Arthur L. Horwich | |
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| Born | 1951 (age 74–75) |
| Alma mater | Brown University |
| Known for | uncovering chaperonin action |
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| Scientific career | |
| Fields | Biology |
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| Notable students | Tapan K. Chaudhuri[1] |
Arthur L. Horwich (born 1951) is an Americanbiologist andSterling Professor of Genetics and Pediatrics at theYale School of Medicine.[2][3] Horwich has also been aHoward Hughes Medical Institute investigator since 1990.[4] His research intoprotein folding uncovered the action ofchaperonins, protein complexes that assist the folding of other proteins; Horwich first published this work in 1989.[5][6]
For his scientific work Horwich has been awarded theGairdner International Award (2004),Louisa Gross Horwitz Prize (2008),Lasker Award (2011),[7]Shaw Prize (2012),Albany Medical Center Prize (2016), andBreakthrough Prize (2020). He is a member of theNational Academy of Sciences and theAmerican Academy of Arts and Sciences.[8][9]
Horwich was born in 1951. He grew up inOak Park, west of Chicago.[10] In 1969, he enteredBrown University as part of a new program that combined the undergraduate degree with medical school.[10] During medical school, Horwich studied fat cell metabolism in the laboratory of John Fain. Horwich received hisA.B. in biomedical sciences in 1972 and hisM.D. in 1975.[2][4] He graduated as valedictorian of the first class to complete the combined program.[10] Horwich went on to do an internship and residency in pediatrics atYale University. Midway through, Horwich was not sure about an entirely clinical future. After completing his residency, he joined theSalk Institute for Biological Studies inLa Jolla, California for a postdoctoral position in molecular biology and virology.[10] At Salk, he worked in Walter Eckhart's laboratory alongsideTony Hunter and witnessed Hunter's discovery of tyrosine phosphorylation.[10] 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."[10]
In 1981, Horwich moved back toNew Haven, Connecticut for a postdoctoral fellowship atYale University School of Medicine. He worked in the laboratory of Leon Rosenberg.[11]
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, Horwich asked whether the pathway that imports an enzyme calledornithine transcarbamylase (OTC) into themitochondria of 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 insidemitochondria. In the mutant strain, proteins entered mitochondria from thecytosol normally but then misfolded and aggregated. They named the protein encoded by the affected geneHSP60, Heat shock protein 60, because it has a mass of 60 kDa and is produced in larger quantity in response to heat. 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.[12]
Since 1987, Horwich and his colleagues have been studying these molecules both invivo andin vitro, with particular emphasis on the Hsp60 homologue inE. 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.
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