Sue Wickner and her coauthors MIchel Wright, Reed Wickner and Jerry Hurwitz published an early paper showing DNA replication in the test tube. They found that the bacterial virus or phage Phi X174 could be converted from single stranded to the double stranded replicative form in the test tube and that the reaction required the gene products of dnaC, dnaE, and dnaG genes of the phage. At NIH, her research has illuminated the action of proteins that utilize adenosine triphosphate energy in tiny machines to replicate DNA, remodel proteins, and break down proteins. She has been a major contributor to the understanding of molecular chaperones, proteins that regulate most cellular processes including replication and transcription and response to stress. Chaperones function to alter activity, refold as well as degrade proteins. Her citation from election to the National Academy of Sciences notes her most recent contributions to ATP-dependent chaperones for proteolysis, showing how they participate in stress responses by removing proteins that folded incorrectly and how they degrade regulatory proteins once their signals have been delivered. Since there are some human diseases that result from abnormally folded and/or aggregated proteins, these ATP-dependent chaperones are important in disease treatment development.
S. Wickner “DNA Replication Proteins of Escherichia coli.” Annu Review of Biochem.78: 1163-1191.
A. N. Kravats, S. M. Doyle, J.R. Hoskins, O.Genest, E, Doody, S. Wickner “Interaction of E. coli Hsp90 with DnaK involves the DnaJ binding region of DnaK. Journal of Molecular Biology429 :858-872.
O.Genest, M. Reidy, T.O. Street, J.R.Hoskins, J.L.Camberg, D.A.Agard, D.C. Masison, and S.Wickner “ Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast.” Mol. Cell. 49:464-473.
S. M. Doyle, O. Genest, and S. Wickner “Protein rescue from aggregates by powerful molecular chaperone machines.” Nat Rev Mol Cell Biol. 14: 617-629.
M. Miot. M. Reidy, S.M. Doyle, J.R. Hoskins, D.M. Johnston, O. Genest, M.C.Vitery, D.C. Masison, and S. Wickner “Species-specific collaboration of heat shock proteins 70 and 100 in thermotolerance and protein disaggregation. Proc. Natl. Acad. Sci. USA108 : 6915-6920.
O. Genest, J.R.Hoskins, J.L.Camberg, S.M.Doyle, and S. Wickner “Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling. Proc Natl Acad Sci U S A. 108:8206-11.
