General
   

Research Areas

   
Structure and Function of Photosynthetic Complexes
Our research focuses on the regulation of carbon assimilation in algae and crop. In particular, the regulation of carbon fixation enzyme Rubisco is hindered by the incomprehension of biogenesis pathways. Prokaryotic hexadecameric Rubisco is reconstituted in vitro by the sequential assistance of folding chaperonin and assembly chaperone, pointing to the complex biogenesis pathway in both prokaryotic and eukaryotic organisms. Research goals include identification of factors involved in the biogenesis of eukaryotic Rubisco, reconstitution of Rubisco with chaperones and regulation of Rubisco in algae and plants. Another study aims to analyse the enzymes involved in the Calvin cycles from common wheat. The research goal is to create high active enzyme after comparing the enzyme activities among copies, varieties and species and check the growth effect after transfer the created genes into plants.

Education

   
University Education
Ph. D. University of Freiburg, Germany; M. S. Nankai University; B. S. nner Mongolia University

Experience

   
Work Experience
2011-Now:Group leader in Institute of Genetics and Developmental Biology, Chinese Academy of Sciences; 2006-2010:Postdoctor in the group of Prof. F. U. Hartl, Department of Cellular Biochemistry, Max-Planck-Institute of Biochemistry

Publications

   
Papers

(1)     Zhao, Q., Zhang, X., Sommer, F., Ta, N., Wang, N., Schroda, M., Cong, Y., Liu, C. (2019). Hetero-oligomeric CPN60 resembles highly symmetric group I chaperonin structure revealed by Cryo-EM. Plant J 98:798-812.

(2)     Gao, F., Chen, B., Jiao, J., Jia, L., Liu, C. (2017). Two Novel Vesicle-Inducing Proteins in Plastids 1 Genes Cloned and Characterized in Triticum urartu. PLoS One 12: e0170439.

(3)     Liang, Z., Chen, K., Li, T., Zhang, Y., Wang, Y., Zhao, Q., Liu, J., Zhang, H., Liu, C., Ran, Y., Gao, C. (2017). Efficient DNA-free genome editing of bread wheat using CRISPR/Cas9 ribonucleoprotein complexes. Nat Commun 8: 14261.

(4)     Li, W., Zhang, F., Wu, R., Jia, L., Li, G., Guo, Y., Liu, C. and Wang, G.(2017). A novel N-methyltransferase in Arabidopsis appears to feed a conserved pathway for nicotinate detoxification among land plants and is associated with lignin biosynthesis. Plant Physiol 174: 1492-1504. 

(5)     Zhao, Q., and Liu, C. (2017). Chloroplast Chaperonin: An Intricate Protein Folding Machine for Photosynthesis. Front Mol Biosci 4:98.

(6)     Zhang, S., Zhou, H., Yu. F., Bai, C., Zhao, Q., He, J. and Liu, C. (2016) Structural insight into the cooperation of chloroplast chaperonin subunits. BMC Biology 14:29.

(7)     Zhang, S., Zhou, H., Yu. F., Gao, F., He, J. and Liu, C. (2016) The functional partition of Cpn60α and Cpn60β subunits in substrates recognition and cooperation with cochaperonin. Mol Plant 9(8):1210-13.

(8)     Xu, Y., Jin, W., Li, Na., Zhang, W., Liu, C., Li, C. and Li, Y. (2016) UBIQUITIN-SPECIFIC PROTEASE 14 interacts with ULTRAVIOLET-B INSENSITIVE 4 to regulate endoreduplication and cell and organ growth in Arabidopsis. Plant Cell 28(5):1200-1214.

(9)     Bai, C., Guo, P., Zhao, Q., Lv, Z., Zhang, S., Gao, F., Gao, L., Wang, Y., Tian, Z., Wang, J., Yang, F. and Liu C. (2015) Protomer Roles in Chloroplast Chaperonin Assembly and Function. Mol Plant 8: 1478-92.

(10) Guo, P., Jiang, S., Bai, C., Zhang, W., Zhao, Q. and Liu, C. (2015) Asymmetric functional interaction between chaperonin and its plastidic cofactors. FEBS J 282: 3959-70.

(11) Gao, F., Wang, W., Zhang, W. and Liu, C. (2015) alpha-Helical Domains Affecting the Oligomerization of Vipp1 and Its Interaction with Hsp70/DnaK in Chlamydomonas. Biochemistry 54: 4877-89.

(12) Bracher, A., Hauser, T., Liu, C., Hartl, F. U. and Hayer-Hartl, M. (2015) Structural Analysis of the Rubisco-Assembly Chaperone RbcX-II from Chlamydomonas reinhardtii. PLoS One 10: e0135448.

(13) Fang, C., Li, C., Li, W., Wang, Z., Zhou, Z., Shen, Y., Wu, M., Wu, Y., Li, G., Kong, L. A., Liu, C., Jackson, S. A. and Tian, Z. (2014) Concerted evolution of D1 and D2 to regulate chlorophyll degradation in soybean. Plant J 77: 700-12.

(14) Liu, C., Young, A. L., Starling-Windhof, A., Bracher, A., Saschenbrecker, S., Rao, B. V., Rao, K. V., Berninghausen, O., Mielke, T., Hartl, F. U., Beckmann, R. and Hayer-Hartl, M. (2010) Coupled chaperone action in folding and assembly of hexadecameric Rubisco. Nature 463(7278):197-202.

