Edward EgelmanDepartment of Biochemistry and Molecular Genetics, University of Virginia School of Medicine, Charlottesville, VA, USA F1000 Faculty Member (since 11 July 2001)
Professor of Biochemistry & Molecular Genetics, University of Virginia School of Medicine
BA, Brandeis University, 1976
PhD Brandeis University,1982
Postdoc, MRC Laboratory of Molecular Biology, 1982-1984
MEMBERSHIPS, PROFESSIONAL ACTIVITIES:
1992-4 National Advisory Committee, Integrated Microscopy Resource, Madison, WI
1993- Editorial Board, Biophysical Journal
1994 Chair, Structural Biology Review Panel (Imaging), Department of Energy
1994-98 Member, NIH BBCB Study Section (Biophysical Chemistry)
2000-2003 Council, Biophysical Society
2001- National Advisory Council, Albany NIH 'Visualization of Biological Complexity' Resource
2001-2003 Program Chair, 2003 Annual Meeting of the Biophysical Society
2003 National Advisory Council, Baylor College of Medicine NIH Resource
2004 Boris Balinsky Lecture, South Africa
2005 Elected Fellow of the Biophysical Society
2005 John P McGovern Lecture, Houston, TX
2006-10 Editor, Macromolecular Assemblages issues, Current Opinion in Structural Biology
2006-7 Editorial Board, Journal of Biological Chemistry
2007-2012 Editor-in-Chief, Biophysical Journal
2007 Elected Fellow of the American Academy of Microbiology
2008 Chair, NIH Pathways to Independence Study Section
2009 Chair, NIH High-End Instrumentation Study Section
2010 Editor, Elsevier 9 Volume Major Reference Work on Comprehensive Biophysics
2013 Chair, Three-Dimensional Electron Microscopy Gordon Conference
Our research is focused on the structure and function of macromolecular assemblies, using the techniques of electron microscopy and computed image reconstruction. We have been mainly working in two different areas: protein-DNA complexes active in homologous recombination and replication, and F-actin (Egelman, 2003). However, the development of new techniques in my lab to study RecA-DNA filaments and F-actin has led to new applications to such systems as bacterial Type Three Secretion Systems (Wang et al, 2006), filamentous bacteriophage and bacterial pili (Craig et al., 2006).
The E. coli RecA filament has been the most intensively studied enzyme in homologous recombination, and we have been studying the helical filament that the RecA filament forms on DNA which is the scaffold within which homologous recombination is initiated. The RecA protein induces a highly unusual structure on the DNA within this filament, and this appears to be an important aspect of RecA's enzymatic role. We have shown that the eukaryotic homolog of RecA, the Rad51 protein, forms a nearly identical structure (Ogawa et al, 1993). We are interested in how human Rad51 interacts with BRCA2, the protein product of a gene identified in familial breast cancer susceptibility (Galkin et al, 2005).
Actin is the most ubiquitous and conserved eukaryotic protein. While it was first identified in muscle, as being the main component of the thin filaments, it is equally abundant in most non-muscle cells, where it plays a key role in the control of cell form and motility. We have found that the F-actin filament can exist in a number of different structural states , which provides insight into many phenomena, including the ability of the cell to control how actin specifically binds more than 40 other proteins.
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F1000 Biology Reports 2009 1:(7) (21 Jan 2009)
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