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Junjie Zhang

Zhang, Junjie
Junjie Zhang
Assistant Professor
Office:
ILSB 2157A
Email:
Phone:
979-458-9882
http://cryoem.tamu.edu
Undergraduate Education
B.S. (2004) Physics, Fudan University
Graduate Education
Ph.D. (2009) Structural Biology, Baylor College of Medicine
Postdoc. Structural Biology, Stanford University (2009-13)
Joined Texas A&M in January 1, 2014

Cryo-EM of Cellular Machineries

The living cell contains a collection of molecular machines to grow and function. These machines include the ribosomes, the chaperons, the proteasomes and other enzymes. Malfunction of these machines, if occurred in human, are related to many diseases. Understanding their three-dimensional (3D) structures is essential to understand how these machines work in the cell and eventually to treat those related diseases.

Here we use an experimental technique called cryo-electron microscopy (cryo-EM) to image these cellular machines in their native environment at liquid nitrogen temperatures. We then use image processing and graphics techniques to visualize their 3D structures, answering the questions such as how they assemble and how they interact with each other.

In addition, we develop computational modeling tools to interpret and animate these obtained 3D structures to further describe their movements and dynamics.

Research Publications

  1. Zhang, J, Tan, P, Guo, L, Gong, J, Ma, J, Li, J et al.. p53-dependent autophagic degradation of TET2 modulates cancer therapeutic resistance. Oncogene. 2018; :.
    doi: 10.1038/s41388-018-0524-5. PubMed PMID:30390073. .

  2. Klein, BJ, Vann, KR, Andrews, FH, Wang, WW, Zhang, J, Zhang, Y et al.. Structural insights into the π-π-π stacking mechanism and DNA-binding activity of the YEATS domain. Nat Commun. 2018;9 (1):4574.
    doi: 10.1038/s41467-018-07072-6. PubMed PMID:30385749. PubMed Central PMC6212594.

  3. Brock, DJ, Kustigian, L, Jiang, M, Graham, K, Wang, TY, Erazo-Oliveras, A et al.. Efficient cell delivery mediated by lipid-specific endosomal escape of supercharged branched peptides. Traffic. 2018;19 (6):421-435.
    doi: 10.1111/tra.12566. PubMed PMID:29582528. PubMed Central PMC5948172.

  4. Cui, Z, Gorzelnik, KV, Chang, JY, Langlais, C, Jakana, J, Young, R et al.. Structures of Qβ virions, virus-like particles, and the Qβ-MurA complex reveal internal coat proteins and the mechanism of host lysis. Proc. Natl. Acad. Sci. U.S.A. 2017;114 (44):11697-11702.
    doi: 10.1073/pnas.1707102114. PubMed PMID:29078304. PubMed Central PMC5676892.

  5. Yang, K, Chang, JY, Cui, Z, Li, X, Meng, R, Duan, L et al.. Structural insights into species-specific features of the ribosome from the human pathogen Mycobacterium tuberculosis. Nucleic Acids Res. 2017;45 (18):10884-10894.
    doi: 10.1093/nar/gkx785. PubMed PMID:28977617. PubMed Central PMC5737476.

  6. Weaver, J, Jiang, M, Roth, A, Puchalla, J, Zhang, J, Rye, HS et al.. GroEL actively stimulates folding of the endogenous substrate protein PepQ. Nat Commun. 2017;8 :15934.
    doi: 10.1038/ncomms15934. PubMed PMID:28665408. PubMed Central PMC5497066.

  7. Gorzelnik, KV, Cui, Z, Reed, CA, Jakana, J, Young, R, Zhang, J et al.. Asymmetric cryo-EM structure of the canonical Allolevivirus Qβ reveals a single maturation protein and the genomic ssRNA in situ. Proc. Natl. Acad. Sci. U.S.A. 2016;113 (41):11519-11524.
    doi: 10.1073/pnas.1609482113. PubMed PMID:27671640. PubMed Central PMC5068298.

  8. Yang, S, Jiang, M, Grabowska, MM, Li, J, Connelly, ZM, Zhang, J et al.. Androgen receptor differentially regulates the proliferation of prostatic epithelial cells in vitro and in vivo. Oncotarget. 2016;7 (43):70404-70419.
    doi: 10.18632/oncotarget.11879. PubMed PMID:27611945. PubMed Central PMC5342561.

  9. Lee, JR, Xie, X, Yang, K, Zhang, J, Lee, SY, Shippen, DE et al.. Dynamic Interactions of Arabidopsis TEN1: Stabilizing Telomeres in Response to Heat Stress. Plant Cell. 2016;28 (9):2212-2224.
    doi: 10.1105/tpc.16.00408. PubMed PMID:27609839. PubMed Central PMC5059806.

  10. Yang, K, Ren, Z, Raushel, FM, Zhang, J. Structures of the Carbon-Phosphorus Lyase Complex Reveal the Binding Mode of the NBD-like PhnK. Structure. 2016;24 (1):37-42.
    doi: 10.1016/j.str.2015.11.009. PubMed PMID:26724995. PubMed Central PMC4706772.

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