- In full:
- Susan Lee Lindquist
- Née:
- Susan McKenzie
- Born:
- June 5, 1949, Chicago, Illinois, U.S.
- Died:
- October 27, 2016, Cambridge, Massachusetts (aged 67)
- Awards And Honors:
- National Medal of Science (2009)
- Subjects Of Study:
- RNA splicing
- eukaryote
- gene regulation
- heat-shock protein
- prion
- protein
- yeast
Susan L. Lindquist
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Who was Susan L. Lindquist?
Susan L. Lindquist (1949–2016) was an American molecular biologist renowned for her groundbreaking discoveries in protein folding and prions. Her work with heat-shock proteins in organisms like fruit flies and yeast revealed their role in regulating RNA and restoring protein homeostasis after stress, providing insights into gene regulation in eukaryotic cells.
Lindquist's prion research uncovered non-genetic inheritance and evolution mechanisms. She found that yeast prions, unlike those causing animal diseases, are inherited without genetic changes, exposing hidden genetic variation for adaptation. Later, she explored mammalian brain prions, suggesting their role in memory storage and investigating amyloid's role in neurodegenerative diseases like Alzheimer's and Parkinson's.
She was an investigator at the Howard Hughes Medical Institute and a member of the National Academy of Sciences and the American Academy of Arts and Sciences.
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What field of science did Susan L. Lindquist work in?
Susan L. Lindquist was an American molecular biologist who worked in the field of molecular biology. Her work led to key discoveries concerning protein folding and prions, which are misfolded proteins that can pass inherited traits to offspring in yeast.
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What were some of Susan Lindquist's main research interests?
Susan L. Lindquist was an American molecular biologist whose research primarily focused on protein folding and prions. She explored heat-shock proteins in organisms like fruit flies, yeast, and flowering plants, revealing their role in regulating RNA splicing and transport and in restoring protein homeostasis after stress. Lindquist discovered that inherited traits could be passed to offspring via misfolded proteins known as prions. Her work also shed light on how yeast adapts and evolves in response to environmental changes, influencing her investigations into the cellular mechanisms driving cancer progression.
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What is protein folding, and why was it important in Lindquist's research?
Protein folding is the process by which a protein molecule assumes its functional three-dimensional shape. This process is essential because a protein's shape determines its function.
Susan L. Lindquist made key discoveries concerning protein folding. Her research on heat-shock proteins, which are produced when cells are exposed to increased temperatures, led to major discoveries about prions, misfolded proteins that can transmit inherited traits in yeast. Lindquist found that these prions could expose hidden genetic variations, allowing yeast to adapt and evolve. She later applied this knowledge to the study of cancer and neurodegenerative diseases such as Alzheimer's and Parkinson's.
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How did Susan Lindquist's discoveries help our understanding of diseases?
Susan Lindquist's research provided significant insights into disease mechanisms, especially concerning protein folding and prions. Her work with heat-shock proteins revealed how cells restore protein homeostasis after stress, which is crucial for understanding cellular responses to damage. Lindquist discovered that yeast prions, unlike those that cause disease, can expose hidden genetic variations, aiding adaptation and evolution.
Later, her investigations into mammalian brain prions and amyloid proteins led to the identification of a yeast protein capable of breaking down amyloid, offering potential therapeutic avenues for neurodegenerative diseases like Alzheimer's and Parkinson's.
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What awards or recognition did Susan L. Lindquist receive for her scientific work?
Susan L. Lindquist (1949–2016) was an American molecular biologist known for her discoveries about protein folding and prions.
Lindquist was a Howard Hughes Medical Institute investigator and a member of the American Academy of Arts and Sciences (1996) and the National Academy of Sciences (1997). She received several awards, including the National Medal of Science (2009), the Max Delbrück Medal (2010), and the Mendel Medal (2010).
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Susan L. Lindquist (born June 5, 1949, Chicago, Illinois, U.S.—died October 27, 2016, Cambridge, Massachusetts) was an American molecular biologist who made key discoveries concerning protein folding and who was among the first to discover that in yeast, inherited traits can be passed to offspring via misfolded proteins known as prions.
Lindquist received a bachelor’s degree (1971) in microbiology from the University of Illinois at Urbana-Champaign and a doctorate (1976) in biology from Harvard University. She then became a postdoctoral researcher at the University of Chicago, where she later joined the faculty (1978) of the department of molecular genetics and cell biology. She remained there until 2001, when she became a professor in the department of biology at the Massachusetts Institute of Technology (MIT). From 2001 to 2004, she served as director of the MIT-affiliated Whitehead Institute for Biomedical Research.
While working as a graduate student at Harvard in the laboratory of American molecular biologist Matthew Stanley Meselson, Lindquist learned of heat-shock proteins—proteins synthesized rapidly and in large quantities following cellular exposure to sudden increases in temperature. Throughout the 1980s and ’90s, Lindquist explored heat-shock proteins in various model organisms, including the fruit fly Drosophila melanogaster, the yeast Saccharomyces cerevisiae, and the flowering plant Arabidopsis thaliana. Her studies revealed that heat-shock proteins directly regulate RNA splicing (the removal of introns from messenger RNA), RNA transport across the nuclear membrane, and RNA degradation in order to prevent new RNA transcripts from being processed while the cell is under stress. Lindquist and colleagues concluded that those activities reset the cell’s damaged regulatory systems and thereby restore protein homeostatis following stress. Once the cell resets, the heat-shock response is turned off. Lindquist’s characterization of that process was groundbreaking, providing scientists with what was then the most complete example of gene regulation for eukaryotic cells (cells possessing a clearly defined nucleus).
In the mid-1990s, Lindquist’s research on heat-shock proteins led her to several major discoveries about prions that shed light on nongenetic mechanisms of inheritance and evolution. In 1995, for example, she and colleagues reported that a heat-shock protein known as Hsp104 was required for the production of a yeast protein called [PSI+], which was thought to be prionlike. The following year, she published evidence indicating that [PSI+] was in fact a prionlike aggregate of a conformationally altered cellular protein, that it was cytoplasmically inherited in yeast, and that it modified and triggered the aggregation of newly formed proteins of the same kind. She also found that yeast prions do not cause disease in their host, are inherited without changes in genotype (genetic constitution), and expose hidden genetic variation, giving rise to new phenotypes (observable traits) that enable yeast to adapt and evolve in response to environmental change. Lindquist subsequently applied that knowledge to investigations of the cellular mechanisms driving cancer progression, since cancer cells are also able to adapt and mutate rapidly in response to environmental factors.
Lindquist later investigated prions and prionlike proteins found in the mammalian brain. Working with Austrian-born American neurobiologist and Nobelist Eric Kandel, she discovered a neuronal protein that could be converted naturally to a prionlike state and hypothesized that the prion form maintained changes at synapses (neuronal junctions) required for memory storage. She also studied a protein known as amyloid to determine its role in memory and inheritance. That work led to her discovery of a yeast protein capable of breaking down amyloid—a discovery that opened up new avenues of research into the development of treatments for neurodegenerative conditions such as Alzheimer disease and Parkinson disease, which are associated with the formation of abnormal amyloid aggregates.
Lindquist was a Howard Hughes Medical Institute investigator and was elected to membership in multiple organizations, including the American Academy of Arts and Sciences (1996) and the National Academy of Sciences (1997). She also received a number of awards, including the National Medal of Science (2009), the Max Delbrück Medal (2010), and the Mendel Medal (2010).