AdoHcy shown in yellow and DNA in light green. B) Structure with DNA
bound in the active site. UHRF1 (yellow) stabilizes the active conformation of DNMT1. C) Structure with unmethylated DNA bound
to the CXXC domain. D) Apoenzyme structure with the RFT domain blocking of the active site.
Recent Publications
1. Lungu et al. (2017) Modular fluorescence complementation sensors for live cell detection of epigenetic signals at endogenous
genomic sites. Nature Communications 8:649.
2. Maier, Möhrle and Jeltsch (2017) Design of synthetic epigenetic circuits exhibiting positive feedback, memory effects and
reversible switching, Nature Communications 8:15336.
3. Jurkowska and Jeltsch (2016) Allosteric control of mammalian DNA methyltransferases - a new regulatory paradigm.
Nucleic Acids Res. 44:8556-8575.
4. Bashtrykov, et al. (2014)TheUHRF1 protein stimulates the activity and specificity of themaintenanceDNAmethyltransferase
DNMT1 by an allosteric mechanism. J. Biol. Chem. 289:4106-15.
5. Jeltsch and Jurkowska (2014) New concepts in DNA methylation. Trends Biochem Sci. 39:310-18.
Biography
Albert Jeltsch completed his PhD working on the mechanism of restriction endonucleases at University of Hannover in 1994. Afterwards, he started to study
DNA methyltransferases at Justus-Liebig University Giessen and at Jacobs University Bremen. Since 2011, he is a Professor of Biochemistry at the University
Stuttgart. He received the Gerhard-Hess award (DFG) and BioFuture award (BMBF). He has long standing expertise in Biochemical study of DNA and protein
methyltransferases, methyl lysine reading domains and in rational and evolutionary protein design. His work has been published in more than 250 publications in
peer reviewed journals and he is in the editorial boards of several journals.
Albert Jeltsch, J Biotechnol Biomater 2018, Volume 8
DOI: 10.4172/2155-952X-C2-091