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Editor - Dr. Xiao-Long Zhou | Chinese Academy of Sciences | 23869
ISSN: 2161-0436

Human Genetics & Embryology
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Dr. Xiao-Long Zhou

Dr. Xiao-Long Zhou Associate Professor Vice Group Leader SIBCB, CAS China
Chinese Academy of Sciences


I am currently an Associate Professor of Biochemistry and Molecular Biology in Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences. My research is primarily dedicated to study protein synthesis and translational quality control. I have investigated molecular mechanism of protein synthesis and its quality control mediated by aminoacyl-tRNA synthetases from various species and their connections to human diseases. I was awarded multiple titles such as Lu Jia-Xi Young Scientist Award of Chinese Academy of Sciences (CAS), Sanofi-SIBS Young Faculty Award, Member and Excellent Member of the Youth Innovation Promotion Association of CAS, Shanghai Rising-Star Award

Research Interest

Aminoacyl-tRNA synthetases (aaRSs) are a group of ancient enzymes and essential components to establish the genetic code. They catalyze the aminoacylation reaction to yield aminoacyl-tRNAs, which are then transported to the ribosome for protein biosynthesis. Aminoacylation of tRNAs requires adequate efficiency and accuracy, which means that the speed of the aa-tRNA production for the ribosome and the risk of generation of wrong aa-tRNA pairs should be carefully controlled and balanced. However, the presence of various types of amino acids and their analogues, and the fact that amino acids only differ in the side chain, greatly challenge the specificity of aaRSs. Therefore, editing activity is evolved in half of the present-day aaRSs to remove any potential produced aa-AMP (pre-transfer editing) and/or aa-tRNA (post-transfer editing) and is an essential checkpoint to ensure the translational quality control (fidelity). Aminoacylation and editing reactions catalyzed by aaRSs are highly significant and directly associated with organismal dysfunctions and diseases. Furthermore, because of wide distribution and divergence of aaRS, editing reaction or domain of aaRSs has been a hot target for designing and developing small aaRS-directed inhibitors for disease treatment. I mainly use biochemical and genetic approaches to investigate translational fidelity mechanism of aaRSs; the non-canonical functions of aaRSs; pathological mechanism of gene mutations in tRNA and aaRS genes; post-transcriptional modification mechanism of tRNA. Therefore, such studies, on one side, could improve our knowledge of mechanism of aminoacylation and editing; and on another side, reveal some aminoacylation/editing-related cellular dysfunctions and provide basis for drug design and development.
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