Abstract

This project concentrates on prokaryote and eukaryote aminoacyl tRNA synthetases, enzymes which establish the rules of the genetic code by matching amino acids with trinucleotide sequences (contained within transfer RNA molecules). There are four components to the program: 1) Investigation of a covalent component to protein-nucleic acid (synthetase-transfer RNA) interactions; 2) Primary structures of and structure-function relationships between aminoacyl tRNA synthetases; 3) Synthesis of and structural relationships between mitochondrial and cytoplasmic forms of synthetases (in a eukaryote) which are specific for the same amino acid; 4) Regulation of aminoacyl tRNA synthetase biosynthesis.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM015539-19
Application #
3268785
Study Section
Physiological Chemistry Study Section (PC)
Project Start
1979-06-01
Project End
1989-05-31
Budget Start
1986-06-01
Budget End
1987-05-31
Support Year
19
Fiscal Year
1986
Total Cost
Indirect Cost

  Institution

Name
Massachusetts Institute of Technology
Department
Type
Schools of Arts and Sciences
DUNS #
City
Cambridge
State
MA
Country
United States
Zip Code
02139

  Publications

Chong, Yeeting E; Guo, Min; Yang, Xiang-Lei et al. (2018) Distinct ways of G:U recognition by conserved tRNA binding motifs. Proc Natl Acad Sci U S A 115:7527-7532
Naganuma, Masahiro; Sekine, Shun-ichi; Chong, Yeeting Esther et al. (2014) The selective tRNA aminoacylation mechanism based on a single G•U pair. Nature 510:507-11
Klipcan, Liron; Safro, Mark; Schimmel, Paul (2013) Anticodon G recognition by tRNA synthetases mimics the tRNA core. Trends Biochem Sci 38:229-32
Zhou, Huihao; Sun, Litao; Yang, Xiang-Lei et al. (2013) ATP-directed capture of bioactive herbal-based medicine on human tRNA synthetase. Nature 494:121-4
Sajish, Mathew; Zhou, Quansheng; Kishi, Shuji et al. (2012) Trp-tRNA synthetase bridges DNA-PKcs to PARP-1 to link IFN-? and p53 signaling. Nat Chem Biol 8:547-54
Lee, Peter S; Zhang, Hui-Min; Marshall, Alan G et al. (2012) Uncovering of a short internal peptide activates a tRNA synthetase procytokine. J Biol Chem 287:20504-8
Xu, Zhiwen; Wei, Zhiyi; Zhou, Jie J et al. (2012) Internally deleted human tRNA synthetase suggests evolutionary pressure for repurposing. Structure 20:1470-7
Park, Min Chul; Kang, Taehee; Jin, Da et al. (2012) Secreted human glycyl-tRNA synthetase implicated in defense against ERK-activated tumorigenesis. Proc Natl Acad Sci U S A 109:E640-7
Guo, Min; Schimmel, Paul (2012) Structural analyses clarify the complex control of mistranslation by tRNA synthetases. Curr Opin Struct Biol 22:119-26
Wang, Jing; Fang, Pengfei; Schimmel, Paul et al. (2012) Side chain independent recognition of aminoacyl adenylates by the Hint1 transcription suppressor. J Phys Chem B 116:6798-805

Showing the most recent 10 out of 83 publications