Shu Quan

Shu Quan

Principle Investigator

Fields of Study

Molecular chaperone assisted protein folding

Protein engineering

Activation mechanisms of histone H3K4 methyltransferases

Biography

     Dr. Quan received her B.S. degree in 2004 from Tsinghua University in China, and her Ph.D. degree in 2010 from University of Michigan in the United States under the guidance of Prof. James Bardwell. She was a postdoctoral fellow at University of Michigan and the Howard Hughes Medical Institute from 2010 to 2013. In 2013, Dr. Quan joined the State Key Laboratory of Bioreactor Engineering and School of Biotechnology in East China University of Science and Technology.

Research Interest

      Protein quality control and the maintenance of proteome homeostasis (known as proteostasis) are crucial for cellular and organismal health. Aberrant protein folding has now been recognized as the basis of many human diseases, including neurodegeneration, peripheral amyloidosis, cystic fibrosis, cancer and cardiovascular disease. Molecular chaperones constitute important components of the proteostasis maintenance network. Understanding the mechanisms by which molecular chaperones use to interact with their client proteins and reverse their aberrant folding states, as well as identifying ways to stabilize proteins in vivo are not only crucial for intervention with numerous currently incurable diseases, but also may reveal ways to restore proteostasis during the aging process.

      Research in my laboratory focuses on the stabilization of proteins in living organisms and on elucidating the mechanism of molecular chaperones. We hope to 1) develop a unique toolbox that can evaluate proteins stability in vivo and generate stabilized proteins suitable for both basic and translational research and to 2) gain insight into how molecular chaperones interact with their clients, as well as their roles in aging and disease. 3) use the protein stabilization platform to solve important questions, such as establishing the flexibility-activity relationship within the histone H3K4 methyltransferases, and elucidating the mechanisms for their activation. We use a combination of techniques in microbiology, biochemistry, biophysics, bioinformatics, and structural biology to achieve our goals.

Publication

1. Quan, S., Wang, L., Petrotchenko, E. V., Makepeace, K. A., Horowitz, S., Yang, J., Zhang, Y., Borchers, C. H., and Bardwell, J. C. (2014) Super Spy variants implicate flexibility in chaperone action. eLife 3, e01584

2. Quan, S., Hiniker, A., Collet, J. F., and Bardwell, J. C. (2013) Isolation of bacteria envelope proteins. Methods in molecular biology 966, 359-366

3. Quan, S.*, and Bardwell, J. C. (2012) Chaperone discovery. BioEssays : news and reviews in molecular, cellular and developmental biology 34, 973-981. *corresponding author

4. Quan, S., Koldewey, P., Tapley, T., Kirsch, N., Ruane, K. M., Pfizenmaier, J., Shi, R., Hofmann, S., Foit, L., Ren, G., Jakob, U., Xu, Z., Cygler, M., and Bardwell, J. C. (2011) Genetic selection designed to stabilize proteins uncovers a chaperone called Spy. Nature structural & molecular biology 18, 262-269

5. Evans, M. L., Schmidt, J. C., Ilbert, M., Doyle, S. M., Quan, S., Bardwell, J. C., Jakob, U., Wickner, S., and Chapman, M. R. (2011) E. coli chaperones DnaK, Hsp33 and Spy inhibit bacterial functional amyloid assembly. Prion 5, 323-334

6. Masip, L., Klein-Marcuschamer, D., Quan, S., Bardwell, J. C., and Georgiou, G. (2008) Laboratory evolution of Escherichia coli thioredoxin for enhanced catalysis of protein oxidation in the periplasm reveals a phylogenetically conserved substrate specificity determinant. The Journal of biological chemistry 283, 840-848

7. Chen, Y., Pan, X., Tang, Y., Quan, S., Tai, P. C., and Sui, S. F. (2008) Full-length Escherichia coli SecA dimerizes in a closed conformation in solution as determined by cryo-electron microscopy. The Journal of biological chemistry 283, 28783-28787

8. Quan, S., Schneider, I., Pan, J., Von Hacht, A., and Bardwell, J. C. (2007) The CXXC motif is more than a redox rheostat. The Journal of biological chemistry 282, 28823-28833

9. Chen, Y., Lu, Y. J., Wang, H. W., Quan, S., Chang, Z., and Sui, S. F. (2003) Two-dimensional crystallization of a small heat shock protein HSP16.3 on lipid layer. Biochemical and biophysical research communications 310, 360-366

Contact

Building 18, Room 1115, 130 Meilong Road, Shanghai, China, 200237

Tel: 86-21-64253924

E-mail: shuquan@ecust.edu.cn