Karin Musier-Forsyth, an American biochemist, is an Ohio Eminent Scholar on the faculty of the Department of Chemistry & Biochemistry at Ohio State University. [1] Musier-Forsyth's research involves biochemical, biophysical and cell-based approaches to understand the interactions of proteins and RNAs involved in protein synthesis and viral replication, especially in HIV.
Musier-Forsyth was born in 1962 in Dover, NJ to Horst and Maria Musier, who immigrated to the United States from Germany in the 1950s. [2] Her family moved to St. Petersburg, Florida in 1967 and she grew up on the Isle of Capri in Treasure Island, Florida. Her extracurricular activities throughout elementary school, high school, and college included piano, dance, and gymnastics. She attended Eckerd College in St. Petersburg Florida and enjoyed a liberal arts education, study abroad opportunities in London, England and Vienna, Austria, and research experiences at Georgia Institute of Technology, as well as at Eckerd. She graduated in 1984 with a Bachelor of Science degree in Chemistry. In 1984, Musier-Forsyth enrolled in graduate school at Cornell University in Ithaca, NY in the Department of Chemistry. Gordon G. Hammes was her mentor and she received her Ph.D. in 1989. Musier-Forsyth met her husband, Craig Forsyth, [3] in graduate school and they were married in Ithaca, NY in 1988. They have one son, Nicholas, born in St. Paul, Minnesota in 2003..
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From 1989-92, Musier -Forsyth did research in the laboratory of Paul Schimmel at MIT as an American Cancer Society postdoctoral fellow. She was hired as an Assistant Professor in the Department of Chemistry at the University of Minnesota in 1993, where she was promoted to Associate Professor in 1998 and full Professor in 2003. In 2007 she was named an Ohio Eminent Scholar and became a Professor in the Department of Chemistry & Biochemistry at Ohio State University.
Musier-Forsyth has published over 100 peer-reviewed articles, and is known for her work on elucidating key protein:nucleic interactions involved in viral replication and in the translation of the genetic code. Her work has provided key insights into how the aminoacyl tRNA synthetases, the large family of enzymes involved in protein synthesis, attach the correct amino acids to tRNAs and contribute to the fidelity of protein translation. Her work has also provided fundamental insights into how retroviral replication involves host amino acyl tRNA synthetases and tRNAs. [9] [10] This work highlights potential areas for therapeutic intervention in treating or preventing viral infections. [11]
A world renowned biochemist, Musier-Forsyth is recognized not only for her science expertise but as an educator and mentor. She has lectured at a wide variety of universities around the world and is active in numerous scientific societies. She is a peer reviewer for scientific publications and government granting organizations. Her activities include the following:
A retrovirus is a type of virus that inserts a DNA copy of its RNA genome into the DNA of a host cell that it invades, thus changing the genome of that cell. After invading a host cell's cytoplasm, the virus uses its own reverse transcriptase enzyme to produce DNA from its RNA genome, the reverse of the usual pattern, thus retro (backward). The new DNA is then incorporated into the host cell genome by an integrase enzyme, at which point the retroviral DNA is referred to as a provirus. The host cell then treats the viral DNA as part of its own genome, transcribing and translating the viral genes along with the cell's own genes, producing the proteins required to assemble new copies of the virus. Many retroviruses cause serious diseases in humans, other mammals, and birds.
An aminoacyl-tRNA synthetase, also called tRNA-ligase, is an enzyme that attaches the appropriate amino acid onto its corresponding tRNA. It does so by catalyzing the transesterification of a specific cognate amino acid or its precursor to one of all its compatible cognate tRNAs to form an aminoacyl-tRNA. In humans, the 20 different types of aa-tRNA are made by the 20 different aminoacyl-tRNA synthetases, one for each amino acid of the genetic code.
Gammaretrovirus is a genus in the Retroviridae family. Example species are the murine leukemia virus and the feline leukemia virus. They cause various sarcomas, leukemias and immune deficiencies in mammals, reptiles and birds.
