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Johns Hopkins University logoProgram in Molecular Biophysics
James BergerBerger Lab

Professor
Department of Biophysics and Biophysical Chemistry
School of Medicine


B.S. 1990, University of Utah
Ph.D. 1995, Harvard University

jmberger@jhmi.edu

713 WBSB
725 N. Wolfe Street
Baltimore, MD 21205

Office: 410-955-7163
Lab:
410-955-7167

 

School of Medicine logo

My laboratory's research is focused on understanding how multi-subunit assemblies use ATP for overcoming topological challenges within the chromosome and controlling the flow of genetic information.  We are particularly interested in developing mechanistic models that explain how macromolecular machines transduce chemical energy into force and motion, and in determining how cells exploit these complexes and their activities for regulating the initiation of DNA replication, chromosome superstructure, and other essential nucleic acid transactions.  Our principal approaches rely on a variety of structural, biochemical, and biophysical methods to define the architecture, function, evolution, and regulation of biological complexes.  We also have extensive interests in mechanistic enzymology and the study of small-molecule inhibitors of therapeutic potential, the development of chemical approaches to trapping weak protein/protein and protein/nucleic acid interactions, and in using microfluidics for biochemical investigations of protein dynamics and structure.


Selected Publications
Montpetit, B., N.D. Thomsen, K.J. Helmke, M.A. Seeliger, J.M. Berger*, and K. Weis*. (*co-corresponding authors) (2011) A conserved mechanism of DEAD-box ATPase activation by nucleoporins and InsP6 in mRNA export. Nature 472:238-242.

Costa, A., I. Ilves, N. Tamberg, T. Petojevic, E. Nogales, M.R. Botchan*, and J.M. Berger*. (*co-corresponding authors) (2011) The structural basis for MCM2-7 helicase activation by GINS and Cdc45. Nat. Struct. Mol. Biol. 18:471-477.

Lyubimov, A.Y., M. Strycharska, and J.M. Berger. (2011) The nuts and bolts of ring-translocase structure and mechanism. Curr. Opin. Struct. Biol. 21:240-248.

Dueber, E.C., A. Costa, J.E. Corn, S.D. Bell, and J.M. Berger. (2011) Molecular determinants of origin discrimination by Orcl initiators in archaea. Nucleic Acids Res. 39:3621-3631.


Tretter, E.M., J.C. Lerman, and J.M. Berger. (2010) A naturally chimeric type llA topoisomerase in Aquifex aeolicus highlights an evolutionary path for the emergence of functional paralogs. Proc. Natl. Acad. Sci. USA 107:22055-22059.

Li, Y., N.K. Stewart, A.J. Berger, S. Vos, A.J. Schoeffler, J.M. Berger, B.T. Chait, and M.G. Oakley. (2010) Escherichia coli condensin MukB stimulates topoisomerase IV activity by a direct physical interaction. Proc. Natl. Acad. Sci. USA 107:18832-18837.

Corbett, K.D., and J.M. Berger. (2010) Structure of the ATP-binding domain of Plasmodium falciparum Hsp90. Proteins 78:2738-2744.

Schoeffler, A.J., A.P. May, and J.M. Berger. (2010) A domain insertion in Escherichia coli GyrB adopts a novel fold that plays a critical role in gyrase function. Nucleic Acids Res. 38:7830-7844.

Duderstadt, K.E., M.L. Mott, N.J. Crisona, K. Chuang, H. Yang, and J.M. Berger. (2010) Origin remodeling and opening in bacteria relies on distinct assembly states of the DnaA initiator. J. Biol. Chem. 285:28229-28239.

Schmidt, B.H., A.B. Burgin, J.E. Deweese, N. Osheroff, and J.M. Berger. (2010) A novel and unified two-metal mechanism for DNA cleavage by type ll and lA topoisomerases. Nature 465:641-644.

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