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1991 - BS/MS, Kiev State University, Kiev, Ukraine
1996 - Ph.D., Institute of Molecular Biology and Genetics, Kiev, Ukraine
1997 - 2003 - Postdoctoral training, University of Texas at Austin and European
Molecular Biology Laboratory, Heidelberg, Germany
RESEARCH
There are three directions of our current research: gene editing/genome engineering, protein engineering, and aging.
Gene/genome editing, genome engineering
The main direction of our research is correction of genetic defects. Currently, we are working on fixing the mutations that cause sickle cell anemia. In our experiments we use several gene editing/genome engineering tools: target-specific variants of the tyrosine DNA recombinases Flp and Cre (as well as related recombinases) along with the CRISPR/Cas9 and TALEN systems.
Site-specific recombinases of the tyrosine type can bring about a full range of the DNA rearrangement reactions: integration and excision, inversion, translocation, and cassette replacement. Tyrosine recombinases mediate these reactions from start to finish in any cell type, without any dependence on the cell DNA repair machinery; they are thus particularly useful for controlled genome rearrangements.
For our gene editing/genome engineering experiments, we design non-viral vectors with different functional elements, including S/MAR and insulator elements. We also experiment with in vitro transcribed mRNA, shRNA, transposase-mediated integrating vectors, and minicircles.
Protein engineering
Our second research direction is protein engineering. We evolve variants of tyrosine recombinases with new target specificity and analyze how individual amino acid substitutions influence the specificity switch. In this research we use Flp, Cre, TD, and R recombinases.
Tyrosine recombinase family is surpisingly numerous: it contains over 1000 members that have similar 3D fold but remarkably different target specificity. These properties make tyrosine recombinases an attractive model for modifying enzyme specificity and deciphering the functional role of their amino acid residues in target recognition.
Aging
The third emerging direction of our research is aging. We want to understand how to systemically eliminate harmful modifications that cells acquire during the aging process and to bring cells to their default state thus rejuvenating them. As a model organism, we use budding yeast as they are able to reset their lifespan during spore formation.
Available positions
Positions for graduate students are available.
PUBLICATIONS
(PubMed database)
SELECTED PUBLICATIONS
Williams J.D., Voziyanova E., Voziyanov Y.
The bacteriophage lambda integrase catalytic domain can be modified to act with the regulatory domain as a recombination-competent binary recombinase.
J. Biol. Chem. 2022:102721. doi: 10.1016/j.jbc.2022.102721
Voziyanova E., Li F., Shah R., Voziyanov Y.
Genome targeting by hybrid Flp-TAL recombinases.
Scientific Reports, 2020
Voziyanova E., Anderson R.P., Voziyanov Y.
Dual Recombinase-Mediated Cassette Exchange by Tyrosine Site-Specific Recombinases.
Methods Mol. Biol., 2017
Voziyanova E., Anderson R.P., Shah R., Li F., Voziyanov Y.
Efficient genome manipulation by variants of site-specific recombinases R and TD.
J. Mol. Biol., 2016
Shah R., Li F., Voziyanova E., Voziyanov Y.
Target-specific variants of Flp recombinase mediate genome engineering reactions in mammalian cells.
FEBS J., 2015
Voziyanova E., Malchin N., Anderson R.P., Yagil E., Kolot M., Voziyanov Y.
Efficient Flp-Int HK022 dual RMCE in mammalian cells.
Nucleic Acids Res., 2013
Anderson R.P., Voziyanova E., Voziyanov Y.
Flp and Cre expressed from Flp-2A-Cre and Flp-IRES-Cre transcription units mediate the highest level of dual recombinase-mediated cassette exchange.
Nucleic Acids Res., 2012
Shultz J.L., Voziyanova E., Konieczka J.H., Voziyanov Y.
A genome-wide analysis of FRT-like sequences in the human genome.
PLoS One, 2011
Malchin N., Molotsky T., Borovok I., Voziyanov Y., Kotlyar A.B., Yagil E., Kolot M.
High efficiency of a sequential recombinase-mediated cassette exchange reaction in Escherichia coli.
J. Mol. Microbiol. Biotechnol., 2010
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