Group-specific antigen, or gag, is the polyprotein that contains the core structural proteins of an Ortervirus. It was named as such because scientists used to believe it was antigenic. Now it is known that it makes up the inner shell, not the envelope exposed outside. It makes up all the structural units of viral conformation and provides supportive framework for mature virion.
Env is a viral gene that encodes the protein forming the viral envelope. The expression of the env gene enables retroviruses to target and attach to specific cell types, and to infiltrate the target cell membrane.
This family represents the bovine leukaemia virus RNA encapsidation (packaging) signal, which is essential for efficient viral replication.
The retroviral psi packaging element, also known as the Ψ RNA packaging signal, is a cis-acting RNA element identified in the genomes of the retroviruses Human immunodeficiency virus (HIV) and Simian immunodeficiency virus (SIV). It is involved in regulating the essential process of packaging the retroviral RNA genome into the viral capsid during replication. The final virion contains a dimer of two identical unspliced copies of the viral genome.
HIV gag stem loop 3 (GSL3) is a secondary structural component of the Retroviral Psi packaging element, also known as the psi recognition element. This domain plays a major role in RNA packaging and is located the 5’ untranslated region of the unspliced HIV-1 genome. GSL3 is known to direct specific packaging of HIV-1 genomic RNA. While deletion of GSL3 leads to decreases in both viral RNA packaging and dimerization, mutagenic studies have shown that it does not eliminate encapsulation of retroviral RNA.
Elongation factor 1-delta is a protein that in humans is encoded by the EEF1D gene.
Tyrosine—tRNA ligase, also known as tyrosyl-tRNA synthetase is an enzyme that is encoded by the gene YARS. Tyrosine—tRNA ligase catalyzes the chemical reaction
Lysyl-tRNA synthetase is an enzyme that in humans is encoded by the KARS gene.
Bifunctional aminoacyl-tRNA synthetase is an enzyme that in humans is encoded by the EPRS gene.
Aspartyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the DARS gene.
Methionyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the MARS gene.
Isoleucyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the IARS1 gene.
In molecular biology, Tat is a protein that is encoded for by the tat gene in HIV-1. Tat is a regulatory protein that drastically enhances the efficiency of viral transcription. Tat stands for "Trans-Activator of Transcription". The protein consists of between 86 and 101 amino acids depending on the subtype. Tat vastly increases the level of transcription of the HIV dsDNA. Before Tat is present, a small number of RNA transcripts will be made, which allow the Tat protein to be produced. Tat then binds to cellular factors and mediates their phosphorylation, resulting in increased transcription of all HIV genes, providing a positive feedback cycle. This in turn allows HIV to have an explosive response once a threshold amount of Tat is produced, a useful tool for defeating the body's response.
Rev is a transactivating protein that is essential to the regulation of HIV-1 protein expression. A nuclear localization signal is encoded in the rev gene, which allows the Rev protein to be localized to the nucleus, where it is involved in the export of unspliced and incompletely spliced mRNAs. In the absence of Rev, mRNAs of the HIV-1 late (structural) genes are retained in the nucleus, preventing their translation.
Susan A. Martinis is an American biochemist. She has co-authored over 57 publications in peer reviewed journals and scientific book chapters. Her expertise is in protein:RNA interactions and aminoacyl tRNA synthetases. As of 2019, she is the Vice Chancellor for Research and Innovation at the University of Illinois at Urbana-Champaign.
Leslie J. Parent is an American microbiologist and immunologist currently professor and vice dean of the College of Medicine at Pennsylvania State University. She is an Elected Fellow of the American Association for the Advancement of Science and American Society for Microbiology.
Xiang-Lei Yang (杨湘磊) is a Chinese-born American molecular biologist. She is a professor at The Scripps Research Institute, located in La Jolla, California. Her work has contributed to the establishment of physiological importance of aminoacyl-tRNA synthetases beyond their classical role in supporting mRNA translation and their disordered processes that contribute to disease. She founded the Translation Machinery in Health and Disease Gordon Research Conference, an ongoing biannual international conference since 2015. She helped co-found aTyr Pharma, a Nasdaq-listed biotechnology company.