Elizabeth A. Craig

Emeritus Professor 2024-present
Professor 2002-2023
Elizabeth Cavert Miller Professor, Steenbock Professor of Microbial Science
Lab Website ecraig@wisc.edu(608) 263-7105

141B HF DeLuca Biochemistry Laboratories
433 Babcock Drive
Madison, WI 53706-1544

Education

B.A., University of Rhode Island
Ph.D., Washington University School of Medicine

Publications
PubMed

The function of molecular chaperones in the cell - Folding and remodeling of proteins

The Craig lab investigates the function of proteins called molecular chaperones in protein homeostasis and core “housekeeping” cellular functions.

Maintenance of cellular homeostasis requires a fine-tuned balance of many biological processes. Protein homeostasis is particularly intricate, because it requires maintaining balance amongst biogenesis, folding, trafficking and degradation of all cellular proteins. A group of ubiquitous proteins, referred to collectively as molecular chaperones, play active roles in maintaining protein homeostasis by transiently binding to many different polypeptides. Of these, the Hsp70 chaperone/J-domain protein co-chaperone systems, which are present in all major cellular compartments, are the most versatile. They play key roles, not only in general homeostasis networks of protein folding and degradation, but also in core biological processes, often by driving assembly and disassembly of multimeric complexes.

The overarching goal of the Craig lab is to understand the attributes of Hsp70s and J-domain proteins, that drive their ability to carry out diverse biological roles. To do so we use well-developed Hsp70/J-domain protein systems that are exceptionally amenable to both genetic and biochemical analysis. These include mitochondrial systems involved in protein translocation and FeS cluster biogenesis, as well as two systems in the cytosol: one is present at the exit of the ribosome tunnel, involved in initial folding events as nascent polypeptide chains emerge; the other includes two structurally similar, yet functionally distinct, J-domain proteins that partner with the same Hsp70, “tuning” its activity in subtly different ways.

Cartoon for Hsp70s/J-domain proteins function in all aspects of protein homeostasis and in core biological processes


Publications

Photo of Betty Craig

Areas of Expertise

  • Biomolecular Folding & Interactions
  • Gene Expression & RNA Biology
  • Metals in Biology