Rujuan LiuAssistant Professor , PhD, Assistant Professor
School of Life Science and Technology
- 1999-2003, Anhui University, China, B.S.
- 2003-2009, Biochemistry and molecular biology, University of Science and technology of China, China, Ph.D.
- 2019-Now, School of Life Science and Technology, ShanghaiTech University, Assistant Professor (TENURE-TRACK)
- 2009-2019, Institute of Biochemistry and Cell Biology, CAS, China, Research Assistant Professor(2009-2011), Research Associate Professor(2011-2018), Research Professor(2018-2019)
- 2017-2017, The University of Chicago, USA, Visiting Scholar
- 2011-2012, European Molecular Biology Laboratory (EMBL), France, Visiting Scholar
RNA Modification/tRNA Biology
RNA molecules play a key role in all cellular processes. Chemical modifications expand RNA molecules from containing the standard four nucleotides Adenosine, Guanosine, Uridine and Cytidine to more than 130 modified nucleotides, which increase the complexity and flexibility of RNAs.In cells, transfer RNAs (tRNAs) are the heaviest modified RNA molecules. TRNA is the key molecule in the “adaptor hypothesis “proposed by Fransis Crick, its most classical function is involved in protein synthesis to ensure the decoding of genetic information. Although this core role of tRNAs has been identified for several decades, many fundamental questions remain to be answered in the tRNA field, such as the function and meaning of the existence of more than 100 different chemical modifications on tRNAs, and the mechanism of occurrences and regulation of these dynamic modifications. Furthermore, many tRNA and tRNA derived RNA fragments have been found to function as regulatory RNA, which play roles beyond protein translation in many physiological and pathological processes. What’s the role of chemical modifications on the coordination between the classical and nonclassical functions of tRNA? The defects of tRNA modifications and mutations of some tRNA modification enzymes are directly associated with various human diseases especially neurological development/degeneration diseases and metabolic disorders, however, little is known about the tRNA modification mechanism, and how modification defects lead to human diseases. Our lab is focus on the molecular mechanisms and biological functions of dynamic tRNA modifications by using tRNA-seq, CLIP-seq, LC-MS/MS, enzymatic assays, and other technologies of biochemistry, biophysics and cellular biology.
Representative Publications (*First Author, # Corresponding Author)
- 1. Zhang, Li-Sheng*; Xiong, Qing-Ping; Perez, Sonia Pena; Liu, Chang; Wei, Jiangbo; Le, Cassy; Zhang, Linda; Harada, Bryan T.; Dai, Qing; Feng, Xinran; Hao, Ziyang; Wang, Yuru; Dong, Xueyang; Hu, Lulu; Wang, En-Duo; Pan, Tao; Klungland, Arne; Liu, Ru-Juan#; He, Chuan#.ALKBH7-mediated demethylation regulates mitochondrial polycistronic RNA processing.NATURE CELL BIOLOGY. 2021. 23(7):684-+.
- 2. Hao Li*; Han Dong*; Beisi Xu*; Qing-Ping Xiong; Cai-Tao Li; Wen-Qing Yang; Jing Li; Zhi-Xuan Huang; Qi-Yu Zeng; En-Duo Wang#; Ru-Juan Liu#.A dual role of human tRNA methyltransferase hTrmt13 in regulating translation and transcription.THE EMBO JOURNAL. 01 Dec 2021.
- 3. Wen-Qing Yang*; Qing-Ping Xiong; Jian-Yang Ge; Hao Li; Wen-Yu Zhu; Yan Nie; Xiuying Lin; Daizhu Lv; Jing Li; Huan Lin; Ru-Juan Liu#.THUMPD3–TRMT112 is a m2G methyltransferase working on a broad range of tRNA substrates.NUCLEIC ACIDS RESEARCH. 20 Oct 2021. 49(20):1100-11919.
