Dear Colleagues,

Please see the following job posting for a postdoctoral fellowship at Purdue 
University.

Thanks
Chitta

Postdoctoral Associate – Atypical ubiquitination in host-pathogen interactions
About Das Lab ( https://www.chem.purdue.edu/das/ ):The broad research interest 
of the group centers around protein ubiquitination and its relationship with 
bacterial and viral pathogens. Specifically, understanding mechanism of action 
of ubiquitin ligases, deubiquitinases (DUBs) and ubiquitin modifying enzymes of 
both prokaryotic and eukaryotic origin. The fact that viruses and bacteria 
manipulate our ubiquitination pathways has been known for at least two decades, 
with several well characterized examples of pathogens using enzymes or 
substrate adaptors to co-opt our ubiquitination pathways. We have recently 
identified atypical modes of ubiquitination and deubiquitination catalyzed by 
bacterial effectors. We wish to unravel mechanism of action of these enzymes, 
including regulation of catalytic activity and substrate selection using 
biochemical, biophysical, molecular biological techniques and integrative 
structural approaches such as cryo-EM, crystallography, cross-linking mass 
spectrometry, and proteomics to answer fundamental questions on how pathogens 
manipulate various ubiquitin-related host signalling pathways. Example 
publications related to this work can be found here:
Kenny S, Iyer S, Gabel C, Tegenfeldt M. Demarco A, Hall MC, Chang L, Davisson 
V, Vande Pol S, Das C. Structure of E6AP in complex with HPV16-E6 and p53 
reveals a novel ordered domain important for E3 ligase activation. Structure.  
2025 Mar 6;33(3):504-516.e4.  doi: 10.1016/j.str.2024.12.013. Epub 2025 Jan 15.
Zhang Z, Fu J, Rack J, Li C, Voorneveld J, Filippov D, Ahel I, Luo ZQ, Das C. 
Legionella metaeffector MavL reverses ubiquitin ADP-ribosylation via a 
conserved arginine-specific macrodomain (2024) Nature Communications 15 (2452): 
https://doi.org/10.1038/s41467-024-46649-2.
Zhang Z, Patel R, Zhao-Qing Luo, Das C. Cryo-EM Detection of AMPylated 
Histidine Implies Covalent Catalysis in AMPylation Mediated by a Bacterial 
Effector. Journal of Molecular Biology 2025 Feb 1;437(3):168917.doi: 
10.1016/j.jmb.2024.168917.
Resources: Das lab is well equipped for carrying out all molecular biology and 
biochemical experiments. In addition to the resources in-house, the Das group 
members also have access to campus-wide facilities such as proteomics facility, 
cryo-EM facility (Titan Krios G4 microscopes), Markey Center for Structural 
Biology (which offers access to crystal growth facilities, 
temperature-controlled crystallization chambers and the Mosquito X1 
Crystallization Robot), Bindley Biophysics Core and Purdue University of Drug 
Discovery.
Application Process: We are seeking a highly motivated recent Ph.D. graduate 
with a strong background in molecular biology and biochemistry. Interested 
candidates should submit a CV, a cover letter detailing research interests and 
accomplishments, and contact information for three references to 
[email protected]<mailto:[email protected]>. We encourage candidates from diverse 
backgrounds to apply. Purdue University is an equal opportunity employer.



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