- PhD, 1966, MIT
Research SummaryPaul Schimmel’s research interests have focused on aminoacyl tRNA synthetases — an ancient and universal set of essential enzymes. His laboratory has worked on a universal mechanism for correcting errors in the interpretation of genetic information, and went on to show how this mechanism is essential for maintaining cellular homeostasis and preventing serious pathologies and disease. His laboratory also discovered what others refer to as a ‘tRNA synthetase-directed primordial’ or ‘second’ genetic code, which was eventually incorporated into the modern code. In a separate line of research published back in 1983, Schimmel developed the concept of what are now known as ESTs (expressed sequence tags), and the strategy of shotgun sequencing — approaches that were adopted into the human genome project several years later. Lastly, his laboratory connected synthetases to disease and, most recently, they reported the structural and functional metamorphosis of these proteins, whereby they are repurposed with novel activities, both inside and outside the cell, in a variety of cell signaling pathways. The Schimmel lab is no longer accepting students.
- Member of the American Academy of Arts and Sciences
- Member of the National Academy of Sciences
- Member of the American Philosophical Society
- Member of the Institute of Medicine (National Academy of Medicine)
- Member of the National Academy of Inventors
- Former President of the Division of Biological Chemistry of the American Chemical Society
- Editorial board member on numerous scientific journals
- Relaxed sequence constraints favor mutational freedom in idiosyncratic metazoan mitochondrial tRNAs. Kuhle, B, Chihade, J, Schimmel, P. 2020. Nat Commun 11, 969.
- Serum-circulating His-tRNA synthetase inhibits organ-targeted immune responses. Adams, RA, Fernandes-Cerqueira, C, Notarnicola, A, Mertsching, E, Xu, Z, Lo, WS, Ogilvie, K, Chiang, KP, Ampudia, J, Rosengren, S et al.. 2019. Cell. Mol. Immunol. , .
- Tyrosyl-tRNA synthetase stimulates thrombopoietin-independent hematopoiesis accelerating recovery from thrombocytopenia. Kanaji, T, Vo, MN, Kanaji, S, Zarpellon, A, Shapiro, R, Morodomi, Y, Yuzuriha, A, Eto, K, Belani, R, Do, MH et al.. 2018. Proc. Natl. Acad. Sci. U.S.A. 115, E8228-E8235.
- Bi-allelic Mutations in Phe-tRNA Synthetase Associated with a Multi-system Pulmonary Disease Support Non-translational Function. Xu, Z, Lo, WS, Beck, DB, Schuch, LA, Oláhová, M, Kopajtich, R, Chong, YE, Alston, CL, Seidl, E, Zhai, L et al.. 2018. Am. J. Hum. Genet. 103, 100-114.
- Distinct ways of G:U recognition by conserved tRNA binding motifs. Chong, YE, Guo, M, Yang, XL, Kuhle, B, Naganuma, M, Sekine, SI, Yokoyama, S, Schimmel, P. 2018. Proc. Natl. Acad. Sci. U.S.A. 115, 7527-7532.
- Publisher Correction: Double mimicry evades tRNA synthetase editing by toxic vegetable-sourced non-proteinogenic amino acid. Song, Y, Zhou, H, Vo, MN, Shi, Y, Nawaz, MH, Vargas-Rodriguez, O, Diedrich, JK, Yates, JR 3rd, Kishi, S, Musier-Forsyth, K et al.. 2018. Nat Commun 9, 1113.
- Double mimicry evades tRNA synthetase editing by toxic vegetable-sourced non-proteinogenic amino acid. Song, Y, Zhou, H, Vo, MN, Shi, Y, Nawaz, MH, Vargas-Rodriguez, O, Diedrich, JK, Yates, JR, Kishi, S, Musier-Forsyth, K et al.. 2017. Nat Commun 8, 2281.
- The emerging complexity of the tRNA world: mammalian tRNAs beyond protein synthesis. Schimmel, P. 2018. Nat. Rev. Mol. Cell Biol. 19, 45-58.
- Two crystal structures reveal design for repurposing the C-Ala domain of human AlaRS. Sun, L, Song, Y, Blocquel, D, Yang, XL, Schimmel, P. 2016. Proc. Natl. Acad. Sci. U.S.A. 113, 14300-14305.
- p53-Dependent DNA damage response sensitive to editing-defective tRNA synthetase in zebrafish. Song, Y, Shi, Y, Carland, TM, Lian, S, Sasaki, T, Schork, NJ, Head, SR, Kishi, S, Schimmel, P. 2016. Proc. Natl. Acad. Sci. U.S.A. 113, 8460-5.