Research Topics

Chromatin Structure, Genome Organization, Genomics, Protein Homeostasis, Proteomics, Regulation of Gene Expression

Disease Research Interests

Aging Related Diseases, Cancer, Metabolic Disorders/Diabetes

B.S., University of Michigan (Microbiology)
Ph.D., Northwestern University (Biochemistry and Biophysics)
Postdoctorate, University of California-San Francisco

Video interview

Molecular Chaperones; Transcription; Chromatin Remodeling; Genome Organization

Physiological balance is maintained, in part, through the rapid and well-timed assembly and disassembly of biological complexes. The dynamic interplay between select factors, including but not limited to proteins and nucleic acids, facilitates an efficient and functional cell environment. In general, pathways are driven forward through cooperative interactions thereby providing important features—rapid and robust action with limited energy input. However, within multi-step pathways cooperative stable assemblies have drawbacks since each complex is recalcitrant to dissociation. Hence, transitions between functional complexes or termination of action would be slow unless catalyzed. Despite the commonality of this problem, the possible cellular mechanisms promoting disassembly-events are not well understood. The primary focus of our laboratory is to identify and characterize the machinery driving a dynamic protein environment.

The Freeman research team exploits three central nuclear processes, transcription, chromatin remodeling, and genome reorganization, as molecular paradigms for understanding how the action of any single system can impact homeostasis, as dysfunction of these pathways can lead to cell death or uncontrolled growth (i.e., cancer). Since these processes employ a number of factors with common binding specificities, a decline in pathway efficiency is highly plausible due to the misassembly of individual complexes or an impairment in the disassembly of the utilized structures. The fundamental properties of molecular chaperones (abundant proteins with promiscuous but weak binding activities) allow biological factors to avoid these challenges by cultivating a self-organizing environment that fosters rapid action. In essence, the ability of molecular chaperones to promote protein dynamics parallels the more established chaperone roles in protein folding in which a chaperone does not dictate the final folded structure (path direction) but rather helps the nascent chain (system) avoid off-pathway energy barriers that commonly occur in protein folding (multi-step) energy landscapes. Our end goal is to understand the mechanisms by which molecular chaperones foster a dynamic nuclear environment thereby ensuring cell and organismal homeostasis.

MCB Distinguished Professorial Scholar, 2024
Fellow, American Association for the Advancement of Science 2021
Fellow, Cell Stress Society International 2020
TUM Ambassador, Technische Universität München 2015
Friedrich Wilhelm Bessel Research Award, Alexander von Humboldt Foundation 2010
Honorary Hans Fischer Senior Fellow, TUM-IAS 2010
Educator of the year, Alumni Association the University of Illinois 2009
Fellow, American Heart Association 2000-2002
Fellow, Leukemia and Lymphoma Society 1997-2000
Fellow, Leukemia Research Foundation 1996-1997

Dept. of Cell & Developmental Biology
University of Illinois
B107 CLSL
601 S. Goodwin Avenue
Urbana, IL 61801