College Introduction

The Institute for Advanced Study (IAS) has been established at Shenzhen University to provide both undergraduate and postgraduate education, focusing on interdisciplinary teaching and research. As a special platform at Shenzhen University, IAS seeks to

People

​Jianfeng Yu

Position,Associate Researcher

E-mail:  j.yu@szu.edu.cn

Address:Office 201-2, L4 Building, South Campus, Shenzhen University

 

Education:

2014,Imperial College London,Life Sciences,PhD.

2007,Imperial College London,Life Sciences,Master

2006,University of Nottingham,Life Sciences,Bachler

 

Work experience:

2014.01—2019.12,Imperial College London,Post-Doctoral Research Associate

2009.06—2013.12,Imperial College London, Research Assistant

 

Research Interests:

The molecular basis of photosynthesis and algal biotechnology.

1. The light-reaction of photosynthesis and protein evolution

Photosynthesis is one of the fundamental reactions that supporting the Earth biosphere. Through the billion-years of evolution, photosynthesis harnessed the solar energy and fixed the atmospheric carbon dioxide into organic matters; while oxygen, the byproduct of photosynthesis, enabled the life dependent on aerobic respiration to roam on the Earth. On the flipside, due to the impact of photosynthesis, the level of atmospheric carbon dioxide had dropped from >20% to <0.1%. Due to the oxygen inhibition, the efficiency of photosynthesis has reduced comparing to that of the prehistoric time. The productivity of photosynthesis is a key limiting factor for the net organic matter on the Earth, hence the “planetary boundary” for the Earth biosphere is dependent on the efficiency and scale of photosynthesis. Therefore, understanding the molecular basis of photosynthesis; investigating its potential for further improvement via protein engineering is what raised my academic interests. Through the previous studies, I and co-workers have conducted a great range of molecular and biochemical research on the Photosystem II complex, which elucidated the impact of some assembly proteins to the efficiency of photosynthesis. I and co-workers have also conducted structural analysis on many proteins and unveiled many molecular interactions and the regulatory processes of photosystem II. To date, my work is mainly on the evolutionary aspect of photosynthesis, I analyze the divergence of photosynthetic genes from microalgae of diverse environment. The analysis is likely to build the functional link between specific genetic variations and their functions. Such work could aid the artificial design of photosynthetic systems, and possibly improve the efficiency of photosynthesis in the future.

2. Algal biotechnology

Microalgae are unicellular photosynthetic organisms. Due to the fast growth rate, greater protein stability etc. some microalgae have been widely used as research subjects for photosynthesis study. Despite microalgae contain large number of desirable compounds, such as antioxidants and pigments, the development of industrial algal biorefinery remains at an early stage. The major challenge is that due to the low cell density in the culture, the cell harvesting procedure became energy intensive, which substantially reduced the profit margin of algal-based products. Therefore, how to obtain dense algal culture on industrial-scale is the key barrier to break for the algal biotech industry. I am investigating the high-density cultivation procedures using the dialysis principles, and I am tuning the cultivation parameters to build a low-cost, autotrophic cultivation system.

 

Publications:

1. Yu, J.*, Knoppová, J., Michoux, F., Bialek, W., Cota, E., Shukla, M. K., Strašková, A., Pascual Aznar, G., Sobotka, R., Komenda, J., Murray, J. W., and Nixon, P. J.* (2018) Ycf48 involved in the biogenesis of the oxygen-evolving photosystem II complex is a seven-bladed beta-propeller protein. Proc. Natl. Acad. Sci. 115, E7824–E7833

2. Bec̆ková, M., Yu, J., Krynická, V., Kozlo, A., Shao, S., Koník, P., Komenda, J., Murray, J. W., and Nixon, P. J. (2017) Structure of Psb29/Thf1 and its association with the FtsH protease complex involved in photosystem II repair in cyanobacteria. Philos. Trans. R. Soc. B Biol. Sci. 372, 20160394

3. Bečková, M., Gardian, Z., Yu, J., Konik, P., Nixon, P. J., Komenda, J., Koník, P., Nixon, P. J., and Komenda, J. (2017) Association of Psb28 and Psb27 proteins with PSII-PSI supercomplexes upon exposure of Synechocystis sp. PCC 6803 to high light. Mol. Plant. 10, 62–72

4. Knoppová, J., Yu, J., Konik, P., Nixon, P. J., and Komenda, J. (2016) CyanoP is involved in the early steps of photosystem II assembly in the cyanobacterium Synechocystis sp. PCC 6803. Plant Cell Physiol. 57, 1921–1931

