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Research Paper Discussed in this Talk
Cheng MY, Hartl FU, Martin J, Pollock RA, Kalousek F, Neupert W, Hallberg EM, Hallberg RL, Horwich AL. Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature. 1989 Feb16;337(6208):620-5.
Educator Resources (Educators only)
These questions and answers were designed to link the iBiology video to the research paper and for use as a classroom activity.
Prepared by Dr. Nathan H. Joh.
About this Talk
Dr. Horwich explains that his lab was studying the import and folding of mitochondrial proteins in yeast mutants when he, and his collaborator Ulrich Hartl, discovered Hsp 60, a mitochondrial matrix protein required for proper folding of imported proteins. Hsp60 was found to have homology with proteins from bacteria and plants leading to the discovery of the molecular chaperonin protein family and its role in protein folding.
This video is located in: iBioMagazine Issue 10
About the Speaker
Arthur Horwich is the Sterling Professor of Genetics and Professor of Pediatrics at Yale School of Medicine and a Howard Hughes Medical Institute Investigator. Using genetics, biochemistry and biophysics, his lab studies the mechanism of action of chaperonins and, more recently, the neurodegenerative diseases resulting from protein misfolding. Horwich has received the Lasker Award and The Shaw Prize, amongst other awards, and he is a member of the National Academy of Sciences.
- Arthur Horwich iBioSeminar: Chaperone-Assisted Protein Folding
- Jodi Nunnari iBioEducation Lecture: Mitochondria
- Susan Lindquist iBioSeminar: Protein Folding and Prions
- Peter Walter iBioEducation Discovery Talk: Unfolding the UPR