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Assistant Professor
Education/Training
College Degree: B.A. (Honors) University of Pennsylvania
Post Doctoral: Ph.D. University of California, Los Angeles
Fellowship: Harvard Medical School
108 N. Greene Street, Room 419D
Baltimore, Maryland 21201
Phone (410) 706-5345
Fax (410) 706-8297
email: etoth001@umaryland.edu Reasearch Description
My research centers on the structure and function of helicases crucial to chromosomal integrity and mRNA processing. I am particularly interested in studying the multiprotein complexes in which these helicases function and how both the content and context of these assemblages determines their in vivo activity. Since helicases often form stable complexes with DNA or RNA, a helicase-nucleic acid complex is a good starting point for the construction of multiprotein assemblies that genuinely reflect the species that are active in vivo.
Each structure will provide information for in vitro functional analyses that will both help to dissect the role of individual components of the complex and aid in the formation of stable higher-order assemblies. Such studies should culminate in a series of snapshots of a working molecular machine. My current projects are the structural analyses of the RecQ helicase Sgs1 and MER3 (a RecQ-like enzyme) from Saccharomyces cerevisiae and the RhlB and Ski mRNA processing helicases from Escherichia coli and yeast, respectively.
Associated site: X-Ray Crystallography Facility - crystal.umaryland.edu MBIC701 Classroom notes
Lab Personnel:
Dimeka Patterson B.S. - research technician and lab manager.
Publications:
Toth, E.A., Li, Y., Sawaya, M.R., Cheng, Y., and Ellenberger, T. (2003). The crystal structure of the bifunctional primase-helicase of bacteriophage T7. Mol Cell., 12(5), 1113-1123.
Silvian, L.F., Toth, E.A., Pham, P., Goodman, M.F., and Ellenberger, T. (2001). Crystal structure of a DinB family error-prone DNA polymerase from Sulfolobus solfataricus. Nat Struct Biol., 8(11), 984-989.
Toth, E.A., and Yeates, T.O. (2000). The structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway. Structure, 8, 163-174.
Toth, E.A., Worby, C., Dixon, J.E., and Yeates, T.O. (2000). The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds. JMB, 301, 433-450.
Colovos, C., Toth, E.A., and Yeates, T.O. (2000). Evaluation of phase accuracy via topological and geometric analysis of electron density maps. Acta Crystallographica D56, 1421-1429. |
