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Eisenstein, Edward

Edward Eisenstein
Associate Professor
9600 Gudelsky Drive Room A231 Rockville, MD 20850
Lab Description

News About This Professor

Research Interests 

Biophysics, molecular interactions, gene-metabolite relationships in medicinal plants, molecular basis for plant disease resistance, plant metabolic engineering for improved biofuel production.


Ph.D., Georgetown University, 1985

Current Research Projects 

Professor Eisentein's laboratory is investigating a number of questions involving plants, including their remarkable capacity to produce a complex array of interesting compounds, the way they respond to pathogens and disease, and also the feasibility of engineering their biosynthetic apparatus for applications ranging from human health to biofuel production.

The Eisenstein Group is currently engaged in three primary research investigations:

Metabolic Engineering of Secondary Metabolite Synthesis in Medicinal Plants of Appalachia

The Eisenstein Group's aim is to identify the genes and enzymes that are involved in the biosyntheses of the important compounds found in black cohosh, Actaea racemosa (syn. Cimicifuga racemosa (L.) Nutt.), a member of the Ranunculaceae (buttercup) family, in an effort to understand the interplay of genetic and environmental factors that are involved in the production of medicinal metabolites, and to apply that knowledge to improve the phytochemical quality of plants through metabolic engineering. Our approach has focused on developing a tissue culture system to generate a useful laboratory model for black cohosh, establishing cDNA libraries for a variety of tissues in the plant, using transcriptional profiling and LC/MS approaches to develop gene-metabolite maps for the production of cimiracemates, terpene glycosides and tryptoamine derivatives in planta, as well as protein production for structural and functional analysis of the enzymes involved in metabolite biosynthesis.

Allosteric Motor Proteins Involved in Plant Disease Resistance

We are studying the classical tobacco-tobacco mosaic virus (TMV) system as a model for the molecular basis for plant-pathogen interactions. The protein encoded by the tobacco N gene is a multi-functional, allosteric, motor protein that binds and hydrolyzes ATP to promote conformational changes that function as a molecular switch to regulate signaling pathways. The N protein, a member of the largest class of polymorphic R proteins which contain a nucleotide-binding domain, a C-terminal, leucine-rich repeat domain, and an N-terminal, Toll/interluckin-1 receptor domain, binds the helicase protein of TMV to activate the hypersensitive response in tobacco. We are exploring the mechanism of N-helicase binding, the nucleotide-promoted dissociation of the TMV helicase protein, and the conformational changes that activate signaling pathways.

Engineering Designer Lignins for Improved Production of Cellulosic Biomass for Biofuels

A principal obstacle to the saccharification of lignocellulosic biomass for ethanol production is the reduction of lignin content for the more effective action of enzymes on cellulose. Our goal in this project is to produce "engineered" lignins in vivo by manipulation and control of precursor availability and biosynthesis. Our approach builds on the discovery of dirigent proteins, which are thought to guide the formation of specific intermediates and polymers of lignin. We are designing a series of proteins that bind monolignol radicals and that promote the formation of specific stereochemical dilignol products. Longer-range goals include the incorporation of oxidase activity into engineered monolignol binding proteins to create functional enzymes capable of generating a defined suite of lignin precursors.

Selected Publications 

Yamniuk, A. P., Edavettal S. C., Bergqvist S., Yadav S. P., Doyle M. L., Calabrese K., et al. (2012).  ABRF-MIRG Benchmark Study: Molecular Interactions in a Three-Component System.. J Biomol Tech. 23(3), 101-14.

McElroy, C. A., Holland P. J., Zhao P., Lim J-M., Wells L., Eisenstein E., et al. (2012).  Structural reorganization of the interleukin-7 signaling complex.. Proc Natl Acad Sci USA. 109(7), 2503-8.

Spiering, M. J., Urban L. A., Nuss D. L., Gopalan V., Stoltzfus A., and Eisenstein E. (2011).  Gene identification in black cohosh (Actaea racemosa L.): expressed sequence tag profiling and genetic screening yields candidate genes for production of bioactive secondary metabolites. Plant cell reports. 30(4), 613-29.

Asim K. Bera, Vesna Atanasova, Howard Robinson, Edward Eisenstein, James P. Coleman, Everett C. Pesci and James F. Parsons (2009) "Structure of PqsD, A Pseudomonas Quinolone Signal Bioynthetic Enzyme, in Complex with Anthranilate," Biochemistry 48, 8644-8655.

Iva Naratilova, Edward Eisenstein, David G. Myszka (2005) Measuring Long Association Phases using Biacore, Analytical Biochemistry 344, 295-297.

D.Travis Gallagher, Dianna Chinchilla, Heidi Lau and Edward Eisenstein (2004) Local and global control mechanism in allosteric threonine deaminase, Methods in Enzymology 380, 85-106.

James F. Parsons, Fenhong Song, Lisa Parsons, Kelly Calabrese, Edward Eisenstein and Jane E. Ladner (2004) "Structure and Function of the Phenazine Biosynthesis Protein PhzF from Pseudomonas fluorescens 2-79," Biochemistry43, 12427-12435.

D. Cheon Yeh, James F. Parsons, Lisa M. Parsons, F. Liu, Edward Eisenstein and John Orban (2004) "NMR assignment of the hypothetical protein HI0004 from Haemophilus influenzae, a putative essential gene product," J. Biomol. NMR 29, 101-102.

David G. Myszka, Yasmina N. Abidiche, Fumio Arisaka, Olwyn Byron, Edward Eisenstein, Preston Hensley, James A. Thomson, Christian R. Lombardo, Frederick Schwarz, Walter Stafford and Michael L. Doyle (2003) The ABRF-MIRG'02 study: assembly state, thermodynamic, and kinetic analysis of an enzyme/inhibitor interaction, J. Biomolecular Techniques 14, 247-269.

Susan Krueger, Susan K. Gregurick, James Zondlo, and Edward Eisenstein (2003) Interaction of GroEL and GroEL/GroES complexes with a Non-native Subtilisin Variant: A Small-Angle Neutron Scattering Study, J. Structural Biology 141, 240-258.

James F. Parsons, Pia, Y. Jensen, Abraham S. Pachikara, Andrew J. Howard, Edward Eisenstein and Jane E. Ladner (2002) Structure of Escherichia coli Aminodeoxychorismate Synthase: Architectural Conservation and Diversity in Chorismate Utilizing Enzymes. Biochemistry 41, 2198-2208.

Edward Eisenstein, Gary L. Gilliland, Osnat Herzberg, John Moult, John Orban, Roberto J. Poljak, linda Banerjei, Delwood Richardson and Andrew J. Howard (2000) "Biological function made crystal clear—annotation of hypothetical proteins via structural genomics," Curr. Opinion in Biotechnology 11, 25-30.

D. Travis Gallagher, Gary L. Gilliland, Gaoyi Xiao, James Zondlo, Kathryn E. Fisher, Diana Chinchilla and Edward Eisenstein (1998) "Structure and Control of Pyridoxal Phosphate-Dependent Allosteric Threonine Deaminase," Structure 6, 465-475.

Zhanglin Lin, Frederick P. Schwarz and Edward Eisenstein (1995) "The Hydrophobic Nature of GroEL-Substrate Binding," J. Biol. Chem270, 1011-1014.

Edward Eisenstein, Kathryn E. Fisher, Hoon Dae Yu, Karin R. Ducote, Dominick A. Iacuzio and Frederick P. Schwarz (1995) "An Expanded Two State Model Accounts for Homotropic Cooperativity in Biosynthetic Threonine Deaminase," Biochemistry 34, 9403-9412.

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