Position title: Professor
Protein folding in the cell â€” the function of molecular chaperones in facilitating protein folding, remodeling of protein:protein complexes and protein translocation across membranes
- 441E Biochemistry Addition
- Ph.D., Washington University (St. Louis) (1972), Postdoctoral Research: Washington University; UC-San Francisco
- Research Interests
- Protein folding in the cell â€” the function of molecular chaperones in facilitating protein folding, remodeling of protein:protein complexes and protein translocation across membranes
- Research Fields
- Disease Biology, Cell Biology, Fungi
Research in the Craig laboratory lies at the interface between genetics, cell biology and biochemistry, focused on understanding how proteins reach their final cellular location and fold into their active conformation. Protein folding and translocation is fraught with many possible missteps, leading to misfolding and aggregation. A number of genetic diseases, including Huntington’s, Alzheimer’s and Creutzfeld Jacob’s diseases are caused by defects in protein folding, underlining the biological importance of this problem. We emphasize the cellular function of molecular chaperones, a highly conserved group of proteins that facilitates the folding of other proteins by transiently binding to their unfolded forms. Using a combination of experimental tools, including yeast genetics, an in organellar mitochondrial system, in vitro translation systems and in vitro analysis of purified proteins, we are probing the mechanisms used by cells to ensure proper protein function. Using the yeast S. cerevisiae as a model system, we analyze the function of the Hsp70:J-protein chaperone machinery in (1) the folding of newly synthesized proteins, (2) the translocation of proteins into mitochondria, (3) the biogenesis of Fe-S proteins and (4) the maintenance of certain yeast proteins in their prion form.
Search PubMed for more publications by Elizabeth Craig
Aloria, K., Schilke, B., Andrew, A. and Craig, E.A. 2004. Iron-induced oligomerization of the yeast frataxin homolog, Yfh1, is dispensable in vivo, EMBO Reports, 5:1096-101.
Eisenmann, H. and Craig, E.A. 2004. Activation of Pleiotropic Drug Resistance by the J-protein and Hsp70 related proteins, Zuo1 and Ssz1. Mol. Microbiology, 53:335-44.
Liu, Q., D’Silva, P., Walter, W., Marszalek, J. and Craig, E.A. 2003. Regulated cycling of mitochondrial Hsp70 at the protein import channel. Science, 300:139-41.
Lopez, N., Aron, R. and Craig, E.A. 2003. Specificity of the Class II Hsp40 Sis1 in maintenance of the yeast prion [RNQ+] Mol. Biol. Cell 14:1172-81.