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Ruiming Xu, Ph.D, Prof.

Principal Investigator

National Laboratory of Biomacromolecules, IBP

Structural studies of gene expression and regulation

E-mail:rmxu@ibp.ac.cn,Tel:010-64888797

Fax:010-64888023,Zip code:100101

Chinese personal homepage, Personal group site 

Biography & Introduction

1980 - 1984     Zhejiang University, China, B.Sc. in Physics

1984 - 1989  Brandeis University, USA, M.A. (1985) & Ph.D. (1990) in Physics

1989 - 1991  Postdoctoral Fellow, Physics Department, University of Texas at Austin

1991 - 1993  Postdoctoral Associate, Physics Department, SUNY at Stony Brook

1993 - 1996  Visiting Scientist and Staff Associate, Cold Spring Harbor Laboratory

1996 - 2005  Assistant, Associate, and full Professor, Cold Spring Harbor Laboratory

2006 - 2008  Professor, Skirball Institute of Biomolecular Medicine & Department of Pharmacology, New York University School of Medicine

2008 - present  Investigator & Great Wall Professor, Institute of Biophysics, Chinese Academy of Sciences

2016 - present  Professor, University of the Chinese Academy of Sciences (UCAS)

Present: Director designate (since 2008), National Laboratory of Protein Science; Director (since 2011), National laboratory of Biomacromolecules; Deputy Director (since Dec. 2015), Institute of Biophysics, CAS.

Research Interest

The main research focus of our group is on structural studies of gene expression and regulation. Two themes of investigation include epigenetic control of gene transcription and mRNA processing:

1. Epigenetic control of gene expression

Epigenetic phenomena are stable inheritance of gene expression patterns controlled by higher order chromatin structure that depends on covalent modifications of DNA and histones. Epigenetic control of gene expression plays important roles in many biological processes, such as in cell type specifications during development, as well as in the development of many environment and age related diseases, such as cancer and diabetes. Our research in this area includes structural and functional studies of the catalytic mechanisms of histone modification enzymes, their substrate specificity, the mechanisms by which the enzymatic activities are regulated, the structural basis for the recognition of modified histones, and the mechanism of establishment and maintenance of higher chromatin structure in general. The results of our study will provide important mechanistic insights into the function of epigenetic inheritance in cell differentiation, epigenetic reprogramming in somatic cloning and iPS techniques, epigenetic deregulation in cancer and aging, and the development of therapeutics targeting epigenetic regulators.

2. RNA processing and protein-RNA interaction

Post-transcriptional mRNA processing includes 5’-capping, splicing and poly-adenylation at the 3’ end. Our current research focuses on mRNA splicing, as most human genes are alternatively spliced, which results in multiple proteins from a single transcript, thus, greatly increased the complexity of the human proteome. RNA splicing is carried out by the spliceosome, which is a large, dynamic complex composed of more than a hundred proteins and several small nuclear RNAs. Our goal is to elucidate the structural basis for splice sites selection and the molecular mechanism of RNA splicing, which include protein-protein and protein-RNA interaction within the spliceosome, and the interaction between the spliceosome, splicing factors and mRNA. In addition, mRNA splicing is coupled to transcriptional regulation, and our interest also includes structural and functional studies of protein-protein and protein-RNA interactions coupling the two processes.

Selected Publications

1. Jin W.X., Wang Y., Liu C.P., Yang N., Jin M.L., Cong Y., Wang M.Z.*, Xu R.M.* (2016) Structural basis for snRNA recognition by the double WD40-repeat domain of Gemin5. Genes & Dev. 30, 2391-2403.

2. Fang Q.L., Chen P., Wang M.Z., Fang J.N., Yang N., Li G.H.*, Xu R.M.* (2016) Human cytomegalovirus IE1 protein alters the higher order chromatin structure by targeting the acidic patch of the nucleosome. eLife 5, e11911.

3. Yang N.*, Yu Z.Y., Hu M.L., Wang M.Z., Lehmann R.*, Xu R.M.* (2015) Structure of Drosophila Oskar reveals a novel RNA binding protein. Proc. Natl. Acad. Sci .USA 112, 11541-11546.

4. Cao D.F., Wang M.Z., Qiu X.Y., Liu D.X., Jiang H.L., Yang N.*, Xu R.M.* (2015) Structural basis for allosteric, substrate dependent stimulation of SIRT1 activity by resveratrol. Genes & Dev. 29, 1316-1325.

5. Zhou T., Xiong J., Wang M.Z., Yang N., Wong J., Zhu B., Xu R.M.* (2014) Structural basis for hydroxymethylcytosine recognition by the SRA domain of UHRF2. Mol. Cell 54, 879-886.

6. Yang D.X., Fang Q.L., Wang M.Z., Ren R., Wang H., He M., Sun Y.W., Yang N.*, Xu R.M.* (2013) Nα-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain. Nat. Struct. Mol. Biol. 20, 1116-1118.

7. Hsu H.C., Wang C.L., Wang M., Yang N., Chen Z., Sternglanz R.*, Xu R.M.* (2013) Structural basis for allosteric stimulation of Sir2 activity by Sir4 binding. Genes & Dev. 27, 64-73.

8. Liu C.P., Xiong C.Y., Wang M.Z., Yu Z.L., Yang N., Chen P., Zhang Z.G., Li G.H.*, Xu R.M.* (2012) Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX. Nat. Struct. Mol. Biol. 19, 1287-1292.

9. Yang N.*, Wang W.X., Wang Y., Wang M.Z., Zhao Q., Rao Z.H., Zhu B.*, Xu R.M.* (2012) Distinct mode of methyl-H3K4 recognition by tandem tudor-like domains of Spindlin1. Proc. Natl. Acad. Sci. USA 109, 17954-17959.

10. Lin P.C. and Xu R.M.* (2012) Structure and assembly of the SF3a splicing factor complex of U2 snRNP. EMBO J. 31, 1579-1590.

 

From Ruiming Xu, 2017-01-10 update

 

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Institute of Biophysics, CAS    Address: 15 Datun Road, Chaoyang District, Beijing, 100101, China
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