James M. Berger
Johns Hopkins University
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Primary Section: 21, Biochemistry Secondary Section: 29, Biophysics and Computational Biology Membership Type:
Member
(elected 2013)
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Biosketch
James Berger is a Professor in the Department of Biophysics and Biophysical Chemistry at the Johns Hopkins School of Medicine. Berger is a structural biologist and biochemist whose research focuses on understanding the assembly and mechanisms of large, nucleic acid-dependent protein complexes responsible for organizing, copying, and preserving the flow genetic information. Berger was born in Albuquerque, NM in 1968 and grew up in the Los Alamos/Santa Fe area. He graduated summa cum Laude in 1990 from the University of Utah with a degree in biochemistry and received his doctorate from Harvard University in 1995. Berger subsequently became a Fellow at the Whitehead Institute for Biomedical Research at MIT until 1998, after which he joined the faculty of the Department of Molecular and Cell Biology at UC Berkeley. In 2013, he moved to his present position at Johns Hopkins.
Research Interests
Berger'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. He is particularly interested in developing mechanistic, atomic-level models that explain how macromolecular machines transduce chemical energy into force and motion, and how cells exploit these complexes and their activities to control replisome formation, gene expression, chromosome superstructure, and other essential nucleic-acid transactions. His approaches rely on a variety of structural, biochemical, and biophysical methods to define the architecture, function, evolution, regulation, and small-molecule inhibition of biological complexes. Since starting his independent research program, Berger's group has biochemically and structurally defined the range and nature of a number of key architectural transitions and the physical consequences of nucleotide binding in systems such as topoisomerases, helicases, condensins, and replication initiators. Berger has also successfully determined how many of these enzymes distinguish between DNA substrates and they are controlled by both cellular factors and therapeutic agents.