(15) Liu, C., Willmund, F., Golecki, J. R., Cacace, S., Hess, B., Markert, C. and Schroda, M. (2007) The chloroplast HSP70B-CDJ2-CGE1 chaperones catalyze assembly and disassembly of VIPP1 oligomers in Chlamydomonas. Plant J 50, 265–277.

(16) Liu, C., Willmund, F., Whitelegge, J. P., Hawat, S., Knapp, B., Lodha, M. and Schroda, M. (2005) J-domain protein CDJ2 and HSP70B are a plastidic chaperone pair that interacts with vesicle inducing protein in plastids 1 (VIPP1). Mol Biol Cell 16: 1165-1177.

 


Research Interests

Biogenesis and Regulation of Rubisco
Rubisco (Ribulose-1,5-bisphosphate carboxylase/oxygenase), an enzyme catalyzed the rate limiting step of carbon assimilation, is infamous for its sluggish kinetics which have resulted in it being the world’s most abundant protein. The significant plasticity in the catalytic properties of natural Rubiscos suggests the changes can be introduced to generate better Rubisco. But the genetic manipulation of Rubisco has been hampered by the unclear of its biogenesis pathway. Our aim is to understand the regulation of the carbon fixation enzyme Rubisco, an undertaking that requires further understanding of its biogenesis. Active prokaryotic hexadecameric Rubisco is reconstituted in vitro via the sequential action of chaperonin and chaperone machinery for folding and assembly, pointing toward a complex biogenesis pathway in both prokaryotic and eukaryotic organisms. First, newly synthesized Rubisco large subunit (RbcL) is captured by chaperonin system to allow the RbcL fold to correct conformation. Second, the assembly chaperone RbcX interacts predominantly with C-terminal of RbcL and stabilize dimeric RbcL. Finally, nuclear translated rubisco small subunit (RbcS) replaced RbcX to form the haloenzyme. But active enkaryotic Rubisco could not generated by same procedure, pointing to the more complicated biogenesis pathway. Our research goals include identification of factors involved in the biogenesis of eukaryotic Rubisco and its regulation in algae and plants, and reconstitution of eukaryotic Rubisco with chaperones in vitro. Now we analyzed that chaperonin system in chloroplast is largely different from enkaryotic ones and we are trying to identify other cofactors in eukaryotic cells.
Regulation of other carbon assimilation enzymes
Our other specific aim is to analyse the enzymes involved in the Calvin cycle from common wheat. Here the main goal is to engineer highly active enzymes and then assessing the effect on growth after transfer of engineered genes into plants. The improved enzyme will be engineered by gene shuffling after comparing the enzyme activities among copies, varieties and species or by site-directed mutagenesis after solving their crystal structures.

Conferences

   
Invited Lectures

(1) 10th Congress and 20th Symposium of algal branch, 2019, Regulation of chloroplast protein homeostasis.

(2) 9th Asia and Oceania Conference on Photobiology, 2019, Structure and Function of Chloroplast Chaperonin System of Chlamydomonas.

(3) Bilateral Symposium on wheat genome and molecular breeding between China and Germany, 2019, Structure and function of key protein of wheat starch content.

(4) The first academic symposium on Chlamydomonas molecular cells in China, 2019,  Chloroplast protein homeostasis regulated by chaperones and proteases.

(5) National Symposium on Photosynthesis, 2019, Biogenesis and Regulation of Rubisco.

(6) Cryo-EM structure of the chloroplast chaperonins, 2018, 1st Asia-Oceania International Congress on Photosynthesis.

(7) Youth Forum on "frontier and cross field of life science", 2018, Biosynthesis of Rubisco.

(8) 18th International Conference on the Cell and Molecular Biology of Chlamydomonas, 2018, Structure and Function of Chloroplast Chaperonin System of Chlamydomonas.

(9) National Congress of Plant Biology, 2016, The Crystal Structure of Chloroplast CPN60 from Chlamydomonas reinhardtii and Functional Partition of Different Subunits.

(10) 2nd Female Scientists Symposiumof Plant Biology, 2015, The structure and function of chloroplast Cpn60.

(11) 3rd International Conference on Plant Metabolism, 2014, The composition and structure of chloroplast chaperonin.

(12) National Congress of Plant Biology, 2013, Three chloroplast chaperonin protomers with various roles constitute authentic oligomers in Chlamydomonas reinhardtii.


Students

已指导学生

国鹏  博士研究生  071009-细胞生物学  

柏翠翠  博士研究生  071009-细胞生物学  

张世佳  博士研究生  071009-细胞生物学  

马远征  博士研究生  071007-遗传学  

贾立加  博士研究生  071007-遗传学  

江姗  博士研究生  071007-遗传学  

胡丽霞  博士研究生  071011-生物物理学  

赵骞  博士研究生  071007-遗传学  

现指导学生

宋辉  博士研究生  071011-生物物理学  

张慧君  博士研究生  0710J3-生物信息学  

王宁  博士研究生  071011-生物物理学  

邵瑞琪  博士研究生  0710J3-生物信息学  

安向向  博士研究生  0710J3-生物信息学  

塔娜  博士研究生  071011-生物物理学  

王冉  博士研究生  071011-生物物理学  

黄金兰  博士研究生  0710J3-生物信息学  

刘亚男  博士研究生  071011-生物物理学  

Honors & Distinctions

   
Honors and Academic Awards
The Fifth Rebeiz Foundation for Basic Research (RFFBR) Paper Award for 2010