A5026856074- RNA and protein synthesis mechanisms
- RNA modifications and cancer
- RNA Research and Splicing
- Genomics and Phylogenetic Studies
- Bacterial Genetics and Biotechnology
- DNA and Nucleic Acid Chemistry
- Enzyme Structure and Function
- Chemical Synthesis and Analysis
- Protein Structure and Dynamics
- RNA regulation and disease
- Advanced biosensing and bioanalysis techniques
- CRISPR and Genetic Engineering
- Biochemical and Molecular Research
- Mass Spectrometry Techniques and Applications
- Machine Learning in Bioinformatics
- Bacteriophages and microbial interactions
- Genomics and Chromatin Dynamics
- Antimicrobial Peptides and Activities
- Fungal and yeast genetics research
- Mitochondrial Function and Pathology
- ATP Synthase and ATPases Research
- Metabolism and Genetic Disorders
- Hereditary Neurological Disorders
- Cell Adhesion Molecules Research
- Plant biochemistry and biosynthesis
Scripps Research Institute
2016-2025
University of Florida
2005-2023
Scripps (United States)
2013-2023
Scripps Institution of Oceanography
2023
John D. and Catherine T. MacArthur Foundation
2023
Scripps Laboratories (United States)
2013-2022
Child Trends
2010-2018
Hong Kong University of Science and Technology
2012-2018
University of Hong Kong
2012-2018
Yale University
1997-2015
Aminoacyl-tRNA synthetases catalyze aminoacylation of transfer RNAs (tRNAs). It is shown that human tyrosyl-tRNA synthetase can be split into two fragments with distinct cytokine activities. The endothelial monocyte–activating polypeptide II–like carboxy-terminal domain has potent leukocyte and monocyte chemotaxis activity stimulates production myeloperoxidase, tumor necrosis factor-α, tissue factor. catalytic amino-terminal binds to the interleukin-8 type A receptor functions as an...
In higher eukaryotes, transfer RNAs (tRNAs) with the same anticodon are encoded by multiple nuclear genes, and little is known about how mutations in these genes affect translation cellular homeostasis. Similarly, surveillance systems that respond to such defects eukaryotes not clear. Here, we discover loss of GTPBP2, a novel binding partner ribosome recycling protein Pelota, mice mutation tRNA gene specifically expressed central nervous system causes stalling widespread neurodegeneration....
High-fidelity transfers of genetic information in the central dogma can be achieved by a reaction called editing. The crystal structure an enzyme with editing activity translation is presented here at 2.5 angstroms resolution. enzyme, isoleucyl–transfer RNA synthetase, activates not only cognate substrate l -isoleucine but also minimally distinct -valine first, aminoacylation step. Then, second, “editing” step, synthetase itself rapidly hydrolyzes valylated products. For this two-step...
Few and limited amino acid sequence homologies have been found among eight bacterial aminoacyl transfer RNA (tRNA) synthetases whose primary structures are known. The entire 939-amino structure of Escherichia coli isoleucyl-tRNA synthetase is now reported. In a 11 consecutive acids matching in E. methionyl-tRNA synthetase, there ten identical residues one conservative change. This the strongest homology recorded between any two tRNA synthetases. part methionine enzyme's three-dimensional has...
Aminoacyl-tRNA synthetases catalyze the first step of protein synthesis. It was shown recently that human tyrosyl-tRNA synthetase (TyrRS) can be split into two fragments having distinct cytokine activities, thereby linking synthesis to signaling pathways. Tryptophanyl-tRNA (TrpRS) is a close homologue TyrRS. A natural fragment, herein designated as mini TrpRS, by others produced alternative splicing. Production this fragment reported stimulated IFN-γ, also stimulates production angiostatic...
Abstract The mischarged species Val-tRNAile and Phe-tRNAile (both Escherichia coli B) were enzymatically synthesized in a heterologous aminoacylation system under special reaction conditions. When mixed with isoleucyl-tRNA synthetase the absence of AMP or PPi, is very rapidly deacylated at pH 7, 5 mm Mg2+, 15°. On other hand, does not deacylate Phe-tRNAile. Isoleucyl-tRNA can form valyl adenylate (Val-AMP) from valine ATP, but synthetase-bound Val-AMP hydrolyzed when confronted tRNAile...