5. Sacharz, J., Bryan, S. J., Yu, J., Burroughs, N. J., Spence, E. M., Nixon, P. J., and Mullineaux, C. W. (2015) Sub-cellular location of FtsH proteases in the cyanobacterium Synechocystis sp: PCC 6803 suggests localised PSII repair zones in the thylakoid membranes. Mol. Microbiol. 96, 448–462

6. Bryan, S. J., Burroughs, N. J., Shevela, D., Yu, J., Rupprecht, E., Liu, L. N., Mastroianni, G., Xue, Q., Llorente-Garcia, I., Leake, M. C., Eichacker, L. A., Schneider, D., Nixon, P. J., and Mullineaux, C. W. (2014) Localisation and interactions of the Vipp1 protein in cyanobacteria. Mol. Microbiol. 94, 1179–1195

7. Krynická, V., Tichý, M., Krafl, J., Yu, J., Kaňa, R., Boehm, M., Nixon, P. J., and Komenda, J. (2014) Two essential FtsH proteases control the level of the Fur repressor during iron deficiency in the cyanobacterium Synechocystis sp. PCC 6803. Mol. Microbiol. 94, 609–624

8. Shinopoulos, K. E., Yu, J., Nixon, P. J., and Brudvig, G. W. (2014) Using site-directed mutagenesis to probe the role of the D2 carotenoid in the secondary electron-transfer pathway of photosystem II. Photosynth. Res. 120, 141–152

9. Knoppová, J., Sobotka, R., Tichy, M., Yu, J., Konik, P., Halada, P., Nixon, P. J., Komenda, J., (2014) Discovery of a chlorophyll binding protein complex involved in the early steps of photosystem II assembly in Synechocystis. Plant Cell. 26, 1200–1212

10. Burroughs, N. J., Boehm, M., Eckert, C., Mastroianni, G., Spence, E. M., Yu, J., Nixon, P. J., Appel, J., Mullineaux, C. W., and Bryan, S. J. (2014) Solar powered biohydrogen production requires specific localization of the hydrogenase. Energy Environ. Sci. 7, 3791–3800

11. Suzuki, H., Yu, J., Kobayashi, T., Nakanishi, H., Nixon, P. J., and Noguchi, T. (2013) Functional roles of D2-Lys317 and the interacting chloride ion in the water oxidation reaction of photosystem II as revealed by fourier transform infrared analysis. Biochemistry. 52, 4748–4757

12. Boehm, M., Yu, J., Reisinger, V., Beckova, M., Eichacker, L. A., Schlodder, E., Komenda, J., and Nixon, P. J. (2012) Subunit composition of CP43-less photosystem II complexes of Synechocystis sp. PCC 6803: implications for the assembly and repair of photosystem II. Philos. Trans. R. Soc. B Biol. Sci. 367, 3444–3454

13. Boehm, M., Yu, J., Krynicka, V., Barker, M., Tichy, M., Komenda, J., Nixon, P. J., and Nield, J. (2012) Subunit organization of a Synechocystis hetero-oligomeric thylakoid FtsH complex involved in photosystem II repair. Plant Cell. 24, 3669–3683

14. Liu, L. N., Bryan, S. J., Huang, F., Yu, J., Nixon, P. J., Rich, P. R., and Mullineaux, C. W. (2012) Control of electron transport routes through redox-regulated redistribution of respiratory complexes. Proc. Natl. Acad. Sci. 109, 11431–11436

15. Komenda, J., Knoppova, J., Kopecna, J., Sobotka, R., Halada, P., Yu, J., Nickelsen, J., Boehm, M., and Nixon, P. J. (2012) The Psb27 assembly factor binds to the CP43 complex of photosystem II in the cyanobacterium Synechocystis sp. PCC 6803. Plant Physiol. 158, 476–486

16. Boehm, M., Romero, E., Reisinger, V., Yu, J., Komenda, J., Eichacker, L. A., Dekker, J. P., and Nixon, P. J. (2011) Investigating the early stages of photosystem II assembly in Synechocystis sp. PCC 6803: isolation of CP47 and CP43 complexes. J. Biol. Chem. 286, 14812–14819

17. Nixon, P. J., Michoux, F., Yu, J., Boehm, M., and Komenda, J. (2010) Recent advances in understanding the assembly and repair of photosystem II. Ann. Bot. 106, 1–16