Arthur L. Horwich
From Wikipedia, the free encyclopedia
| Authur L. Horwich | |
| Born | 1951 |
|---|---|
| Residence | United States |
| Nationality | American |
| Fields | Biologist |
| Institutions | Yale School of Medicine Howard Hughes Medical Institute |
| Alma mater | Brown University |
| Known for | uncovering chaperonin action |
| Notable awards | Hans Neurath Award, Protein Society (2001) Gairdner International Award (2004) Stein and Moore Award, Protein Society (2006) Wiley Prize in Biomedical Science (2007) Rosenstiel Award (2008) |
Arthur L. Horwich (born 1951) is an American biologist and Eugene Higgins Professor of Genetics and Pediatrics at Yale School of Medicine.[1][2] Horwich has also been a Howard Hughes Medical Institute investigator since 1990.[3] He uncovered chaperonin action in 1989.[4]
Contents |
[edit] Early years
Horwich was born in 1951. He grew up in Oak Park, west of Chicago.[5] In 1969, he entered Brown University as part of a new program that combined the undergraduate degree with medical school.[5] During medical school, Horwich studied fat cell metabolism in the laboratory of Dr. John Fain. He received his A.B. in biomedical sciences in 1972 and his M.D. in 1975.[1][3] He graduated as valedictorian of the first class to complete the combined program.[5] Horwich went on to do an internship and residency in pediatrics at Yale University. Midway through, Horwich was not sure about an entirely clinical future. After completing his residency, he joined the Salk Institute for Biological Studies in La Jolla, California for a postdoctoral position in molecular biology and virology.[5] At Salk, he worked in Walter Eckhart's laboratory alongside Tony Hunter and witnessed Hunter's discovery of tyrosine phosphorylation.[5] He credits this time with sharpening his skills as a scientist. He said, "Tony taught me the nuts and bolts of thinking about a problem."[5]
[edit] Research
In 1981, he moved back to New Haven, Connecticut for a postdoctoral fellowship at Yale University School of Medicine. He worked in the laboratory of Leon Rosenberg.
In 1984, he moved across the hall from Rosenberg's lab to start his own laboratory as an assistant professor in the department of genetics. He still collaborated with members of the Rosenberg laboratory, including Wayne Fenton. As an independent researcher, he asked whether the pathway that imported OTC in mammalian cells also could work in yeast. In 1987, during a genetic screen in yeast, Horwich and his colleagues stumbled across a protein folding function inside mitochondria. In the mutant strain, proteins entered mitochondria from the cytosol normally but then misfolded and aggregated. The gene affected encoded a 60 kDa protein that they named Hsp60 because it was mildly heat inducible. Hsp60 is found in an 850 kDa double ring assembly, each ring containing 7 copies of Hsp60. Such assemblies, known as chaperonins, also exist in other cellular compartments and are essential components, mediating protein folding under both heat shock and normal conditions. [6]
Since 1987, Horwich and his colleagues have been studying these molecules both in vivo and in vitro, with particular emphasis on the Hsp60 homologue in E. coli known as GroEL. They and others found early on that a chaperonin-mediated folding reaction can be reconstituted in a test tube, and that has enabled structural and functional studies that have begun to explain how chaperonins work.
[edit] Awards and honors
In 2003, Horwich was elected to the National Academy of Sciences. He received the 2004 Gairdner International Award "for his fundamental discoveries concerning chaperone assisted protein folding in the cell and its relevance to neurodegeneration".[7] He received the 2007 Wiley Prize in Biomedical Science jointly with Franz-Ulrich Hartl, Managing Director of the Max Planck Institute of Biochemistry, "for their significant contribution in protein folding".[8] He received the 2008 Lewis S. Rosenstiel Award for Distinguished Work in Basic Medical Science jointly with F. Ulrich Hartl "for their pioneering work in the field of protein-mediated protein folding".[9]
He has also received two Protein Society awards - the Hans Neurath Award in 2001 and the Stein and Moore Award in 2006.[10]
[edit] References
- ^ a b Arthur L. Horwich. Yale School of Medicine. Retrieved on 2008-03-18.
- ^ Form leads to function. Yale School of Medicine. Retrieved on 2008-01-24.
- ^ a b Arthur L. Horwich, M.D.. Howard Hughes Medical Institute. Retrieved on 2008-01-24.
- ^ Cheng, M.Y., Hartl, F.U., Martin, J., Pollock, R. A., Kalousek, F., Neupert, W., Hallberg, E. M., Hallberg, R. L. & Horwich, A. L. (February 16, 1989). "Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria". Nature 337: 620–625. doi:. PMID 2645524.
- ^ a b c d e f Tinsley H. Davis (2004). Biography of Arthur L. Horwich. The National Academy of Sciences, USA. Retrieved on 2008-01-24.
- ^ Cheng, M.Y., Pollock, R.A., Hendrick, J. P. & Horwich, A. L. (June 15, 1987). "Import and Processing of Human Ornithine Transcarbamoylase Precursor by Mitochondria from Saccharomyces cerevisiae". PNAS 84 (12): 4063–4067. The National Academy of Sciences, USA. doi:.
- ^ 2004 winners. The Gairdner Foundation. Retrieved on 2008-01-24.
- ^ Recipients Of 6th Annual Wiley Prize In Biomedical Sciences Announced By Wiley Foundation. Medical News Today (2007-02-02). Retrieved on 2008-01-24.
- ^ Award Winners 2008. Brandeis University. Retrieved on 2008-02-01.
- ^ Past Recipients. The Protein Society. Retrieved on 2008-02-01.
