Olena Vatamaniuk
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Cornell University 608 Bradfield Hall Ph.D. in Plant Physiology, Kyiv State University, Kyiv, UKRAINE B.S. in Plant Physiology, Lviv State University, Lviv, UKRAINE. Olena Vatamaniuk is an Assistant Professor of Molecular Biology of Abiotic Stress. She joined the Cornell faculty in 2005. Her PhD research, focusing on cold stress-promoted morphophysiological changes in meristems of corn roots, encouraged her to learn molecular mechanisms that allow plants to adjust to the environment. Driven by the desire to extend her expertise from plant to molecular physiology, cellular biology and biochemistry, she conducted her postdoctoral studies at the Department of Biology at the University of Pennsylvania, were she focused on molecular mechanisms of phytochelatin-dependent heavy metal detoxification of plants. Finding that this pathway, formerly suggested to be restricted to plants and some fungi, operates in at least some animals, the nematode worm Caenorhabditis elegans, prompted her to gain additional expertise in C. elegans biology, at the Department of Genetics of the University of Pennsylvania. Her research program focuses on defining common and unique mechanisms, utilized by plants, fission yeast and animals to accommodate heavy metals, encountered in the environment. |
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Research Program My research program focuses on molecular analysis of mechanisms used by different organisms to detoxify heavy metals. Heavy metals (e.g. essential heavy metals such as copper (Cu2+), zinc (Zn2+) and non-essential heavy metals such as cadmium (Cd2+), lead (Pb2+), mercury (Hg2+)) are chemical elements whose densities exceed 5g/cm3. Since heavy metals are not biodegradable, chronic exposure leads to their accumulation in the tissues, and causes various disease states. Therefore, to protect themselves from heavy metal poisoning, cells adopted several, primarily, chelating-based mechanisms for tight regulation of the concentration of free metal ions. We study the phytochelatin (PC)-dependent pathway for heavy metals detoxification. PCs are synthesized from glutathione, GSH, by PC synthases, which have the general structure ( g-Glu-Cys)n Xaa (n = 2-11). Originally, PCs were discovered, and suggested to function only in fungi and plants. We determined, however, that this pathway operates and is required for heavy metal tolerance in some animals, including the nematode worm C. elegans. Furthermore, we discovered that at least one of components of this pathway exists in higher animals, which lack PCs. Our interests include mechanism of the pathway’s action, whether it functions in heavy metal detoxification in higher animals, or has undergone evolutionary divergence, such that its representative in different organisms serves different roles. Using a combination of genetic, molecular and biochemical techniques, we analyze interactions of PC-dependent pathway with other detoxification pathways. We focus on specific aspects of proteome response to heavy metal toxicity, and common and unique features manifested by different organisms. Our studies are expected to contribute to optimization of approaches for prevention heavy metal accumulation and poisoning of organisms, and to be utilized for environmental decontamination.Courses Taught Graduate level course: CSS/BIOL PL 642: Mineral Nutrition: From Plants to Humans .CSS 610: Physiology of Environmental Stresses in Plants (will co-teach) |
Selected Publications 1.Romanyuk N.D, Rigden, D.J Vatamaniuk O.K., Lang, A. Cahoon, R.E., Jez, J.M., Rea, P.A.(2006) Mutanenic definition of papain-like catalytic triad, sufficiency of N-terminal domain for single-site core catalytic enzyme acylation and C-terminal domain for augmentative metal activation of an eukaryotic phytochelatin synthase. Plant Physiology 2006 May 19(Epub ahead of print) 2. Vatamaniuk O.K., Bucher E.A., Sundaram M.V. and Rea P.A. (2005) CeHMT-1, a putative phytochelatin transporter, is required for cadmium tolerance in Caenorhabditis elegans. J Biol Chem, 280, 23684-23690. web access: http://www.jbc.org/cgi/content/abstract/280/25/23684 3. Rea P.A., Vatamaniuk O.K., Rigden D.J. (2004) Weeds, worms and more: papain’s long-lost cousin, phytochelatin synthase. Plant Phys. 136, 2463-2474. web access: http://www.plantphysiol.org/cgi/content/full/136/1/2463 4. Vatamaniuk, O.K., Mari, S., Lang A., Demkiv, L.O. and Rea, P.A. (2004) Phytochelatin synthase, a dipeptidyl transferase that undergoes multisite acylation with g-glutamylcysteine during catalysis. STOICHIOMETRIC AND SITE-DIRECTED MUTAGENIC ANALYSIS OF AtPCS1-CATALYZED PHYTOCHELATIN SYNTHESIS. J. Biol. Chem. 279, 22449-22460. web access: http://www.jbc.org/cgi/content/full/279/21/22449 5. Vatamaniuk O.K., Bucher E.A. and Rea P.A. (2002) Worms take the ‘phyto’ out of ‘phytochelatins’. Trends in Biotechnol., 20, 61-64. web access: http://dx.doi.org/10.1016/S0167-7799(01)01873-X 6. Vatamaniuk O.K., Bucher E.A., Ward J.T. and Rea P.A. (2001) A new pathway for heavy metal detoxification in animals: phytochelatin synthase is required for cadmium tolerance in Caenorhabditis elegans. J. Biol. Chem., 276, 20817-20820. web access: http://www.jbc.org/cgi/content/full/276/24/20817 7. Vatamaniuk, O.K., Mari, S., Lu, Y. -P. and Rea, P.A. (2000) Mechanism of heavy metal ion activation of phytochelatin (PC) synthase: blocked thiols are sufficient for PC synthase-catalyzed transpeptidation of glutathione and related thiol peptides. J. Biol. Chem., 275, 31451-31459. web access: http://www.jbc.org/cgi/content/full/275/40/31451 8. Vatamaniuk, O.K., Mari, S., Lu, Y.-P., and Rea, P.A. (1999) AtPCS1, a phytochelatin synthase from Arabidopsis: isolation and in vitro reconstitution. Proc. Natl. Acad. Sci. USA, 96, 7110-7115. web access: http://www.pnas.org/cgi/content/full/96/12/7110Click here for a PubMed listing of Dr. Vatamaniuk's publications
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