- 4. Jing Li*; Yan-Nan Wang; Bei-Si Xu; Ya-Ping Liu; Mi Zhou; Tao Long; Hao Li; Han Dong; Yan Nie; Peng R. Chen; En-Duo Wang#; Ru-Juan Liu#.Intellectual disability-associated gene ftsj1 is responsible for 2'-O-methylation of specific tRNAs.EMBO REPORTS. Jun 2020. -(-):-.
- 5. Huang, Zhi-Xuan*; Li, Jing; Xiong, Qing-Ping; Li, Hao; Wang, En-Duo#; Liu, Ru-Juan#.Position 34 of tRNA is a discriminative element for m5C38 modification by human DNMT2.NUCLEIC ACIDS RESEARCH. 06 Dec 2021. 49(22).
- 6. Ru-Juan Liu#*; Tao Long*; Hao Li*; JingHua Zhao; Jing Li; MingZhu Wang; Andrés Palencia; JinZhong Lin; Stephen Cusack; En-Duo Wang#.Molecular Basis of the Multifaceted Functions of Human leucyl-tRNA Synthetase in Protein Synthesis and Beyond.NUCLEIC ACIDS RESEARCH. 21 May 2020. 48(9):4946-4959.
- 7. Li, Jing*; Zhu, Wen-Yu; Yang, Wen-Qing; Li, Cai-Tao; Liu, Ru-Juan#.The occurrence order and cross-talk of different tRNA modifications.SCIENCE CHINA-LIFE SCIENCES. 2021.
- 8. Hao, Guiyun*; Li, Hao*; Yang, Fei; Dong, Duoling; Li, Zezhong; Ding, Yingying; Pan, Wei; Wang, Enduo#; Liu, Rujuan#; Zhou, Huchen#.Discovery of benzhydrol-oxaborole derivatives as Streptococcus pneumoniae leucyl-tRNA synthetase inhibitors.BIOORGANIC & MEDICINAL CHEMISTRY. Jan 2021. 29(115871):1-12.
- 9. Li, Jing*; Li, Hao; Long, Tao; Dong, Han; Wang, En-Duo#; Liu, Ru-Juan#.Archaeal NSUN6 catalyzes m(5)C72 modification on a wide-range of specific tRNAs.NUCLEIC ACIDS RESEARCH. 28 Feb 2019. 47(4):2041-2055.
- 10. Liu, Ru-Juan#*; Long, Tao*; Li, Jing; Li, Hao; Wang, En-Duo#.Structural basis for substrate binding and catalytic mechanism of a human RNA:m(5)C methyltransferase NSun6.NUCLEIC ACIDS RESEARCH. 20 Jun 2017. 45(11):6684-6697.
- 11. Long, Tao*; Li, Jing; Li, Hao; Zhou, Mi; Zhou, Xiao-Long; Liu, Ru-Juan#; Wang, En-Duo#.Sequence-specific and Shape-selective RNA Recognition by the Human RNA 5-Methylcytosine Methyltransferase NSun6.JOURNAL OF BIOLOGICAL CHEMISTRY. 11 Nov 2016. 291(46):24293-24303.
- 12. Zhou, Mi*; Long, Tao; Fang, Zhi-Peng; Zhou, Xiao-Long; Liu, Ru-Juan#; Wang, En-Duo.Identification of determinants for tRNA substrate recognition by Escherichia coli C/U34 2 '-O-methyltransferase.RNA BIOLOGY. 03 Aug 2015. 12(8):900-911.
- 13. Liu, Ru-Juan*; Long, Tao*; Zhou, Mi; Zhou, Xiao-Long; Wang, En-Duo#.tRNA recognition by a bacterial tRNA Xm32 modification enzyme from the SPOUT methyltransferase superfamily.NUCLEIC ACIDS RESEARCH. 03 Sep 2015. 43(15):7489-7503.
- 14. Liu, Ru-Juan*; Zhou, Mi*; Fang, Zhi-Peng; Wang, Meng; Zhou, Xiao-Long; Wang, En-Duo#.The tRNA recognition mechanism of the minimalist SPOUT methyltransferase, TrmL.NUCLEIC ACIDS RESEARCH. 2013. 41(16):7828-7842.